Thymus Chemokine-1, also called Chemokine (C-X-C motif) ligand 7 (CXCL7) , is a member of the CXC chemokines. Similar to other ELR domain containing CXC chemokines such as IL-8 and the GRO proteins, Thymus Chemokine-1 has been shown to bind CXCR-2 and be a chemoattractant forneutrophils and play a role in their activation. Although CTAP-III, ß-TG and PBP represent amino-terminal extended variants of Thymus Chemokine-1 and possess the same CXC chemokine domains, these proteins do not exhibit Thymus Chemokine-1 activity. Recently, it has been shown that the additional amino-terminal residues of CTAP-III mask the critical ELR receptor binding domain that is exposed on Thymus Chemokine-1 and may account for lack of Thymus Chemokine-1 activity. Rat CXCL7 shares 72% amino acid sequence identity with mouse CXCL7.
Recombinant rat Thymus Chemokine-1/ CXCL7 produced in CHO cells is a polypeptide chain containing 62 amino acids. A fully biologically active molecule, rrThymus Chemokine-1/CXCL7 has a molecular mass of 9.8 kDa analyzed by reducing SDS-PAGE and is obtained by chromatographic techniques at GenScript.