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The MCP proteins are members of the CC chemokine family that signal through CCR2 and, with the exception of MCP-1, other  CCR receptors. The MCP proteins chemoattract and activate monocytes, activated Tcells, basophils, NK cells, and immature dendritic cells. The MCP family cross-reacts across species. Recombinant Human MCP-3 is a 9.0 kDa protein containing 76 amino acid residues including the four highly conserved cysteine residues present in the CC chemokines. Product Properties Synonyms NC28, Small-inducible cytokine A7 Accession P80098 Source E.coli-derived Human CCL7 protein,Gln24-Leu99. GeneID 6354 Tag None Molecular Weight Approximately 9.0 kDa. AA Sequence QPVGINTSTT CCYRFINKKI PKQRLESYRR TTSSHCPREA VIFKTKLDKE ICADPTQKWV QDFMKHLDKK TQTPKL Endotoxin < 1 EU/μg of protein as determined by LAL method Purity ＞ 97%, as determined by SDS-PAGE and HPLC analysis. Biological Activity Fully biologically active when compared to standard. The biologically active determined by a chemotaxis bioassay using human monocytes is in a concentration range of 10-100 ng/mL. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM PB, pH 7.4, 150 mM NaCl. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Human CCL13 is belonging to the CC chemokine family and is encoded by the gene CCL13. CCL13 (MCP-4) shares 56-61 % sequence identity with MCP-1 (CCL2) and MCP-3 (CCL7) and is 60 % identical to Eotaxin (CCL11). CCL13 was a potent chemoattractant for monocytes and eosinophils and stimulated histamine release from basophils. CCL13 can induce a calcium flux in HEK-293 cells transfected with the receptor CCR2B and CCR3. That shows the function receptors of CCL3 are CCR2B and CCR3.   Product Properties   Synonyms CCL13 Protein, Human; CKb10 Protein, Human; MCP-4 Protein, Human; MCP4 Protein, Human; NCC-1 Protein, Human; NCC1 Protein, Human; SCYA13 Protein, Human; SCYL1 Protein, Huma Accession Q99616 GeneID 6357 Source E.coli-derived human Monocyte Chemotactic Protein-4, Gln24-Thr98 Molecular Weight Approximately 8.6 kDa. AA Sequence QPDALNVPST CCFTFSSKKI SLQRLKSYVI TTSRCPQKAV IFRTKLGKEI CADPKEKWVQ NYMKHLGRKA HTLKT Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 96 % by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The biological activity determined by a chemotaxis bioassay using human monocytes is in a concentration of 10-100 ng/ml. Endotoxin Less than 1 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM PBS, pH 7.4, 130 mM NaCl. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom.Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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CXCL9, a member of the alpha subfamily of chemokines that lack the ELR domain, was initially identified as a lymphokine-activated gene in mouse macrophages. Human CXCL9 was subsequently cloned using mouse MIG cDNA as a probe. The human CXCL9 cDNA encodes a 125 amino acid residue precursor protein with a 22 amino acid residue signal peptide that is cleaved to yield a 103 amino acid residue mature protein.The carboxy-terminal residues of CXCL9 are prone to proteolytic cleavage resulting in size heterogeneity of natural and recombinant CXCL9.The CXCL9 gene is induced in macrophages and in primary glial cells of the central nervous system specifically in response to IFN-gamma. CXCL9 has been shown to be a chemoattractant for activated T-lymphocytes and TIL. And it elicits their chemotactic functions by interacting with the chemokine receptor CXCR3.   Product Properties   Synonyms Monokine-like Protein  Accession Q07325 GeneID 4283 Source E.coli-derived Human MIG/CXCL9, Thr23-Thr125. Molecular Weight Approximately 11.7 kDa. AA Sequence TPVVRKGRCS CISTNQGTIH LQSLKDLKQF APSPSCEKIE IIATLKNGVQ TCLNPDSADV  KELIKKWEKQ VSQKKKQKNG KKHQKKKVLK VRKSQRSRQK KTT Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity The biological activity determined by a chemotaxis bioassay using human peripheral blood T-lymphocytes is in a concentration range of 10-100 ng/mL. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM PB, pH 7.4, 50 mM NaCl. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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Myoglobin is a member of the globin superfamily and is predominantly expressed in skeletal and cardiac muscles. It forms a monomeric globular haemoprotein that is primarily responsible for the storage and facilitated transfer of oxygen from the cell membrane to the mitochondria. This protein also plays a role in regulating physiological levels of nitric oxide.   Product Properties   Accession P02144 GeneID 4151 Source E.coli-derived Human Myoglobin, Gly2-Gly154. Molecular Weight Approximately 17.1 kDa. AA Sequence GLSDGEWQLV LNVWGKVEAD IPGHGQEVLI RLFKGHPETL EKFDKFKHLK SEDEMKASED LKKHGATVLT ALGGILKKKG HHEAEIKPLA QSHATKHKIP VKYLEFISEC IIQVLQSKHP GDFGADAQGA MNKALELFRK DMASNYKELG FQG Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95% by SDS-PAGE. Biological Activity Data not available. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Supplied as a 0.2 μm filtered solution in 25 mM Tris-HCl, pH 8.0, with 50 % glycerol. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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NOV is a member of the CCN family of secreted, cysteine-rich regulatory proteins. The full-length NOV protein contains four structural domains that confer distinct, and sometimes opposing, biological activities. Elevated expression of NOV is associated with certain tumors, including Wilm’s tumor and most nephroblastomas. However, in other tumor types and certain cancer cell lines, increased tumorigenicity and proliferation is correlated with decreased NOV expression. Additionally, NOV induces cell adhesion and cell migration by signaling through specific cell-surface integrins, and by binding to heparin sulfate proteoglycans and to fibulin 1C. NOV has also been reported to exert proangiogenic activities.   Product Properties   Synonyms Nephroblastoma Overexpressed gene, CCN3, IGFBP9, NovH Accession P48745 GeneID 4856 Source E.coli-derived Human NOVprotein,Gln28-Met357. Molecular Weight Approximately 36.2 kDa. AA Sequence MQVAATQRCP PQCPGRCPAT PPTCAPGVRA VLDGCSCCLV CARQRGESCS DLEPCDESSG LYCDRSADPS NQTGICTAVE GDNCVFDGVI YRSGEKFQPS CKFQCTCRDG QIGCVPRCQL DVLLPEPNCP APRKVEVPGE CCEKWICGPD EEDSLGGLTL AAYRPEATLG VEVSDSSVNC IEQTTEWTAC SKSCGMGFST RVTNRNRQCE MLKQTRLCMV RPCEQEPEQP TDKKGKKCLR TKKSLKAIHL QFKNCTSLHT YKPRFCGVCS DGRCCTPHNT KTIQAEFQCS PGQIVKKPVM VIGTCTCHTN CPKNNEAFLQ ELELKTTRGK M Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95 % by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 1.0 μg/mL, corresponding to a specific activity of > 1000 IU/mg. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM Tris-HCl, pH 8.6, 150 mM NaCl. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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Nesfatin-1 (NEFA Encoded Satiety and Fat-influencing protein 1) is a secreted, 10 kDa peptide derived from the translation product of the NUCB2 gene. Human Nesfatin-1 shares 85% aa identity with mouse Nesfatin-1. It is a naturally occurring protein and originally identified as a hypothalamic neuropeptide. Additionally, Nesfatin can be found in other areas of brain, and in pancreatic isletsβ-cells, gastric endocrine cells and adipocytes. It is responsible for regulating appetite and production of body fat. Excess nesfatin-1 in the brain leads to a loss of appetite, less frequent hunger, a 'sense of fullness', and a drop in body fat and weight. A lack of nesfatin-1 in the brain leads to an increase of appetite, more frequent episodes of hunger, an increase of body fat and weight, and the inability to 'feel full'.   Product Properties   Synonyms Nucleobindin 2 Accession P80303 GeneID 4925 Source E.coli-derived human Nesfatin-1 protein, Val25-Leu106. Molecular Weight Approximately 9.6 kDa. AA Sequence VPIDIDKTKV QNIHPVESAK IEPPDTGLYY DEYLKQVIDV LETDKHFREK LQKADIEEIK SGRLSKELDL VSHHVRTKLD EL Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >95% by SDS-PAGE and HPLC analyses. Biological Activity The biological activity is tested by in vivo assay using healthy wild type male mice (C57BL/6J). Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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Neuritin also known as NRN1 and CPG15 is a neurotrophic factor, which is expressed in response to induction of neuronal activity by NGF, BDNF, NT3 and other neural stimulators. It promotes neurite outgrowth and especially branching of neuritic processes in primary hippocampal and cortical cells. Recombinant Human Neuritin is a covalently disulfide-linked homodimer, consisting of two 9.7 kDa polypeptide monomers, each containing 88 amino acid residues. It shares 99 % and 97 % a.a. sequence identity with murine and rat neuritin, respectively.   Product Properties   Synonyms NRN1 Accession Q9NPD7 GeneID 51299 Source E.coli-derived Human Neuritin, Ala28-Asn115. Molecular Weight Approximately 19.4 kDa. AA Sequence AGKCDAVFKG FSDCLLKLGD SMANYPQGLD DKTNIKTVCT YWEDFHSCTV TALTDCQEGA KDMWDKLRKE SKNLNIQGSL FELCGSGN Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97 % by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by by a cell proliferation assay using rat C6 cells is less than 25 ng/mL, corresponding to a specific activity of > 4.0 × 10^4 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20 ℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only！

