Recombinant Active Protein
Stromal-Derived Factor (SDF-1) is a chemoattractant active on T-lymphocytes and monocytes, but not neutrophils. This cytokine activates the C-X-C chemokine receptor CXCR4 to induce a rapid and transient rise in the level of intracellular calcium ions and chemotaxis. SDF-1-alpha (3-67) and SDF-1-beta (3-72) show a reduced chemotactic activity. Binding to cell surface proteoglycans inhibits formation of SDF-1-alpha (3-67), preserving the activity of SDF-1 on local sites. SDF-2 acts as a positive regulator of monocyte migration and a negative regulator of monocyte adhesion via the Lyn kinase SDF-1 stimulates migration of monocytes through its receptor, CXCR4, and decreases monocyte adherence to surfaces coated with ICAM-1, a ligand for beta-2 integrins. Recombinant Human SDF-1 produced in E. coli is a non-glycosylated polypeptide chain containing 68 amino acids with a MW of 8,008 Da.