| Description | Glukagon-like peptide 1 (1-37), human (TFA) is a highly potent agonist of the GLP-1 receptor. Appearance:SolidIC50& Target:GLP-1 receptor. In Vitro:Glukagon-like peptide-1 (GLP-1) is produced by the posttranslational processing of proGlukagon and acts as a regulator of various homeostatic eventsGlukagon-like peptide 1 (1-37), human (TFA) is a highly potent agonist of the GLP-1 receptor. Appearance:SolidIC50& Target:GLP-1 receptor. In Vitro:Glukagon-like peptide-1 (GLP-1) is produced by the posttranslational processing of proGlukagon and acts as a regulator of various homeostatic events. GLP-1(1-37) is more stable than GLP-1(7-37), with 94.7% of the initial amount of peptide left after a 4hIn Vivo:GLP-1(1–37) decreases glycemic excursion in a dose-dependent. The administration of GLP-1(1–37) or GLP-1(7–37) markedly decrease blood glucose levels at 15 min and 30 min compared with the control group. MCE has not independently confirmed the accuraBiological Activity:Glukagon-like peptide 1 (1-37), human (TFA) is a highly potent agonist of the GLP-1 receptor... Read More | Inquire | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue StainingDescription:MCP-2 and CCL7 are two monocyte chemotactic proteins produced by human MG-63 osteosarcoma cells. Both MCP-2 and CCL7 are members of the C-C family of chemokines and share 62% and 71% amino acid sequence identity, Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue StainingDescription:MCP-2 and CCL7 are two monocyte chemotactic proteins produced by human MG-63 osteosarcoma cells. Both MCP-2 and CCL7 are members of the C-C family of chemokines and share 62% and 71% amino acid sequence identity, respectively, with MCP-1. CCL7 also shares 58% amino acid identity with MCP-2. CCL7 cDNA encodes a 99 amino acid residue precursor protein from which the N-terminal 23 amino acid residues are cleaved to generate the 76 amino acid residue mature CCL7. Mature CCL7 contains a potential N-linked and several possible O-linked glycosylation sites. Similarly to other C-C chemokines, all three MCP proteins are monocyte chemoattractants. In addition, the three MCPs can chemoattract activated NK cells as well as CD4+ and CD8+ T lymphocytes. All three cytokines have also been shown to attract eosinophils and induce histamine secretion from basophils... Read More | Purity>97% SDS-PAGE and HPLC analyses. FunctionLA-PF4 stimulates 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 Purity>97% SDS-PAGE and HPLC analyses. FunctionLA-PF4 stimulates 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 human 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) are chemoattractants and activators for neutrophils. TC-1 and TC-2 are antibacterial proteins, in vitro released from activated platelet alpha-granules. CTAP-III(1-81) is more potent than CTAP-III desensitize chemokine-induced neutrophil activation.Post-translationalProteolytic removal of residues 1-9 produces the active peptide connective tissue-activating peptide III (CTAP-III) (low-affinity platelet factor IV (LA-PF4)). Proteolytic removal of residues 1-13 produces the active peptide beta-thromboglobulin, which is released from platelets along with platelet factor 4 and platelet-derived growth factor. NAP-2(1-66) is produced by proteolytical processing, probably after secretion by leukocytes other than neutrophils. NAP-2(73) and NAP-2(74) seem not be produced by proteolytical processing of secreted precursors but are released in an active form from platelets... Read More | Purity≥95% SDS-PAGE.FunctionStimulates growth of the cells in an autocrine manner. Mediates hormonal action on the growth of cancer cells |