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Neuron specific enolase (NSE), also known as ENO2 or gamma-enolase, is a dimeric, Mg 2+ -dependent enzyme that catalyzes the dehydration of 2-phospho-D glycate (PGA) to phosphoenolpyruvate (PEP) in the glycolytic pathway and catalyzes the reverse reaction in gluconeogenesis. NSE is a 47.1 kDa member of the Enolase family of enzymes. It is expressed in developing neurons and glia, is known to catalyze the generation of phosphoenolpyruvate, and is suggested to possess neurotrophic activity for neurons, likely through an extracellular mechanism. Human Neuron-specific Enolase is 433 amino acids (aa) in length. The enzymatic site spans most of the length of the molecule. Neuron-specific Enolase exists as both a noncovalently-linked homodimer, or heterodimer with alpha-enolase. Full-length human Enolase 2 shares 99% aa identity with both murine and canine Enolase 2. It shares 83% aa identity with human enolases 1 and 3.   Product Properties   Synonyms 2-phospho-D-glycerate hydrolyase, ENO2, Enolase 2, gamma-Enolase, Neural enolase, neurone-specific enolase, Neuron-specific enolase, NSE Accession P09104.3 GeneID 2026 Source E.coli-derived human NSE protein, Ser2-Leu434. Molecular Weight Approximately 47.1 kDa. AA Sequence SIEKIWAREI LDSRGNPTVE VDLYTAKGLF RAAVPSGAST GIYEALELRD GDKQRYLGKG VLKAVDHINS TIAPALISSG LSVVEQEKLD NLMLELDGTE NKSKFGANAI LGVSLAVCKA GAAERELPLY RHIAQLAGNS DLILPVPAFN VINGGSHAGN KLAMQEFMIL PVGAESFRDA MRLGAEVYHT LKGVIKDKYG KDATNVGDEG GFAPNILENS EALELVKEAI DKAGYTEKIV IGMDVAASEF YRDGKYDLDF KSPTDPSRYI TGDQLGALYQ DFVRDYPVVS IEDPFDQDDW AAWSKFTANV GIQIVGDDLT VTNPKRIERA VEEKACNCLL LKVNQIGSVT EAIQACKLAQ ENGWGVMVSH RSGETEDTFI ADLVVGLCTG QIKTGAPCRS ERLAKYNQLM RIEEELGDEA RFAGHNFRNP SVL Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >96% by SDS-PAGE and HPLC analyses. Biological Activity Testing in progress. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4, with 5% Trehalose. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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Neurotrophin-3 (NT-3) is a member of the NGF family of neurotrophic factors (also named neurotrophins) that are required for the differentiation and survival of specific neuronal subpopulations in both the central as well as the peripheral nervous systems. The NT-3 cDNA encodes a 257 amino acid residue precursor protein with a signal peptide and a proprotein that are cleaved to yield the 119 amino acid residue mature NT-3. The amino acid sequence of mature NT-3 is identical in human, mouse and rat. The neurotrophin family is comprised of at least four proteins including NGF, BDNF, NT-3, and NT-4/5. These secreted cytokines are synthesized as prepropeptides that are proteolytically processed to generate the mature proteins.   Product Properties   Synonyms HDNF ; NGF-2 ; NGF2 ; NT-3; NT3 Accession P20783-1 Source E. coli-derived human NT-3 protein, Tyr139-Thr257 Molecular Weight Approximately 13.8 kDa. AA Sequence YA EHKSHRGEYS VCDSESLWVT DKSSAIDIRG HQVTVLGEIK TGNSPVKQYF YETRCKEARP VKNGCRGIDD KHWNSQCKTS QTYVRALTSE NNKLVGWRWI RIDTSCVCAL SRKIGRT Tag None Purity > 90% by SDS-PAGE. concentration 0.46 mg/mL Biological Activity Measured by its binding ability in a functional ELISA. Immobilized human NT3 at 2 μg/mL (100 μL/well) can bind human TrkB-Fch. The EC50 of human TrkB-Fch is 120-350 ng/mL. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 5.2.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Neurturin is a member of the GDNF family of ligands, which include glial cell-derived neurotrophic factor (GDNF), Neurturin, Persephin, and Artemin. GDNF family proteins are distant members of the Transforming Growth Factor beta (TGF-beta ) superfamily. Similarly to other TGF-beta family proteins, Neurturin is synthesized as a precursor protein that is cleaved at the dibasic cleavage site (RXXR) to release the carboxy-terminal domain. The carboxy-terminal domain of Neurturin contains the characteristic seven conserved cysteine residues necessary for the formation of the cysteine-knot and the single interchain disulfide bond. Biologically active human Neurturin is a disulfide-linked homodimer of the carboxy-terminal 102 amino acid residues. Mature human Neurturin shares approximately 92% amino acid sequence identity with mouse Neurturin. Mature Neurturin also shares about 40% similarities with the other three members of the GDNF family ligands. Unlike other members of TGF-beta family, bioactivities of all GDNF family ligands are mediated through a unique multicomponent receptor complex composed of high affinity ligand binding component (GFR alpha -1-GFR alpha -4) and a common signaling component (cRET receptor tyrosine kinase). Each member of the GDNF family ligands has its preferred binding protein. Neurturin preferentially binds to GFR alpha -2 but can also bind GFR alpha -1 at higher concentrations. Neurturin had been shown to promote the survival of a variety of neurons including sympathetic, sensory, and central nervous system neurons. Neurturin is expressed in both neuronal and non-neuronal tissues.   Product Properties   Synonyms NRTN; NTN Accession Q99748 GeneID 4902 Source E.coli-derived Human Neurturin, Ala96-Val197. Molecular Weight Approximately 23.4 kDa. AA Sequence ARLGARPCGL RELEVRVSEL GLGYASDETV LFRYCAGACE AAARVYDLGL RRLRQRRRLR RERVRAQPCC RPTAYEDEVS FLDAHSRYHT VHELSARECA CV Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 96% by SDS-PAGE and HPLC analyses. Biological Activity The biologically active as determined by its binding ability in a functional ELISA. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 30 mM Citrate Sodium, pH 4.2, 400 mM NaCl, with 0.02% Tween-20. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water to a concentration of 0.5 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Neutrophil Activating Peptide 2 (NAP-2), also known as Chemokine (C-X-C motif) ligand 7 (CXCL7) and Pro-platelet basic protein (PPBP), is a member of the CXC chemokines. NAP-2 is found in the alpha-granules of human platelets. Nap-2 / PPBP / CXCL7 is released in large amounts from platelets following their activation. Similar to other ELR domain containing CXC chemokines such as IL-8 and the GRO proteins, NAP-2 has been shown to bind CXCR2 and to chemoattract and activate neutrophils. Nap-2 / PPBP / CXCL7 has been shown to stimulate various cellular processes including DNA synthesis, mitosis, glycolysis, intracellular cAMP accumulation, prostaglandin E2 secretion, and synthesis of hyaluronic acid and sulfated glycosaminoglycan. It also stimulates the formation and secretion of plasminogen activator by synovial cells. Nap-2 is a ligand for CXCR1 and CXCR2, and Nap-2, Nap-2 (73), Nap-2 (74), Nap-2 (1-66), and most potent Nap-2 (1-63).   Product Properties   Synonyms CXCL7, LDGF, MDGF, Small-inducible cytokine B7 Accession P02775 GeneID 5473 Source E.coli-derived Human NAP-2/CXCL7, Ala59-Asp128. Molecular Weight Approximately 7.6 kDa. AA Sequence AELRCMCIKT TSGIHPKNIQ SLEVIGKGTH CNQVEVIATL KDGRKICLDP DAPRIKKIVQ KKLAGDESAD Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity The biological activity determined by a chemotaxis bioassay using human peripheral blood neutrophils is in a concentration range of 1.0-10.0 ng/mL. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM PB, pH 7.4, 50 mM NaCl. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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Noggin is a bone morphogenetic protein (BMP) antagonist expressed in Spemann's organizer. It inhibits TGF-β family ligands and preventing them from binding to their corresponding receptors.   Product Properties   Synonyms NOG, SYM1, symphalangism 1 (proximal), synostoses (multiple) syndrome 1, SYNS1 Uniprot No. Q13253 Source HEK293 cells -derived human Noggin protein, Gln28-Cys232, with a His tag at the C-terminal Molecular Weight The protein migrates as 30 KDa under reducing (R) condition (SDS-PAGE) . Activity Measured by its ability to bind BMP2 with Elisa method . Optimal concentrations should be determined by each laboratory for each application Purity > 95% as determined by SDS-PAGE. Endotoxin <1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered solution in PBS. Reconstitution It is recommended that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute the lyophilized powder in ddH2O or PBS up to 100 μg/ml.   Storage   The product should be stored at -85~-65℃ for 1 year from date of receipt.   Caution   1.Please operate with lab coats and disposable gloves,for your safety. 2.This product is for research use only.

