gro-2

C-X-C motif chemokine 2 (CXCL2,MIP-2) belongs to the intercrine alpha (chemokine CxC) family. It was originally identified as a heparin-binding protein secreted from a murine macrophage cell line in response to endotoxin stimulation. The expression of mouse MIP-2 is stimulated by endotoxin. The mouse MIP-2 shares approximately 63% aa sequence identity with murine KC, another mouse alpha chemokine, which is induced by PDGF. It has been suggested that mouse KC and MIP-2 are the homologs of the human GROs and rat CINCs. Chemotactic for human polymorphonuclear leukocytes but does not induce chemokinesis or an oxidative burst. The expression of MIP-2 was found to be associated with neutrophil influx in pulmonary inflammation and glomerulonephritis, suggesting that MIP-2 may contribute to the pathogenesis of inflammatory diseases.

GRO beta CXCL2 Protein, Rat, Recombinant is expressed in E. coli expression system. The predicted molecular weight is 7.6 kDa and the accession number is A6KKD4.

GRO beta CXCL2 Protein, Human, Recombinant is expressed in E. coli expression system. The predicted molecular weight is 7.9 kDa and the accession number is A0A024RDD9.

GRO beta CXCL2 Protein, Mouse, Recombinant (His & SUMO) is expressed in E. coli expression system with His and SUMO tag. The predicted molecular weight is 21.2 kDa and the accession number is P10889-1.

GRO beta CXCL2 Protein, Mouse, Recombinant (His) is expressed in yeast with His tag. The predicted molecular weight is 9.2 kDa and the accession number is P10889.

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 βthrombogulin (βTG), are proteolytically processed carboxylterminal fragments of platelet basic protein (PBP) which is found in the alphagranules of human platelets. Although CTAPIII, βTG, 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.