Recombinant Rat CXCL12/SDF-1 alpha is a single non-glycosylated polypeptide chain containing 68 amino acids.
Background: SDF-1 alpha and SDF-1 beta, members of the chemokine alpha subfamily that lack the ELR domain, were initially identified using the signal sequence trap cloning strategy from a mouse bone-marrow stromal cell line. These proteins were subsequently also cloned from a human stromal cell line as cytokines that supported the proliferation of a stromal cell-dependent pre-B-cell line. SDF-1 alpha and SDF-1 beta cDNAs encode precursor proteins of 89 and 93 amino acid residues, respectively. Both SDF-1 alpha and SDF-1 beta are encoded by a single gene and arise by alternative splicing. The two proteins are identical except for the four amino acid residues that are present in the carboxy-terminus of SDF-1 beta and absent from SDF-1 alpha. SDF-1/PBSF is highly conserved between species, with only one amino acid substitution between the mature human and mouse proteins. SDF-1/PBSF acts via the chemokine receptor CXCR4 and has been shown to be a chemoattractant for T-lymphocytes, monocytes, pro- and pre- B cells, but not neutrophils.
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