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Cardiotrophin-like cytokine (CLC), also referred to as novel neurotrophin-1 (NNT-1) or B cell-stimulating factor-3 (BSF-3), is a new member of the IL-6 family of structurally related cytokines that includes IL-6, CNTF, LIF, CT-1, IL-11 and OSM. All family members share the receptor subunit gp130 that belong to the type I cytokine receptor superfamily. Ligand binding leads to gp130 homodimerization or heterodimerization (with LIF receptor or OSM receptor beta ), and induces cell signaling and functional activity. For several family members, including CNTF, IL-6, and IL-11, binding of the ligand to a specific receptor alpha subunit (CNTF R alpha, IL-6 R alpha, or IL-11 R alpha ) is required prior to gp130 homo- or hetero-dimerization. CLC cDNA encodes a 225 amino acid (aa) residue precursor protein with a putative 27 aa residue signal peptide that is cleaved to yield the mature protein. Among the IL-6 family, CLC is the most homologous to cardiotrophin, having 29% aa sequence homology. CLC has been shown to bind with the soluble orphan receptor cytokine-like factor-1 (CLF) to form a heterodimeric composite cytokine that subsequently interacts with the membrane- associated CNTF R alpha to initiate gp130-LIF R dimerization and cell signaling. Alternatively, when co-expressed within the cell, CLC can complex with soluble CNTF R alpha to form an alternate composite cytokine that is secreted. This composite cytokine is also capable of initiating gp130-LIF R dimerization. The E. coli-expressed CLC can initiate cell signaling via the tripartite membrane- associated CNTF R alpha and gp130-LIF R. E. coli-expressed CLC does not bind efficiently with soluble CNTF R alpha in solution to initiate cell signaling on cells expressing gp130 and LIF R.   Product Properties   Synonyms Cardiotrophin-like cytokine factor 1, BSF-3 Accession Q9UBD9 GeneID 23529 Source E.coli-derived Human NNT-1/BCSF-3, Leu28-Phe225. Molecular Weight Approximately 22.3 kDa. AA Sequence LNRTGDPGPG PSIQKTYDLT RYLEHQLRSL AGTYLNYLGP PFNEPDFNPP RLGAETLPRA TVDLEVWRSL NDKLRLTQNY EAYSHLLCYL RGLNRQAATA ELRRSLAHFC TSLQGLLGSI AGVMAALGYP LPQPLPGTEP TWTPGPAHSD FLQKMDDFWL LKELQTWLWR SAKDFNRLKK KMQPPAAAVT LHLGAHGF Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 98 % by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using human TF-1 cells is less than 4 ng/mL, corresponding to a specific activity of > 2.5 × 10 5 IU/mg in the presence of human CNTF R alpha. Fully biologically active when compared to standard. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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The neuregulin family of structurally related glycoproteins comprises products from four distinct but related genes, Nrg-1, Nrg-2, Nrg-3, and Nrg-4. All NRG1 isoforms contain an EGF-like domain that is required for their direct binding to the ErbB3 or ErbB4 receptor tyrosine kinases. The ErbB3 or ErbB4 subsequently recruits and heterodimerizes with ErbB2, resulting in tyrosine phosphorylation and NRG1 signaling.   Product Properties   Synonyms ARIA; GGF2; HGL; HRG; HRG1; MST131 Accession Q02297 GeneID 3084 Source E.coli-derived Human NRG1-α, Ser177-Lys241. Molecular Weight Approximately 7.4 kDa. AA Sequence SHLVKCAEKE KTFCVNGGEC FMVKDLSNPS RYLCKCQPGF TGARCTENVP MKVQNQEKAE ELYQK Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97 % by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using serum free human MCF-7 cells is less than 40 ng/mL, corresponding to a specific activity of ＞ 2.5 × 10 4 IU/mg.. Fully biologically active when compared to standard. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered solution in 20 mM PB, pH 6.0, 150 mM NaCl. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. For your safety and health, please wear lab coats and disposable gloves for operation. 2. For research use only!

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The neuregulin family of structurally related glycoproteins comprises products from four distinct but related genes, Nrg-1, Nrg-2, Nrg-3, and Nrg-4. Through alternative splicing or the use of alternative promoters, Nrg-1 has been shown to encode more than 14 soluble or transmembrane proteins. The extracellular domain of the transmembrane NRG1 isoforms can be proteolytically cleaved to release soluble growth factors. All NRG1 isoforms contain an EGF-like domain ( alpha - or beta -splice variant that differ in their C-terminal region) that is required for their direct binding to the ErbB3 or ErbB4 receptor tyrosine kinases. The ErbB3 or ErbB4 subsequently recruits and heterodimerizes with ErbB2, resulting in tyrosine phosphorylation and NRG1 signaling. NRG1 isoforms can be classified into three major subtypes. Type I (Neu Differentiation Factor, NDF; Heregulin, HRG; Acetylcholine Receptor Inducing Activity, ARIA) and type II (Glial Growth Factor, GGF) NRG1s have an immunoglobulin (Ig)-like domain N-terminal to the EGF-like domain. Type I NRG1s differ from type II NRG1s by having a glycosylation-rich domain between the Ig-like and the EGF-like domains. Type III NRG1s (Sensory and Motor neuron-Derived Factor) lacks the Ig-like domain but has a cysteine rich domain (CRD) instead. NRG1 isoforms show distinct spatial and temporal expression patterns. These proteins play important roles during development of both the nervous system and the heart. They have been shown to regulate the selective expression of neurotransmitter receptors in neurons and at the neuromuscular junction, and promote the differentiation and development of Schwann cells from neural crest stem cells. NRG1s have also been shown to be involved in the establishment of the oligodendroglial lineage.   Product Properties   Synonyms ARIA; GGF; GGF2; HGL; HRG; Neuregulin-1 beta 1; NRG1 beta 1 Accession Q02297 GeneID 3084 Source E.coli-derived Human NRG1-β1, Ser177-Glu241. Molecular Weight Approximately 7.5 kDa. AA Sequence SHLVKCAEKE KTFCVNGGEC FMVKDLSNPS RYLCKCPNEF TGDRCQNYVM ASFYKHLGIE FMEAE Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using serum free human MCF-7 cells is less than 0.5 ng/mL, corresponding to a specific activity of > 2.0 × 10 6 IU/mg. Fully biologically active when compared to standard. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered solution in 1 × PBS, pH 7.4, with 5% trehalose. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 to -70 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Neuregulin 1 or NRG1 is one of four proteins in the neuregulin family that act on the EGFR family of receptors. Nrg-1 has been shown to encode more than 14 soluble or transmembrane proteins. The extracellular domain of the transmembrane NRG1 isoforms can be proteolytically cleaved to release soluble growth factors. All NRG1 isoforms contain an EGF-like domain ( alpha - or beta -splice variant that differ in their C-terminal region) that is required for their direct binding to the ErbB3 or ErbB4 receptor tyrosine kinases. NRG1 is a trophic factor that has been implicated in neural development, neurotransmission, and synaptic plasticity. Neuregulin 1 (NRG1) is essential for the development and function of multiple organ systems, and its dysregulation has been linked to diseases such as cancer and schizophrenia. NRG1 is a schizophrenia candidate gene and plays an important role in brain development and neural function.   Product Properties   Synonyms Heregulin-beta1, HRG1 Accession Q02297 GeneID 3084 Source E.coli-derived Human NRG1-β2, Ser177-Gln237. Molecular Weight Approximately 7.0 kDa. AA Sequence SHLVKCAEKE KTFCVNGGEC FMVKDLSNPS RYLCKCPNEF TGDRCQNYVM ASFYKAEELY Q Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 96% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using serum free human MCF-7 cells is less than 5 ng/mL, corresponding to a specific activity of > 2.0 × 10 5 U/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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Neurotrophin-4 (NT-4), is a member of the NGF family of neuronal and epithelial growth factors. Neurotrophins have six conserved cysteine residues that are involved in the formation of three disulfide bonds.Mature human NT-4 shares 91% and 95% aa sequence identity with mouse and rat NT-4/5, respectively. The mature protein is secreted as a homodimer and can also form heterodimers with BDNF or NT-3. NT-4 binds and induces receptor dimerization and activation of TrkB. NT-4 promotes the development and survival of selected peripheral and CNS neurons.   Product Properties   Synonyms Neurotrophin-5, NT-5; Neurotrophin-4 ;GLC10 Accession P34130 GeneID 4909 Source E.coli-derived Human NT-4, G81-A210, with an N-terminal Met. Molecular Weight Approximately 28.1 kDa. AA Sequence MGVSETAPAS RRGELAVCDA VSGWVTDRRT AVDLRGREVE VLGEVPAAGG SPLRQYFFET RCKADNAEEG GPGAGGGGCR GVDRRHWVSE CKAKQSYVRA LTADAQGRVG WRWIRIDTAC VCTLLSRTGR A Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97 % by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by the dose-dependent induction of choline acetyl transferase activity in rat basal forebrain primary septal cell cultures is less than 50 ng/mL, corresponding to a specific activity of > 2.0 × 10 4 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 5.5. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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Brain-type Natriuretic Peptide (BNP) is a nonglycosylated peptide that is produced predominantly by ventricular myocytes and belongs to the natriuretic peptide family. Proteolytic cleavage of the 12 kDa BNP precursor gives rise to N-terminal Pro‑BNP (NT-proBNP) and mature BNP. Plasma NT-proBNP is a marker for congestive heart failure, while mature BNP (aa 103‑134) promotes vasodilation and fluid and sodium excretion. Human BNP precursor shares 29% and 51% aa sequence identity with mouse and porcine BNP precursor, respectively.   Product Properties   Synonyms Natriuretic peptides B, Gamma-brain natriuretic peptide Accession P16860 GeneID 4879 Source E.coli-derived Human NT-pro-BNP, His27-Arg102. Molecular Weight Approximately 8.5 kDa. AA Sequence HPLGSPGSAS DLETSGLQEQ RNHLQGKLSE LQVEQTSLEP LQESPRPTGV WKSREVATEG IRGHRKMVLY TLRAPR Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 98 % by SDS-PAGE and HPLC analyses. Biological Activity Data is not available. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20mM Tris-HCl, pH 8.0, 150mM NaCl. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Oncostatin M (OSM) is a growth and differentiation factor that participates in the regulation of neurogenesis, osteogenesis and hematopoiesis. It stimulates the proliferation of fibroblasts, smooth muscle cells and Kaposi’s sarcoma cells, but inhibits the growth of some normal and tumor cell lines.   Product Properties   Synonyms Oncostatin M/oncostatin-M; Uniprot No. P13725 Source Human OSM Protein is expressed from HEK293 without tag. It contains Ala26-Arg221. Molecular Weight The protein has a predicted 25.8 kDa Purity > 95% as determined by SDS-PAGE. Biological Activity The ED50 as determined by a cell proliferation assay using human TF-1 cells is 5-30 pg/mL. Endotoxin < 0.01 EU per 1μg of the protein by the LAL method. Formulation Dissolved in sterile PBS buffer. Concentration 0.2 mg/ml   Storage   The product should be stored at -85~-65℃ for 1 year from date of receipt. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Please operate with lab coats and disposable gloves,for your safety. 2. This product is for research use only.

