C-X-C Motif Chemokine 7/CXCL7/NAP-2 Protein(C-6His) (recombinant human)

Protein Construction: Recombinant Human C-X-C Motif Chemokine 7 is produced by our Mammalian expression system and the target gene encoding Ser35-Asp128 is expressed with a 6His tag at the C-terminus. Sequence: Ser35-Asp128. Fusion tag: C-6His Endotoxin: < 1.0 EU per µg as determined by the LAL method. Apparent Molecular Mass: 12-16 kDa. Protein function: Human Chemokine (C-X-C motif) Ligand 7 (CXCL7), also known as neutrophil activating peptide 2 (NAP-2), is a member of the CXC chemokines containing an ELR domain (Glu-Leu-Arg tripeptide motif). Similar to other ELR domain containing CXC chemokines, such as IL-8 and the GRO proteins, CXCL7 binds CXCR2, chemoattracts and activates neutrophils. CXCL7, Connective Tissue Activating Protein III (CTAPIII) and ßthrombogulin (ßTG), are proteolytically processed carboxylterminal fragments of platelet basic protein (PBP) which is found in the alphagranules of human platelets. Although CTAPIII, ßTG, and PBP represent amino-terminal extended variants of NAP2 and possess the same CXC chemokine domains, these proteins do not exhibit CXCL7/NAP2 activity. CXCL7 induces cell migration through the G-protein-linked receptor CXCR-2. Protein function: LA-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. [The UniProt Consortium]