CXCL12β-1

hSDF-1 beta, IRH, hIRH, PBSF

CXCL12, also known as SDF-1, is a heparin-binding member of the CXC (or alpha-) family of chemokines. SDF-1 alpha and SDF-1 beta are the first cytokines 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. CXCL12β is synthesized as a 93 amino acid (aa) precursor that contains a 21 aa signal sequence and a 72 aa mature region. The mature molecule exhibits a typical three antiparallel beta -strand chemokine-like fold. There are no potential N-linked glycosylation sites. The C-terminus is likely associated with heparin binding. SDF-1 beta circulates and undergoes proteolytic processing. CD26 will remove the first two N-terminal amino acids, possibly creating a reduced-activity chemokine. On the cell surface, the receptor for this chemokine is CXCR4 and syndecan4. Among its many functions, CXCL12 is known to influence lymphopoiesis, regulate patterning and cell number of neural progenitors, and promote angiogenesis. It also enhances the survival of myeloid progenitor cells.

Approximately 8.5 kDa.

Sterile Filtered White lyophilized (freeze-dried) powder.

> 97% by SDS-PAGE and HPLC analyses.