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Osteoprotegerin (OPG), also called OCIF (osteoclastogenesis inhibitory factor) is a secreted 55-60 kDa protein that regulates bone density. As a member of the tumor necrosis factor receptor (TNFR) superfamily of proteins, it is designated TNFRSF11B. Human OPG cDNA encodes 401 amino acids (aa) including a 21 aa signal peptide and a 380 aa mature soluble protein with four TNFR domains, two death domains and a heparin-binding region. The cysteine-rich TNFR domains are essential for ligand interaction, while a cysteine at the C-terminus mediates homodimerization. Mature human OPG shares 86%, 87%, 92%, 92% and 88% amino acid sequence identity with mouse, rat, equine, canine and bovine OPG, respectively. OPG is widely expressed and constitutively released as a homodimer by mesenchymal stem cells, fibroblasts and endothelial cells. Regulation of its expression by estrogen, parathyroid hormone and cytokines is complex and changes with age. OPG has been called a decoy receptor for the TNF superfamily ligands, TRANCE (tumor necrosis factor-related activation-induced cytokine), also called RANK L (receptor activator of NF kappa B ligand), and TRAIL (TNF-related apoptosis-inducing ligand), which also bind TNF family receptors RANK and TRAIL receptors 1-4, respectively. TRAIL decreases the release of OPG from cells that express it, while OPG inhibits TRAIL-induced apoptosis. Expression of RANK L on the cell surface, and thus its ability to stimulate osteoclastogenesis, is regulated by OPG by intracellular and extracellular mechanisms. Within osteoblasts, interaction of the basic domain of OPG with RANK L in the Golgi inhibits RANK L secretion.   Product Properties   Synonyms TNFRSF11B, Osteoclastogenesis Inhibitory Factor, Tumor Necrosis Factor Receptor Superfamily Member 11B Accession O00300 GeneID 4982 Source E.coli-derived Human OPG, Glu22-Lys194. Molecular Weight Approximately 19.7 kDa. AA Sequence ETFPPKYLHY DEETSHQLLC DKCPPGTYLK QHCTAKWKTV CAPCPDHYYT DSWHTSDECL YCSPVCKELQ YVKQECNRTH NRVCECKEGR YLEIEFCLKH RSCPPGFGVV QAGTPERNTV CKRCPDGFFS NETSSKAPCR KHTNCSVFGL LLTQKGNATH DNICSGNSES TQK Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95 % by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by neutralizing the stimulation of U937 cells is less than 10 ng/mL, corresponding to a specific activity of > 1.0 × 10 5 IU/mg in the presence of 10 ng/mL soluble rHuRANKL (sRANKL). Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM PB,150 mM NaCl, pH 6.0. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Osteoprotegerin (OPG), also called OCIF (osteoclastogenesis inhibitory factor) is a secreted 55-60 kDa protein that regulates bone density. As a member of the tumor necrosis factor receptor (TNFR) superfamily of proteins, it is designated TNFRSF11B. Human OPG cDNA encodes 401 amino acids (aa) including a 21 aa signal peptide and a 380 aa mature soluble protein with four TNFR domains, two death domains and a heparin-binding region. The cysteine-rich TNFR domains are essential for ligand interaction, while a cysteine at the C-terminus mediates homodimerization. Mature human OPG shares 86%, 87%, 92%, 92% and 88% amino acid sequence identity with mouse, rat, equine, canine and bovine OPG, respectively. OPG is widely expressed and constitutively released as a homodimer by mesenchymal stem cells, fibroblasts and endothelial cells. Regulation of its expression by estrogen, parathyroid hormone and cytokines is complex and changes with age. OPG has been called a decoy receptor for the TNF superfamily ligands, TRANCE (tumor necrosis factor-related activation-induced cytokine), also called RANK L (receptor activator of NF kappa B ligand), and TRAIL (TNF-related apoptosis-inducing ligand), which also bind TNF family receptors RANK and TRAIL receptors 1-4, respectively. TRAIL decreases the release of OPG from cells that express it, while OPG inhibits TRAIL-induced apoptosis. Expression of RANK L on the cell surface, and thus its ability to stimulate osteoclastogenesis, is regulated by OPG by intracellular and extracellular mechanisms. Within osteoblasts, interaction of the basic domain of OPG with RANK L in the Golgi inhibits RANK L secretion. Extracellularly, OPG binding to RANK L results in clathrin-mediated internalization and degradation of both proteins. Binding of OPG by syndecan-1 heparin sulfates on multiple myeloma cells also results in OPG internalization and degradation, contributing to bone loss.   Product Properties   Accession O00300 GeneID 4982 Source Yeast-derived Human OPG-Fc, Glu22-Lys194. Molecular Weight Approximately 109.6 kDa. AA Sequence ETFPPKYLHY DEETSHQLLC DKCPPGTYLK QHCTAKWKTV CAPCPDHYYT DSWHTSDECL YCSPVCKELQ YVKQECNRTH NRVCECKEGR YLEIEFCLKH RSCPPGFGVV QAGTPERNTV CKRCPDGFFS NETSSKAPCR KHTNCSVFGL LLTQKGNATH DNICSGNSES TQKCGIDVTL EPKSSDKTHT CPPCPAPEFE GAPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPTPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GK Tag with an C-terminal Fc Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95 % by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by neutralizing the stimulation of U937 cells is less than 10 ng/mL, corresponding to a specific activity of > 1.0 × 10^5 IU/mg in the presence of 10 ng/mL soluble rHuRANKL (sRANKL). Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM PB, pH 6.0, 150 mM NaCl, 0.02 % Tween-80. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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OTOR also named Otoraplin and MIAL, is a 15 kDa disulfide bonded homodimer, which is secreted via the Golgi apparatus and is a member of the MIA/OTOR family. The OTOR shares high sequence identity with the mouse (90%), chicken (80%), and bullfrog (60%) orthologs and with the related human CDRAP/MIA protein (43%). Members of this family which also includes MIA, MIA2, and TANGO share a Src homology-3 (SH3)-like domain. OTOR is mainly expressed in the cochlea of the inner-ear and appears to be involved in early chondrogenesis of the otic capsule, which is required for normal inner ear development and auditory function. It is highly homologous to MIA/cartilage-derived retinoic acid-sensitive protein (CD-RAP), which is a cartilage-specific protein that is also expressed in malignant melanoma cells.   Product Properties   Synonyms Fibrocyte-derived Protein, Melanoma Inhibitory Activity-like Protein Accession Q9NRC9 GeneID 56914 Source E.coli-derived human OTOR protein, Vla18-Glu128. Molecular Weight Approximately 12.7 kDa. AA Sequence VHGIFMDRLA SKKLCADDEC VYTISLASAQ EDYNAPDCRF INVKKGQQIY VYSKLVKENG AGEFWAGSVY GDGQDEMGVV GYFPRNLVKE QRVYQEATKE VPTTDIDFFC E Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >97% by SDS-PAGE and HPLC analyses. Biological Activity Testing in progress. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM PB, pH 7.4, 150 mM NaCl. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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PTH (parathyroid hormone) is a critical hormone in the regulation of Ca++ homeostasis. PTH is secreted by the chief cells of the parathyroid glands as a polypeptide. PTH secretion is enhanced by low Ca++ concentrations and inhibited by FGF-23. In normal human plasma, PTH correlates negatively with active Vitamin D and positively with ionized calcium. Human and other mammalian PTH will bind and stimulate human or rat PTH1R, activating adenylate cyclase and increasing cAMP production. PTH promotes secretion of TRANCE/RANKL and periostin through PTH1R binding on osteoblasts and/or bone marrow stromal cells TRANCE/RANKL induces differentiation of osteoclasts, which in turn promote release of Ca++ from bone. PTH1R on osteocytes,  however, allows PTH to promote bone formation and IGF-1 production. In addition, PTH increases hematopoietic stem cell proliferation and mobilization and induces arterial vasodilation by regulating Ca++ influx in PTH1R-expressing arterial smooth muscle. In renal epithelium, PTH promotes conversion of Vitamin D to its active form, lowers Ca++ excretion and increases phosphate excretion.   Product Properties   Synonyms Parathormone, Parathyrin Accession P01270 GeneID 5741 Source E.coli-derived Human PTH1-84, Ser32-Gln115. Molecular Weight Approximately 9.4 kDa. AA Sequence SVSEIQLMHN LGKHLNSMER VEWLRKKLQD VHNFVALGAP LAPRDAGSQR PRKKEDNVLV ESHEKSLGEA DKADVNVLTK AKSQ Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by its ability to induce cAMP accumulation in murine MC3T3E1 cells is less than 50 ng/mL, corresponding to a specific activity of > 2.0×10 4 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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PTHrP, also named parathyroid hormone-related protein, is belonging to the parathyroid hormone family. PTHrP is expressed in cancer cells (breast cancer, certain types of lung cancer including squamous cell lung carcinoma). The receptor for PTHrP is PTHR1. PTHrP plays a central role in regulating the hypercalcemia. Recombinant human PTHrP is a 9.9 kDa linear polypeptide of 86 amino acid residues and it shares 86 % a.a. identity with mouse PTHLH.   Product Properties   Synonyms Parathormone, Parathyrin Accession P12272 GeneID 5744 Source E.coli-derived human PTHrP protein, Ala37-Pro122. Molecular Weight Approximately 9.9 kDa. AA Sequence AVSEHQLLHD KGKSIQDLRR RFFLHHLIAE IHTAEIRATS EVSPNSKPSP NTKNHPVRFG SDDEGRYLTQ ETNKVETYKE QPLKTP Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >98% by SDS-PAGE and HPLC analyses. Biological Activity Testing in progress. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 10 mM PB, pH 6.0, 300 mM NaCl. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Procalcitonin (PCT) belongs to a group of related proteins including calcitonin gene-related peptides I and II, amylin, adrenomodulin and calcitonin (CAPA peptide family). Mature PCT is expressed as a 116 amino acid (aa) protein which is subsequently cleaved into 3 parts: a 57 aa pro-region, a 32 aa Calcitonin peptide and a 21 aa Katacalcin peptide. PCT is a peptide precursor of the hormone calcitonin, the latter being involved with calcium homeostasis. PCT is produced by parafollicular cells (C cells) of the thyroid and by the neuroendocrine cells of the lung and the intestine. But its level is related to the severity of bacterial sepsis, it is considered to be one of the earliest and most specific markers of sepsis.   