Measured by its ability to chemoattract 5-10 day cultured human peripheral blood lymphocytes (PBL). The ED50 for this effect is 10-30 ng/mL. Measured by its ability to chemoattract BaF3 mouse pro‑B cells transfected with human CXCR4. The ED50 for this effect is 0.3-1.5 ng/mL.
Source
E. coli-derived CXCL12/SDF-1 beta protein Lys22-Met93
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Bioactivity2
Theoretical MW
8 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Publications
Read Publications using 351-FS/CF in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA.
Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human/Feline CXCL12/SDF-1 beta (aa 22-93), CF
CXCL12/SDF-1 beta
hSDF-1beta
SDF 1beta
SDF1 beta
SDF1b
Background
CXCL12, also known as SCYB12, PBSF and SDF-1 beta , is an 8.3 kDa, heparin-binding member of the CXC (or alpha-) family of chemokines (1, 2). Feline CXCL12( beta ) is synthesized as a 93 amino acid (aa) precursor that contains a 21 aa signal sequence and a 72 aa mature region (3). The mature molecule exhibits a typical three antiparallel beta -strand chemokine-like fold. There are no potential N-linked glycosylation sites. N-terminal aa’s 1-8 form a receptor binding site, while aa’s 1 and 2 (Lys-Pro) are involved in receptor activation (4). The C-terminus is likely associated with heparin binding (5). SDF-1 beta circulates and undergoes proteolytic processing. CD26 will remove the first two N-terminal amino acids, possibly creating a reduced-activity chemokine (5, 6). In addition to the beta -isoform, alternate splicing of the feline SDF-1 gene generates an alpha -isoform. The alpha isoform is identical to SDF-1 beta , but shorter by four aa’s at the C-terminus (3). Although alpha - and beta -isoforms show similar activity, SDF-1 alpha is differentially processed, and different cells secrete the two isoforms (5, 7). Mature feline SDF-1 beta is 96%, 97% and 100% aa identical to rat, mouse and human SDF-1 beta , respectively. Human (and by inference, feline) SDF-1 is active on mouse cells. SDF-1 alpha and beta are reported to be monomers at neutral pH and physiologic ionic strength (4). SDF-1 alpha is also reported to form dimers in the presence of heparansulfate (8). On the cell surface, this may well facilitate SDF-1 interaction with its two receptors, CXCR4 and syndecan-4 (9). Heparin sulfate is known to protect SDF-1 from proteolysis, and CXCR4 exists constitutively as a dimer (9-11). Among its many functions, CXCL12 is known to influence lymphopoiesis, regulate patterning and cell number of neural progenitors, and promote angiogenesis (12, 13). It also enhances the survival of myeloid progenitor cells.
Zlotnik, A. and O. Yoshie (2000) Immunity 12:121.
Rollins, B.J. (1997) Blood 90:909.
Nishimura, Y. et al. (1998) Eur. J. Immunogenet. 25:303.
Crump, M.P. et al. (1997) EMBO J. 16:6996.
Sierra, M.D. L. et al. (2004) Blood 103:2452.
Davis, D.A. et al. (2005) Blood 105:4561.
Stumm, R.K. et al. (2002) J. Neurosci. 22:5865.
Veldkamp, C.T. et al. (2005) Protein Sci. 14:1071.
Charnaux, N. et al. (2005) FEBS J. 272:1937.
Percherancier, Y. et al. (2005) J. Biol. Chem. 280:9895.
Babcock, G.J. et al. (2003) J. Biol. Chem. 278:3378.
Klein, R.S. et al. (2004) Trends Immunol. 25:306.
Salcedo, R. and J.J. Oppenheim (2003) Microcirculation 10:359.
Broxmeyer, H.E. et al. (2003) J. Leukoc. Biol. 73:630.
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