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.
면역원
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.
애플리케이션
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.
생화학적/생리학적 작용
Sorbin And SH3 Domain Containing 2 (SORBS2) acts as a potential link between Abl kinases and the actin cytoskeleton.
물리적 형태
Solution in 0.01M phosphate buffered saline pH 7.4, containing 15 mM sodium azide.
면책조항
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Sertoli cells are crucial for spermatogenesis in the seminiferous epithelium because their actin cytoskeleton supports vesicular transport, cell junction formation, protein anchoring, and spermiation. Here, we show that a junction-mediating and actin-regulatory protein (JMY) affects the blood-tissue barrier (BTB) function
Palladin (PALLD) belongs to the PALLD/myopalladin (MYPN)/myotilin family of actin-associated immunoglobulin-containing proteins in the sarcomeric Z-line. PALLD is ubiquitously expressed in several isoforms, and its longest 200 kDa isoform, predominantly expressed in striated muscle, shows high structural homology to MYPN.
Journal of the American Heart Association, 9(17), e017055-e017055 (2020-08-19)
Background Sorbs2b (sorbin and SH3 domain-containing 2b) was recently identified as a cardiomyopathy gene from a zebrafish mutagenesis screen. However, cardiac functions of its mammalian ortholog remain elusive. Methods and Results We conducted a detailed expression and subcellular localization analysis
There has not been a broad analysis of the combined effects of altered activities of microRNAs (miRNAs) in pancreatic ductal adenocarcinoma (PDAC) cells, and it is unclear how these might affect tumor progression or patient outcomes. We combined data from
The Journal of biological chemistry, 272(28), 17542-17550 (1997-07-11)
Arg and c-Abl represent the mammalian members of the Abelson family of protein-tyrosine kinases. A novel Arg/Abl-binding protein, ArgBP2, was isolated using a segment of the Arg COOH-terminal domain as bait in the yeast two-hybrid system. ArgBP2 contains three COOH-terminal