Product Properties   Synonyms CALC1, CALCA, Calcitonin 1, calcitonin gene-related peptide 1, CGRP, Katacalcin, Procalcitonin Accession P01258-1 GeneID 796 Source E.coli-derived human PCT/Procalcitonin protein, Ala26-Asn141. Molecular Weight Approximately 12.8 kDa. AA Sequence APFRSALESS PADPATLSED EARLLLAALV QDYVQMKASE LEQEQEREGS SLDSPRSKRC GNLSTCMLGT YTQDFNKFHT FPQTAIGVGA PGKKRDMSSD LERDHRPHVS MPQNAN Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >98% by SDS-PAGE and HPLC analyses. Biological Activity Testing in progress. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM Tris-HCl, pH 8.0, 150 mM NaCl. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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PDGF is involved in a number of biological processes, including hyperplasia, embryonic neuron development, chemotaxis, and respiratory tubule epithelial cell development. The A-chain homodimers of the platelet-derived growth factor (PDGF AA) are widely expressed in normal and transformed cells. The mitogenic properties of PDGF AA are well established. FGF-2 and platelet-derived growth factor-A (PDGF-AA) are potent modulators of oligodendrocytes, the main responsible cells for myelin   Product Properties   Synonyms PDGF1, PDGF-A, PDGFAA, PDGF-AA Accession P04085 GeneID 5154 Source E.coli-derived human PDGF-AA, Ser87-His211, with an N-terminal Met. Molecular Weight Approximately 28.8 kDa. AA Sequence MSIEEAVPAV CKTRTVIYEI PRSQVDPTSA NFLIWPPCVE VKRCTGCCNT SSVKCQPSRV HHRSVKVAKV EYVRKKPKLK EVQVRLEEHL ECACATTSLN PDYREEDTGR PRESGKKRKR KRLKPT Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >95% by SDS-PAGE analyses. Biological Activity The ED50 for this effect is 50-200 ng/mL in a fluorometric assay using the redox sensitive dye. Measured in a cell proliferation assay using NR6R-3T3 mouse fibroblast cells. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM PB, 300 mM NaCl, pH 6.0. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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Platelet-derived growth factor (PDGF) was discovered as a major mitogenic factor present in serum but absent from plasma. In vitro, PDGF-BB stimulated MAP kinase activity and cell motility of isolated lymphatic endothelial cells. In vivo, PDGF-BB potently induced growth of lymphatic vessels. Expression of PDGF-BB in murine fibrosarcoma cells induced tumor lymphangiogenesis, leading to enhanced metastasis in lymph nodes. The PDGF signaling system contributes to and vascular remodeling. Growth factors such as PDGF exert potent effects on wound healing including the regeneration of tooth-supporting structures.   Product Properties   Synonyms Becaplermin, ODGF, PDGF-2, PDGFBB, PDGF-BB Accession P01127 GeneID 5155 Source E.coli-derived human PDGF-BB protein, Ser82-Thr190, with an N-terminal Met. Molecular Weight Approximately 24.8 kDa AA Sequence MSLGSLTIAE PAMIAECKTR TEVFEISRRL IDRTNANFLV WPPCVEVQRC SGCCNNRNVQ CRPTQVQLRP VQVRKIEIVR KKPIFKKATV TLEDHLACKC ETVAAARPVT Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97 % by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 3 ng/ml, corresponding to a specific activity of > 3.3 × 10^5 IU/mg. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. For your safety and health, please wear lab coats and disposable gloves for operation. 2. For research use only.

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The platelet-derived growth factor (PDGF) family of heparin-binding growth factors consists of five known members, denoted PDGF-AA, PDGF-BB, PDGF-AB, PDGF-CC and PDGF-DD.The PDGFs interact with two related protein tyrosine kinase receptors, PDGFR-α and PDGFR-β, and are potent mitogens for a variety of cell types. They play an important role in a number of biological processes, including hyperplasia, chemotaxis, embryonic neuron development, and respiratory tubules' epithelial cell development.   Product Properties Synonyms   PDGFCC; PDGF-CC   Source E.coli Molecular Weight Approximately 27 kDa, a disulfide-linked homodimer of two 117 amino acid, C-terminal polyhistidine tagged proteins. AA Sequence Accession :NP_057289 Val235-Gly345,  with an N-terminal Met and 6-His tag; Biological Activity Measured in a cell proliferation assay using NR6R3T3 mouse fibroblast cells. The ED50 for this effect is 70-350 ng/mL. Purity > 97% by SDS-PAGE. Endotoxin <0.1EU per 1μg of the protein by the LAL method. Formulation Lyophilized from 0.2 µm filtered concentrated solution in 30 % Acetonitrile and 0.1 % TFA. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in 4 mM HCl to a concentration of 0.1 mg/mL. Further dilutions should be made in appropriately buffered solutions.   Shipping and Storage The product should be stored at -25~-15℃ for 1 year from date of receipt. 1 month, 2 ~8 °C under sterile conditions after reconstitution. 3 months, -25~-15℃ under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1.Please operate with lab coats and disposable gloves,for your safety. 2.This product is for research use only.

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Persephin is a secreted protein belonging to the glial cell line-derived neurotrophic factor (GDNF) family of the TGF-beta superfamily. It shares 38 - 46% amino acid (aa) identity with family members GDNF, neurturin and artemin. Persephin is expressed at very low levels in most tissues. The 156 aa, 10 - 12 kDa mature protein contains a signal sequence, a pro-domain and a 96 aa mature sequence with several cysteines that are conserved among family members. It circulates as an unglycosylated disulfide-linked homodimer. Mature human Persephin shares 81% and 80%, 89% and 87% amino acid sequence identity with mouse, rat, bovine and canine Persephin, respectively. Like other GDNF family members, Persephin acts through engagement of GRF alpha 4, a glycosylphosphatidylinositol (GPI)-linked GDNF receptor family (GRF) member that signals through the receptor tyrosine kinase RET. Persephin is reported to promote both the survival and growth of central dopaminergic and motor neurons, and kidney development. These effects are correlated with the expression patterns of GFR alpha 4, and RET. Functional GFR alpha 4 isoforms are found only in thyroid, adrenal medulla and portions of the central nervous system, and include GPI-linked, transmembrane and soluble forms. In vitro, Persephin promotes survival only in neurons which coexpress GPI-linked GFR alpha 4 with RET. This effect does not show a strong correlation to the recruitment of RET in lipid rafts seen with other GDNF family members.   Product Properties   Synonyms Persephin; PSP; PSPN Accession P06734 GeneID 2208 Source E.coli-derived Human Persephin, Ala61-Gly156. Molecular Weight Approximately 20.5 kDa. AA Sequence ALSGPCQLWS LTLSVAELGL GYASEEKVIF RYCAGSCPRG ARTQHGLALA RLQGQGRAHG GPCCRPTRYT DVAFLDDRHR WQRLPQLSAA ACGCGG Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97 % by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using human TT medullary thyroid cancer cells is less than 10 ng/mL, corresponding to a specific activity of > 1.0 × 10^5 IU/mg. Fully biologically active when compared to standard. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Pigment epithelium-derived factor (PEDF) is encoded by the SERPINF1 gene in humans and found in verebrates. It is a secreted phosphoglycoprotein that belongs to the clade F subfamily, serpin superfamily of proteinase inhibitors. The PEDF is a noninhibitory serpin with neurotrophic, anti-angiogenic, and anti-tumorigenic properties. It is synthesized as a 418 a.a. about 50kDa precursor that contains a 19 a.a. signal sequence and a 399 a.a. mature region that shows a pyroglutamate at Gln20. Like other serpins, it contains three β-sheets, 810 α-helices, and a C-terminal RCL (reactive center loop). Unlike other serpins with Ser protease inhibiting activity. PEDF has functions of inducing extensive neuronal differentiation in retinoblastoma cells, inhibiting of angiogenesis. As it does not undergo the S (stressed) to R (relaxed) conformational transition characteristic of active serpins, it exhibits no serine protease inhibitory activity. PEDF is researched as a therapeutic candidate for treatment of such conditions as choroidal neovascularization, heart disease, and cancer.   Product Properties   Synonyms Serpin peptidase inhibitor, clade F，member 1,SerpinF1, EPC-1, Cell proliferation-inducing gene 35  protein Accession P36955 GeneID 5176 Source E.coli-derived human Pigment Epithelium-derived Factor protein,Gln20-Pro418 Molecular Weight Approximately 44.4 KDa AA Sequence QNPASPPEEG SPDPDSTGAL VEEEDPFFKV PVNKLAAAVS NFGYDLYRVR SSTSPTTNVL LSPLSVATAL SALSLGAEQR TESIIHRALY YDLISSPDIH GTYKELLDTV TAPQKNLKSA SRIVFEKKLR IKSSFVAPLE KSYGTRPRVL TGNPRLDLQE INNWVQAQMK GKLARSTKEI PDEISILLLG VAHFKGQWVT KFDSRKTSLE DFYLDEERTV RVPMMSDPKA VLRYGLDSDL SCKIAQLPLT GSMSIIFFLP LKVTQNLTLI EESLTSEFIH DIDRELKTVQ AVLTVPKLKL SYEGEVTKSL QEMKLQSLFD SPDFSKITGK PIKLTQVEHR AGFEWNEDGA GTTPSPGLQP AHLTFPLDYH LNQPFIFVLR DTDTGALLFI GKILDPRGP Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97 % by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The ED50 as determined by its ability to enhance the adhesion of human Saos2 cells to bovine Collagen I coated plate is less than 2 ng/ml, corresponding to a specific activity of > 5.0 × 10 5 IU/mg. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM PB, pH 7.4, 150 mM NaCl. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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PlGF-2 is an angiogenic factor that belongs to the cysteine-knot superfamily of growth factors. PlGF-2 is expressed in umbilical vein endothelial cells and placenta. It signals through the VEGFR-1/FLT1 receptor, and stimulates endothelial cell proliferation and migration. PlGF-2 also signals through Neuropilin (NP-1), and can bind with high affinity to heparin. Recombinant Human PlGF-2 is a 34.6 kDa disulfide-linked homodimeric protein of two 152 amino acid polypeptide chains.   