Anti-SDF-1/CXCL12 Polyclonal Antibody is a Rabbit antibody targeting SDF-1/CXCL12. Anti-SDF-1/CXCL12 Polyclonal Antibody can be used in ELISA,IF,IHC-Fr,IHC-P,WB.

IgG

Human,Mouse (predicted:Rat,Chicken,Dog,Pig,GuineaPig,Rabbit)

Sample:
Lane 1: Mouse Liver tissue lysates
Lane 2: Human HT-1080 tissue lysates
Lane3: Human A549 cell lysates
Lane4: Human HeLa cell lysates
Lane 5: Human MCF-7 cell lysates
Lane 6: Human HepG2 cell lysates
Primary: Anti-CXCL12 (TMAB-01671) at 1/1000 dilution
Secondary: IRDye800CW Goat Anti-Rabbit IgG at 1/20000 dilution
Predicted band size: 8 kDa
Observed band size: 10 kDa

WB: 1:500-2000; IHC-P: 1:100-500; IHC-Fr: 1:100-500; IF: 1:50-200; ELISA: 1:5000-10000

Polyclonal

KLH conjugated synthetic peptide: human SDF-1/CXCL12

Human

CXCL12

Stromal cell-derived factor 1

Chemokines,Alpha Chemokines (CXC),Host Virus Interaction

Chemoattractant active on T-lymphocytes, monocytes, but not neutrophils. Activates the C-X-C chemokine receptor CXCR4 to induce a rapid and transient rise in the level of intracellular calcium ions and chemotaxis. Also binds to another C-X-C chemokine receptor CXCR7, which activates the beta-arrestin pathway and acts as a scavenger receptor for SDF-1. SDF-1-beta(3-72) and SDF-1-alpha(3-67) show a reduced chemotactic activity. Binding to cell surface proteoglycans seems to inhibit formation of SDF-1-alpha(3-67) and thus to preserve activity on local sites. Acts as a positive regulator of monocyte migration and a negative regulator of monocyte adhesion via the LYN kinase. Stimulates migration of monocytes and T-lymphocytes through its receptors, CXCR4 and CXCR7, and decreases monocyte adherence to surfaces coated with ICAM-1, a ligand for beta-2 integrins. SDF1A/CXCR4 signaling axis inhibits beta-2 integrin LFA-1 mediated adhesion of monocytes to ICAM-1 through LYN kinase. Inhibits CXCR4-mediated infection by T-cell line-adapted HIV-1. Plays a protective role after myocardial infarction. Induces down-regulation and internalization of CXCR7 expressed in various cells.