SORBS2 or ArgBP2 is an adapter protein that regulates actin-dependent cell adhesion and migration. ArgBP2 facilitates the ubiquitination and degradation of c-Abl. In heart muscle cells, ArgBP2 is localized at Z-disks of sarcomeres and may regulate elasticity of cardiac sarcomeres, whereas in the epithelial cells ArgBP2 may modulate the assembly of signaling complexes in stress fibers . Monoclonal Anti-SORBS2 antibody is specific for SORBS2 (85 kDa) in humans, rats, mice, dogs and hamsters. Staining of the SORBS2 band in immunoblotting is specifically inhibited with the immunizing peptide.
Sorbin And SH3 Domain Containing 2 (SORBS2), also known as ArgBP2, is an Arg/Abl binding protein. It contains an N-terminal sorbin homology (SoHo) domain, that interacts with lipid raft proteins, three C-terminal src homology 3 (SH3) domains, a Ser/Thr-rich domain and several potential Abl phosphorylation sites. SORBS2 associate is a substrate of Arg and v-Abl, which is phosphorylated on tyrosine in v-Abl-transformed cells. SORBS2 is widely expressed in human tissues and is particularly abundant in heart.
Immunogen
mouse myeloma cells and splenocytes from BALB/c mice immunized with a synthetic peptide corresponding to C- terminal region of human SORBS2 , conjugated to KLH.
Application
Monoclonal Anti-SORBS2 antibody is suitable for use in western blot (2-4 μg/mL using HeLa or NRK or 3T3 total cell extracts), immunocytochemistry, and immunoprecipitation.
Biochem/physiol Actions
Sorbin And SH3 Domain Containing 2 (SORBS2) acts as a potential link between Abl kinases and the actin cytoskeleton.
Physical form
Solution in 0.01M phosphate buffered saline pH 7.4, containing 15 mM sodium azide.
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