Product Properties   Synonyms Placenta Growth Factor-2, PGFL Accession P49763-3 GeneID 5228 Source E.coli-derived Human PlGF-2 protein,Leu19-Arg131. Molecular Weight Approximately 34.6 kDa. AA Sequence LPAVPPQQWA LSAGNGSSEV EVVPFQEVWG RSYCRALERL VDVVSEYPSE VEHMFSPSCV SLLRCTGCCG DENLHCVPVE TANVTMQLLK IRSGDRPSYV ELTFSQHVRC ECRPLREKMK PERRRPKGRG KRRREKQRPT DCHLCGDAVP RR Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The biologically active as determined by its ability to chemoattract human monocytes using a concentration range of 5.0-50 ng/mL. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4, with 0.02 % Tween-20. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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CXCL4, also called PF4 (platelet factor 4), is an 8 kDa member of the CXC chemokine family, sharing features with CXCL8/IL-8 and CXCL7/NAP-2. Mature human CXCL4 shares 65-76% amino acid sequence identity with mouse, rat, bovine, ovine and porcine CXCL4. The active protein is a tetramer of CXCL4 subunits that forms a ring of heparin-binding positive charges from sites at the C-terminal region of each monomer. Megakaryocytes synthesize CXCL4 and store it in platelet alpha -granules. Secretion from activated platelets can produce micromolar levels in serum and over 100-fold higher within clots. In contrast to other CXC chemokines, CXCL4 does not contain an ELR motif and lacks binding to nearly all chemokine receptors. A potential high-affinity G-protein-coupled receptor for CXCL4, the CXCR3 isoform CXCR3B, is expressed in human but not mouse. In most cases, it is likely that cell surface binding and signaling properties of CXCL4 are due to binding of glycosaminoglycans chains, particularly chondroitin sulfates. CXCL4 released from activated platelets binds and regulates thrombin/thrombomodulin complexes, regulates and enhances production of activated Protein C (APC), and limits the coagulation cascade. It binds and influences the enzymatic activity of coagulation factor Xa. It binds fibrin and affects clot structure. Therapeutic doses of the anticoagulant heparin neutralize CXCL4 procoagulant effects.   Product Properties   Synonyms Iroplact, Oncostatin-A Accession P02776 GeneID 5196 Source E.coli-derived Human GRO-γ,Glu32-Ser101. Molecular Weight Approximately 7.8 kDa AA Sequence EAEEDGDLQC LCVKTTSQVR PRHITSLEVI KAGPHCPTAQ LIATLKNGRK ICLDLQAPLY KKIIKKLLES Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The biological activity determined by a chemotaxis bioassay using human fibroblasts is in a concentration of 1.0-10 ng/mL. Endotoxin < 1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in Acetonitrile and TFA Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycle. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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PTN was identified independently by several groups as a novel heparin-binding, developmentally regulated cytokine. Depending on the biological activities studied, this protein has variously been referred to as heparin-binding brain mitogen (HBBM), heparin-binding growth factor-8 (HBGF-8), heparin-binding neurite promoting factor, heparin-binding neurotrophic factor (HBNF),  heparin-affinity regulatory peptide (HARP), heparin-binding growth-associated molecule (HB-GAM), osteoblast-specific factor  (OSF-1), and pleiotrophin. PTN is a highly conserved protein; the amino acid sequences of human, bovine, rat, and mouse PTN share > 98% homology.PTN is a member of a family of heparin-binding proteins that share sequence, structural, and functional similarity. Other members of this family include midkine (MK), and chicken retinoic acid-induced heparin-binding protein (RI-HB), an avian homologue of MK. The expression of all these cytokines is restricted and highly regulated during development. PTN can be  used as an attachment substrate to stimulate neurite outgrowth in mixed cultures of embryonic rat, mouse or chicken brain cells.  Although both natural and recombinant human PTN have been reported to be mitogenic for fibroblasts, endothelial, and epithelial cells, the data are still highly controversial.   Product Properties   Synonyms HARP; HBBM; HB-GAM; HBGF8; HBNF Accession P21246 GeneID 5764 Source E.coli-derived human PTN, Gly33-Asp168. Molecular Weight Approximately 15.3 kDa. AA Sequence GKKEKPEKKV KKSDCGEWQW SVCVPTSGDC GLGTREGTRT GAECKQTMKT QRCKIPCNWK KQFGAECKYQ FQAWGECDLN TALKTRTGSL KRALHNAECQ KTVTISKPCG KLTKPKPQAE SKKKKKEGKK QEKMLD Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 96 % by SDS-PAGE and HPLC analyses. Biological Activity The biological activity was measured by its ability to enhance neurite outgrowth of E16-E18 rat embryonic cortical neurons, when neurons were plated on 96 well culture plates that had been pre-coated with 100 µl/well of a solution of 5-10 µg/mL rHuPTN. Fully biologically active when compared to standard. Endotoxin Less than 0.1 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom.Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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This gene encodes insulin, a peptide hormone that plays a vital role in the regulation of carbohydrate and lipid metabolism. After removal of the precursor signal peptide, proinsulin is post-translationally cleaved into three peptides: the B chain and A chain peptides, which are covalently linked via two disulfide bonds to form insulin, and C-peptide. Binding of insulin to the insulin receptor (INSR) stimulates glucose uptake. A multitude of mutant alleles with phenotypic effects have been identified. There is a read-through gene, INS-IGF2, which overlaps with this gene at the 5' region and with the IGF2 gene at the 3' region. Alternative splicing results in multiple transcript variants. Product Properties   Synonyms Human Proinsulin C-Peptide Analogue, IDDM Protein, Human; IDDM1 Protein, Human Accession P01308 GeneID 3630 Source E.coli-derived human Proinsulin C-Peptide Analogue protein,Arg55-Arg89 Molecular Weight Approximately 3.6 kDa. AA Sequence RREAEDLQVG QVELGGGPGA GSLQPLALEG SLQKR Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95 % by SDS-PAGE and HPLC analyses. Biological Activity Data Not Available. Endotoxin Less than 0.1 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom.Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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Kallikrein 3, commonly known as prostate specific antigen (PSA), is a serine protease of the human tissue Kallikrein gene family. The human tissue kallikrein (KLK) gene family contains 15 members that play important roles in cancer. Kallikrein-3, called prostate specific antigen (PSA), is a glycoprotein enzyme encoded in humans by the KLK3 gene. PSA is secreted by the epithelial cells of the prostate gland, hydrolyzes semenogelin-1 thus leading to the liquefaction of the seminal coagulum. PSA is an established tumor marker that aids in the diagnosis, staging, and follow up of prostate cancer.   Product Properties   Synonyms APS seminin, hK3, Kallikrein 3, KLK2A1, KLK3, P-30 antigen, PSA Accession P07288 GeneID 354 Source E.coli-derived human PSA/Kallikrein-3 protein, Ile25-Pro261. Molecular Weight Approximately 26.1 kDa. AA Sequence IVGGWECEKH SQPWQVLVAS RGRAVCGGVL VHPQWVLTAA HCIRNKSVIL LGRHSLFHPE DTGQVFQVSH SFPHPLYDMS LLKNRFLRPG DDSSHDLMLL RLSEPAELTD AVKVMDLPTQ EPALGTTCYA SGWGSIEPEE FLTPKKLQCV DLHVISNDVC AQVHPQKVTK FMLCAGRWTG GKSTCSGDSG GPLVCNGVLQ GITSWGSEPC ALPERPSLYT KVVHYRKWIK DTIVANP Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95 % by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The biological activity determined by a chemotaxis bioassay using human monocytes is in a concentration of 10-100 ng/ml. Endotoxin Less than 0.1 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20mM Tris-HCl, pH 8.0, 150mM NaCl, 3% trehalose Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom.Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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RANTES is a CC chemokine that can signal through the CCR1, CCR3, CCR5 and US28 (cytomegalovirus receptor) receptors. It is a chemoattractant towards monocytes, memory T cells (CD4+/CD45RO), basophils, and eosinophils. RANTES also has the capability to inhibit certain strains of HIV-1, HIV-2 and simian immunodeficiency virus (SIV). Recombinant Human RANTES is a 7.8 kDa protein containing 68 amino acid residues, including the four highly conserved cysteine residues present in the CC chemokines.   Product Properties   Synonyms SIS-delta, Small-inducible cytokine A5, T-cell-specific protein RANTES Accession P13501 GeneID 6352 Source E.coli-derived Human CCL5 protein,Ser24-Ser91. Molecular Weight Approximately 7.8 kDa. AA Sequence SPYSSDTTPC CFAYIARPLP RAHIKEYFYT SGKCSNPAVV FVTRKNRQVC ANPEKKWVRE YINSLEMS Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 98 % by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The biological activity determined by a chemotaxis bioassay using human peripheral blood monocytes is in a concentration range of 1.0-10 ng/mL. Endotoxin Less than 0.1 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20mM PB, pH 7.4, 100 mM NaCl. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom.Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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Rb encoded by the RB1 gene in humans, is expressed by retina and belongs to the etinoblastoma-associated protein family. The hole protein consists of 928 a.a. and the rHuRb fragment occupies sequence of 792-929 a.a.. Rb is a key regulator of entry into cell division that acts as a tumor suppressor. It has many functions, for example, promotes G0-G1 transition when phosphorylated by CDK3/cyclin-C, and acts as a transcription repressor of E2F1 target genes and so on. The rHuRb is the region that rich of modified residue like phosphothreonine and N6-acetyllysine. Product Properties   Synonyms p105-Rb, pRb, pp110 Accession Q59HH0 GeneID 4595173 Source E.coli-derived human Rb137 protein, Phe792-Lys928. Molecular Weight Approximately 16.5 kDa. AA Sequence MASFPSSPLR IPGGNIYISP LKSPYKISEG LPTPTKMTPR SRILVSIGES FGTSEKFQKI NQMVCNSDRV LKRSAEGSNP PKPLKKLRFD IEGSDEADGS KHLPGESKFQ QKLAEMTSTR TRMQKQKMND SMDTSNKEEK HHHHHH Tag C-His Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95 % by SDS-PAGE and HPLC analyses. Biological Activity Data Not Available. Endotoxin Less than 1.0 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom.Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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Human RSPO1 protein, also known as R-Spondin 1, is a naturally occurring protein in the human body that plays a significant role in the Wnt signaling pathway. This pathway regulates various cellular functions, including cell growth, differentiation, and tissue regeneration. RSPO1 acts as an agonist, meaning it enhances the activity of Wnt proteins by binding to their receptors and activating them. This activation leads to downstream signaling events that impact cell behavior and tissue development.   Product Properties Synonyms   R-Spondin 1；Roof Plate-specific Spondin 1   Uniprot No.  Q2MKA7 Source E.coli-derived human RSPO1 protein, Arg21-Ala263，with N-terminal His tag. Molecular Weight Approximately 27.6 kDa. Purity > 50% as determined by SDS-PAGE. Endotoxin < 1 EU per 1μg of the protein by the LAL method. Formulation Liquid in 20 mM Tris，1 M NaCl，pH8.0，the concentration is 0.05 mg/ml.   Shipping and Storage The product should be stored at -25~-15℃ for 1 year from date of receipt. Cautions 1.Please operate with lab coats and disposable gloves, for your safety. 2.This product is for research use only.

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S100B is a member of the S100 family of proteins containing two EF-hand-type calcium-binding motifs. S100B exerts both  intracellular and extracellular functions. Intracellular S100B acts as a stimulator of cell proliferation and migration and an inhibitor of apoptosis and differentiation, which might have important implications during brain, cartilage and skeletal muscle development and repair, activation of astrocytes in the course of brain damage and neurodegenerative processes, and of cardiomyocyte remodeling after infarction, as well as in melanomagenesis and gliomagenesis. As an extracellular factor, S100B engages RAGE (receptor for advanced glycation end products) in a variety of cell types with different outcomes (i.e. beneficial or detrimental, pro-proliferative or pro-differentiative) depending on the concentration attained by the protein, the cell type and the microenvironment. This calcium binding astrocyte-specific cytokine, presents a marker of astrocytic activation and reflects CNS injury. The excellent sensitivity of S100B has enabled it to confirm the existence of subtle brain injury in patients with mild head trauma, strokes, and after successful resuscitation from cardiopulmonary arrest. Recent findings provide evidence, that S100B may decrease neuronal injury and/or contribute to repair following traumatic brain injury (TBI). Hence, S100B, far from being a negative determinant of outcome, as suggested previously in the human TBI and ischemia literature, is of potential therapeutic value that could improve outcome in patients who sustain various forms of acute brain damage.   Product Properties   Synonyms NEF Protein, Human; S100 Protein, Human; S100-B Protein, Human; S100beta Protein, Human Accession P04271 GeneID 6285 Source E.coli-derived Human S100B protein,Ser2-Glu92 Molecular Weight Approximately 10.6 kDa. AA Sequence SELEKAMVALIDVFHQYSGREGDKHKLKKSELKELINNELSHFLEEIKEQEVVDKVMETLDNDG DGECDFQEFMAFVAMVTTACHEFFEH E Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97 % by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The biological activity determined by a chemotaxis bioassay using human monocytes is in a concentration of 10-100 ng/ml. Endotoxin Less than 1 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 mm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom.Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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CD40 Ligand, also known as TNFSF, a type II membrane protein with homology to TNF, is transiently expressed on activated T cells and known to be important for B cell Ig production and for activation and differentiation of monocytes and dendritic cells. Mature human CD40 Ligand consists of a 22 amino acid (aa) cytoplasmic domain, a transmembrane segment, and an 215 aa extracellular region . It is primarily expressed on activated CD4+ T lymphocytes, and also found in other types of cells, like NK cells, mast cells, basophils and eosinophils. In total CD40 ligand has three binding partners: CD40, α5β1 integrin and αIIbβ3. CD40 Ligand dysregulation on T cells and antigen presenting cells contributes to the immune deficiency associated with HIV infection and AIDS. CD40 ligation by CD40 Ligand promotes B cell activation and T cell-dependent humoral responses.   Product Properties   Synonyms CD154 antigen, CD154, CD40 antigen ligand, CD40 Ligand, gp39, HIGM1, T-B cell-activating molecule, T-BAM, TNFSF5, TNFSF5IMD3, TRAP Accession P29965 GeneID 959 Source E.coli-derived human sCD40L protein, Met113-Leu261. Molecular Weight Approximately 16.3 kDa. AA Sequence MQKGDQNPQI AAHVISEASS KTTSVLQWAE KGYYTMSNNL VTLENGKQLT VKRQGLYYIY AQVTFCSNRE ASSQAPFIAS LWLKSPGRFE RILLRAANTH SSAKPCGQQS IHLGGVFELQ PGASVFVNVT DPSQVSHGTG FTSFGLLKL Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95 % by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by the dose-dependent stimulation of IL-8 production by human PBMC is less than 5-10 ng/mL. Fully biologically active when compared to standard. Endotoxin Less than 1.0 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20mM PBS, pH 7.0. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom.Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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SCF, also known as stem cell factor or kit ligand, is a cytokine that plays a critical role in the survival, proliferation, and differentiation of hematopoietic stem cells and early progenitor cells. SCF is primarily produced by bone marrow stromal cells and functions by binding to the c-kit receptor on the surface of hematopoietic cells. Dysregulation of SCF signaling has been implicated in various types of cancer and hematological disorders.   Product Properties   Synonyms KITLG; FPH2; KL-1; Kitl; MGF; SF; SHEP7; KL Accession P21583-1 Source Recombinant Human SCF Protein is expressed from E.coli without tag. It contains Glu26-Ala189 Molecular Weight Approximately 18.45 kDa. Tag None Purity > 95% by SDS-PAGE and HPLC analyses. Endotoxin Less than 1.0 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from 0.22 μm filtered solution in PBS (pH 7.4). Normally 8% trehalose is added as protectant before lyophilization. Reconstitution Centrifuge the tube before opening, Reconstituting to a concentration more than 100 μg/ml is recommended. Dissolve the lyophilized protein in distilled water.   Storage   The product should be stored at -25~-15℃ for 1 year from date of receipt. 2-7 days, 2 ~8 °C under sterile conditions after reconstitution. 3 -6 months, -85~-65℃ under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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Secreted protein acidic and rich in cysteine (SPARC), also named as osteonectin or BM-40, is an acronym for “secreted protein, acidic and rich in cysteine”. Mature human SPARC shows 92%, 92%, 97%, 99%, 96% and 85% aa identity with mouse, rat, canine, bovine, porcine and chick SPARC. SPARC is the founding member of a family of secreted matricellular proteins with similar domain structure. It is produced by fibroblasts, capillary endothelial cells, platelets and macrophages, especially in areas of tissue morphogenesis and remodeling. SPARC is required for the collagen in bone to become calcified but is also involved in extracellular matrix synthesis and promotion of changes to cell shape. The gene product has been associated with tumor suppression but has also been correlated with metastasis based on changes to cell shape which can promote tumor cell invasion.   Product Properties   Synonyms Basement-membrane Protein 40, BM-40, Osteonectin, ON, SPARC Accession P09486 GeneID 6678 Source E.coli-derived human SPARC protein, Ala18-Asp1303. Molecular Weight Approximately 32.7 kDa. AA Sequence APQQEALPDE TEVVEETVAE VTEVSVGANP VQVEVGEFDD GAEETEEEVV AENPCQNHHC KHGKVCELDE NNTPMCVCQD PTSCPAPIGE FEKVCSNDNK TFDSSCHFFA TKCTLEGTKK GHKLHLDYIG PCKYIPPCLD SELTEFPLRM RDWLKNVLVT LYERDEDNNL LTEKQKLRVK KIHENEKRLE AGDHPVELLA RDFEKNYNMY IFPVHWQFGQ LDQHPIDGYL SHTELAPLRA PLIPMEHCTT RFFETCDLDN DKYIALDEWA GCFGIKQKDI DKDLVI Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 99 % by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by its ability to inhibit the cell growth of Mv1Lu mink lung epithelial cells is less than 3.0 μg/mL, corresponding to a specific activity of > 333 IU/mg. Fully biologically active when compared to standard. Endotoxin Less than 0.1 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom.Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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  Name Catalog No. Size Recombinant Human SLC1A5 Full Length Protein (VLP) C230780E 20 μg C230780S 100 μg C230780M 100 μg C230780L 1 mg   Product Properties   Synonyms SLC1A5 / AAAT / ASCT2 / M7V1 / RDR / RDRC Source HEK293 Cells AA sequence Accession #Q15758: Met1 - Met541 Endotoxin < 1EU per μg by the LAL method. Purity >95% as determined by DLS. Formulation 115mM Gly 4% trehalose Activity ELISA：Immobilized Human SLC1A5 VLP at 5 ug/mL (30 uL/well) can bind idactamab (P100098) , The EC50 was approximately 0.004176 ug/ml. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with PBS.   Figure Figure 1. Immobilized Human SLC1A5 VLP at 5 ug/mL (30 uL/well) can bind idactamab (P100098) , The EC50 was approximately 0.004176 ug/ml. Storage The product should be stored at -85~-65℃ for 1 year from date of receipt. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions   1. Please operate with lab coats and disposable gloves,for your safety.        2. This product is for research use only. 

