E. coli-derived recombinant human CXCL12/SDF‑1 beta Lys22-Met93 Accession # P48061
Specificity
Detects human CXCL12/SDF-1 beta in ELISAs and Western blots. In sandwich ELISAs, less than 0.2% cross-reactivity with recombinant (rh) SDF‑1 alpha and recombinant mouse SDF‑1 alpha is observed.
Source
N/A
Isotype
IgG
Clonality
Polyclonal
Host
Goat
Gene
CXCL12
Purity Statement
Antigen Affinity-purified
Innovator's Reward
Test in a species/application not listed above to receive a full credit towards a future purchase.
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.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Preservative
No Preservative
Concentration
LYOPH
Reconstitution Instructions
Reconstitute at 0.2 mg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for CXCL12/SDF-1 beta Antibody [Biotin]
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.
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Salcedo, R. and J.J. Oppenheim (2003) Microcirculation 10:359.
Broxmeyer, H.E. et al. (2003) J. Leukoc. Biol. 73:630.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
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