
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:
[“MKPVSLSYRCPCRFFESHVARANVKHLKILNTPNCALQIVARLKNNNRQVCIDPKLKWIQEYLEKALNK”]
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.
References:
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.