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  Name Catalog No. Size Recombinant Human SLC7A11 Protein-VLP C230752E 20 μg C230752S 100 μg C230752M 100 μg C230752L 1 mg   Product Properties   Synonyms (Amino acid transport system xc-)(Calcium channel blocker resistance protein CCBR1)(Solute carrier family 7 member 11)(xCT) Source HEK293 Cells AA sequence Accession #Q9UPY5: Met1 - Leu501 Endotoxin < 1EU per μg by the LAL method. Purity > 85% as determined by DLS. Formulation 115mM Gly 4% trehalose Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with PBS.   Storage   The product should be stored at -85~-65℃ for 1 year from date of receipt. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions   1. Please operate with lab coats and disposable gloves,for your safety.        This product is for research use only.   

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Fas and Fas Ligand (FasL) belong to the TNF superfamily, and are type I and type II transmembrane proteins, respectively. Binding of FasL to Fas triggers apoptosis in Fas-bearing cells. The mechanism of apoptosis involves recruitment of pro-caspase 8 through an adaptor molecule called FADD, followed by processing of the pro-enzyme into active forms. These active caspases then cleave various cellular substrates, leading to the eventual cell death. sFasR is capable of inhibiting FasL-induced apoptosis by acting as a decoy receptor that serves as a sink for FasL. The full length Fas (receptor) is a 319 amino acid type I transmembrane protein, which contains a 157 amino acid extracellular domain, a 17 amino acid transmembrane domain, and a 145 amino acid cytoplasmic domain. Recombinant Human soluble Fas (sFas Receptor) is a 157 amino acid polypeptide (17.6 kDa) corresponding to the TNFR-homologous cysteine-rich extracellular Fas domain. Product Properties   Synonyms TNFRSF6, CD95, Apo I, Fas Antigen Accession P25445 GeneID 355 Source E.coli-derived Human sFasR/TNFRSF6 protein,Arg17-Asn173. Molecular Weight Approximately 17.6 kDa. AA Sequence RLSSKSVNAQ VTDINSKGLE LRKTVTTVET QNLEGLHHDG QFCHKPCPPG ERKARDCTVN GDEPDCVPCQ EGKEYTDKAH FSSKCRRCRL CDEGHGLEVE INCTRTQNTK CRCKPNFFCN STVCEHCDPC TKCEHGIIKE CTLTSNTKCK EEGSRSN Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95 % by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The ED50 as determined by its ability to inhibit the cytotoxicity of Jurkat cells is between 10-15 µg/mL in the presence of 2 ng/mLof rHuFas Ligand. Endotoxin Less than 1.0 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 mm filtered concentrated solution in 20 mM PB, pH 7.4, 150 mM NaCl. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom.Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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TNF receptor 1 (TNF RI; also called TNF R-p55/p60 and TNFRSF1A) is a 55 kDa type I transmembrane protein member of the TNF receptor superfamily, designated TNFRSF1A. Human TNF RI is a 455 amino acid (aa) protein that contains a 21 aa signal sequence and 190 aa ECD with a PLAD (pre-ligand assembly domain) that mediates constitutive dimer/trimer formation, followed by four CRD (cysteine-rich domains), a 23 aa transmembrane domain, and a 221 aa cytoplasmic sequence that contains a neutral sphingomyelinase activation domain and a death domain. The ECD of human TNF RI shows 70%, 69%, 80%, 80%, and 73% aa identity with mouse, rat, canine, feline and porcine TNF RI, respectively; and it shows 23% aa identity with the ECD of TNF RII. Both TNF RI and TNF RII (TNFRSF1B) are widely expressed and contain four TNF-alpha trimer-binding CRD in their ECD. However, TNF RI is thought to mediate most of the cellular effects of TNF-alpha. It is essential for proper development of lymph node germinal centers and Peyer's patches, and for combating intracellular pathogens such as Listeria. TNF RI is also a receptor for TNF-beta /TNFSF1B (lymphotoxin-alpha ). TNF RI is stored in the Golgi and translocates to the cell surface following pro-inflammatory stimuli. TNF-alpha stabilizes TNF RI and induces its sequestering in lipid rafts, where it activates NF kappa B and is cleaved by ADAM-17/TACE. Product Properties   Synonyms Human sTNF RI Accession P19438 GeneID 7132 Source E.coli-derived Human sTNF RI protein,Ile22-Thr211. Molecular Weight Approximately 17.6 kDa. AA Sequence IYPSGVIGLV PHLGDREKRD SVCPQGKYIH PQNNSICCTK CHKGTYLYND CPGPGQDTDC RECESGSFTA SENHLRHCLS CSKCRKEMGQ VEISSCTVDR DTVCGCRKNQ YRHYWSENLF QCFNCSLCLN GTVHLSCQEK QNTVCTCHAG FFLRENECVS CSNCKKSLEC TKLCLPQIEN VKGTEDSGTT Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97 % by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The ED50 as determined by its ability to inhibit the TNF-alpha mediated cytotoxicity in the L-929 cells is less than 0.05 μg/mL, corresponding to a specific activity of > 2 × 10 4IU/mg in the presence of 0.25 ng/mL of rHuTNF-alpha. Endotoxin Less than 0.1 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 mm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom.Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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TNF RII (Tumor Necrosis Factor Receptor II), also known as TNFRSF1B, p75/p80, and CD120b, is a widely expressed receptor for membrane-associated TNF-alpha and Lymphotoxin-alpha. Its activation initiates pro-inflammatory and pro-survival responses via NFkB-dependent signaling pathways, although it may also induce apoptosis. Product Properties   Synonyms Human sTNF RII Accession P20333 GeneID 7133 Source E.coli-derived Human sTNF RI protein,Ile22-Thr211. Molecular Weight Approximately 20.0kDa. AA Sequence MPAQVAFTPY APEPGSTCRL REYYDQTAQM CCSKCSPGQH AKVFCTKTSD TVCDSCEDST YTQLWNWVPE CLSCGSRCSS DQVETQACTR EQNRICTCRP GWYCALSKQE GCRLCAPLRK CRPGFGVARP GTETSDVVCK PCAPGTFSNT TSSTDICRPH QICNVVAIPG NASMDAVCTS TSPT Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97 % by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The ED50 as determined by its ability to inhibit the TNF-α mediated cytotoxicity in the L-929 cells is less than 0.2 μg/mL, corresponding to a specific activity of > 5000 IU/mg in the presence of 0.25 ng/mL of rHuTNF-α. Endotoxin Less than 0.1 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 mm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom.Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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Shh (Sonic Hedgehog protein) is a signaling molecule and a member of the Hedgehog (Hh) family. It plays a crucial role in physiological processes such as embryonic development, tissue regeneration, and cell proliferation. The Shh protein activates the Hh signaling pathway by binding to its receptor Patched (Ptch), which in turn activates the G protein-coupled receptor Smoothened (Smo). This signaling pathway is involved in the directed development of various organs and tissues during embryogenesis, including the central nervous system, limbs, and cardiovascular system. Due to the importance of Shh protein in development and tissue repair, it is also widely studied for its applications in stem cell culture, tissue engineering, and drug development. This recombinant human Shh is provided in the form of lyophilized powder, with high activity, high purity, low endotoxin, and without any additional tags. Product Properties   Synonyms HHG1, HHG-1, HLP3, HPE3, MCOPCB5 Accession Q15465 Source E.coli-derived Human shh, Cly25-Gly197, with an N-terminal Met. Molecular Weight Approximately 19.8kDa. AA Sequence IVIGPGRGFG KRRHPKKLTP LAYKQFIPNV AEKTLGASGR YEGKISRNSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDKLNALAI SVMNQWPGVK LRVTEGWDED GHHSEE SLHY EGRAVDITTS DRDRSKYGML ARLAVEAGFD WVYYESKAHI HCSVKAENSVAAKSGG Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 98 % by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by inducing alkaline phosphatase production of murine C3H/10T1/2 cells is less than 1 μg/mL, corresponding to a specific activity of > 1.0 × 103 IU/mg. Fully biologically active when compared to standard. Endotoxin Less than 1.0 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM PB, pH 7.4, 150 mM NaCl. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom.Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at-25~-15℃  for 1 year. 7 days, 2 to 8 °C under sterile conditions after reconstitution.  3 months,-85~-65℃ under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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