AFAP1L2 / Unconjugated /

Product Details

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 GSK3beta, 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.
Conjugate	Unconjugated
Clone
Target Species	Human, Mouse, Rat
Applications	ELISA, WB, IHC
Supplier	Aviva Systems Biology
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About AFAP1L2
Enables SH2 domain binding activity; SH3 domain binding activity; and protein tyrosine kinase activator activity. Involved in several processes, including positive regulation of epidermal growth factor receptor signaling pathway; regulation of gene expression; and regulation of mitotic cell cycle. Located in cytosol and plasma membrane. [provided by Alliance of Genome Resources, Apr 2022]

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