Recombinant Human CXCL9/MIG is a single non-glycosylated polypeptide chain containing 103 amino acids.
Background: CXCL9, a member of the α subfamily of chemokines that lack the ELR domain, was initially identified as a lymphokine activated gene in mouse macrophages. 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 residue precursor protein with a 22 amino acid residue signal peptide that is cleaved to yield a 103 amino acid residue mature protein. CXCL9 has an extended carboxy-terminus containing greater than 50% basic amino acid residues and is larger than most other chemokines. A chemokine receptor (CXCR3) specific for CXCL9 and IP-10 has recently been cloned and shown to be highly expressed in IL-2-activated T-lymphocytes.
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