IP-10 was originally identified as an IFN-g-inducible gene in monocytes, fibroblasts and endothelial cells. It has since been shown that IP-10 mRNA is also induced by LPS, IL-1b, TNF-a, IL-12 and viruses. Additional cell types that have been shown to express IP-10 include activated T-lymphocytes, splenocytes, keratinocytes, osteoblasts, astrocytes and smooth muscle cells. IP-10 is also expressed in psoriatic and lepromatous lesions of skin. The mouse homologue of human IP-10, Crg-2, has been cloned and shown to share approximately 67% amino acid sequence identity with human IP-10. Human IP-10 cDNA encodes a 98 amino acid (aa) residue precursor protein with a 21 aa residue signal peptide that is cleaved to form the 77 aa residue secreted protein. The amino acid sequence of IP-10 identified the protein as a member of the chemokine a family that lacks the ELR domain. IP-10 has been shown to be a chemoattractant for activated T-lymphocytes. Recently, IP-10 has been reported to be a potent inhibitor of angiogenesis and to display a potent thymus-dependent antitumor effect. A chemokine receptor specific for IP-10 and Mig has been cloned and shown to be highly expressed in IL-2-activated T-lymphocytes.

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