Human CXCL9/MIG PE‑conjugated Antibody

CXCL9, a member of the alpha  subfamily of chemokines that lack the ELR domain, was initially identified as a lymphokine-activated gene in mouse macrophages. Human CXCL9 was subsequently cloned using mouse MIG cDNA as a probe. The CXCL9 gene is induced in macrophages and in primary glial cells of the central nervous system specifically in response to IFN-gamma. CXCL9 has been shown to be a chemoattractant for activated T-lymphocytes and TIL but not for neutrophils or monocytes. The human CXCL9 cDNA encodes a 125 amino acid (aa) residue precursor protein with a 22 aa residue signal peptide that is cleaved to yield a 103 aa residue mature protein. CXCL9 has an extended carboxy-terminus containing greater than 50% basic aa residues and is larger than most other chemokines. The carboxy-terminal residues of CXCL9 are prone to proteolytic cleavage resulting in size heterogeneity of natural and recombinant CXCL9. CXCL9 with large carboxy-terminal deletions have been shown to have diminished activity in the calcium flux assay. CXCL9 is a homodimer and will heterodimerize with CXCL12. It is reported to bind to CXCR3, CXCR6 and CCR3. Over amino acids (aa) 23-125, human and mouse CXCl9 share 67% aa sequence identity.