Description
Macrophage inflammatory protein-2(MIP-2) was originally identified as a heparin binding protein secreted from a murine macrophage cell line in response to endotoxin stimulation. The protein is produced by a variety of cell types, including intestinal epithelium, macrophages, astrocytes and fibroblasts. Homologs of the mouse MIP-2 have been identified in human, rat and cotton rat. MIP-2 is an ELR-containing member of the alpha (CXC) subfamily of chemokines. The cotton rat MIP-2 gene encodes a 101 amino acid (aa) residue precursor protein with a 28 aa putative signal peptide that is cleaved to generate the 73 aa mature protein. Mature cotton rat MIP-2 has two intrachain disulfide bonds and no potential glycosylation sites. It shares approximately 79% and 85% aa sequence identity with rat CINC-3 and mouse MIP-2, respectively. MIP-2 is a potent neutrophil attractant and activator. MIP-2 binds and activates the chemokine receptor CXCR-2. The recombinant cotton rat MIP-2 has been shown to bind and activate the human CXCR-2