| Description | Purity >95% by SDS-PAGE, MW: 8 kDa (SDS-PAGE). SDF-1 a and SDF-1 Beta, members of the chemokine a subfamily that lack the ELR domain, were initially identified using the signal sequence trap cloning strategy from a mouse bone-marrow stromal cell line. SDF-1 a and SDF-1 Beta cDNAs encode precursor proteins of 89 and 93 amino acid residues, respectively. Both SDF-1 a 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 a. 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. Mice lacking SDF-1 or CXCR4 have been found to have impaired B-lymphopoiesis, myelopoiesis, vascular development, cardiogenesis and abnormal neuronal cell migration and patterning in the central nervous system. Recombinant Mouse SDF-1 a/CXCL12 produced in CHO cells is a polypeptide chain containing 68 amino acids. A fully biologically active molecule, rm SDF-1 Beta/CXCL12 has a molecular mass of 8 kDa analyzed by reducing SDS-PAGE and is obtained by chromatographic techniques. |
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| Other Names | CXCL12, C-X-C motif chemokine 12, HIRH, IRH, SDF-1, SDF-1b, SDF1A, SDF1B, TPAR1, TLSF-a, TLSF-b, SDF-1a, SDF1, Sdf1alpha, Stromal cell-derived factor 1, TLSF, HSDF-1, PBSF, SCYB12 |
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