AFAP1L2 antibody was raised against a 15 amino acid peptide near the carboxy terminus of human AFAP1L2.
Features and Benefits
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Target description
AFAP1L2, also known as XB130, is structurally similar to actin-filament-associated protein (AFAP), containing several SH2- and SH3-binding motifs, two pleckstrin homology domains, a coiled-coil region, and many potential phosphorylation sites. It interacts with and is phosphorylated by c-Src tyrosine kinase. Suppression of AFAP1L2 via siRNA reduced Src activity, IL-8 production, EGF-induced phosphorylation of Akt and GSK3b, and altered cell cycles in human lung epithelial cells suggesting that AFAP1L2 plays a role as an adaptor in the regulation of Src signal transduction and multiple cellular functions. Recent experiments have shown that AFAP1L2 is highly expressed in thyroid and is the substrate RET/PTC kinase, a thyroid-specific kinase that plays a pathogenic role in papillary thyroid cancer. Down-regulation of AFAP1L2 in these cancer cells reduced Akt activity, inhibiting cell-cycle progression and cancer cell survival in suspension, indicating that AFAP1L2 may be a valuable target in thyroid cancer therapy. At least four isoforms of AFAP1L2 are known to exist.
Linkage
The action of this antibody can be blocked using blocking peptide SBP3500054.
Physical form
Supplied at approx. 1 mg/mL in phosphate buffered saline containing 0.02% sodium azide.
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