SDF1 – Stromal Cell-Derived Factor 1α ( CXCL12) tested in migration, LPS-Free
Recombinant Stromal Cell-Derived Factor 1α (SDF-1α) is a 8 kDa chemokine protein expressed in many tissues and cell types.
The protein is almost identical (92% homology) in human, mouse and rat.
The chemokine SDF-1α binds to the chemokine receptor CXCR4 and plays an essential and unique role in homeostatic regulation of leukocyte traffic, hematopoiesis, organogenesis, cell differentiation and tissue regeneration (Murphy, 2002).
SDF-1α forms an heterocomplex with the alarmin HMGB1 (High Mobility Group 1) to promote the recruitment of cells via CXCR4 receptor.
It has the sequence:
Molecular Mass: Stromal Cell-Derived Factor 1α (SDF-1α, CXCL12) consists of 69 amino acid residues and has a calculated molecular mass of approximately 8 kDA
Purity: The purified protein is >95% homogeneous (electrophoresis and mass spectrometry). It contains no nucleic acids.
Endotoxin Level: The purified protein is free from LPS (Cambrex Limulus Amoebocyte Assay QCL-1000, <0.1 ng LPS per mg protein).
Activity: Measured by its ability to induce migration. Maximal activity in the cell migration assay is obtained at 1 nM.
Buffer: Stromal Cell-Derived Factor 1α (SDF-1α, CXCL12) is lyophilized from DPBS without Ca and Mg.
Storage: 2-8°C when lyophilized. The protein once reconstituted with water can be stored frozen (-20°C). Avoid repeated freezing and thawing.
This product is intended for research only, and cannot be used on humans.
Schiraldi et al (2012) HMGB1 promotes recruitment of inflammatory cells to damaged tissues by forming a complex with CXCL12 and signaling via CXCR4. J Exp Med. 2012: 551–563.