A target of NESH-SH3/Abi3bp (TARSH) was originally identified as an SH3 domain-binding molecule of the NESH-SH3/Abi3 protein that is involved in Rac-dependent actin polymerization. In recent studies, TARSH gene expression was dramatically induced in mouse embryonic fibroblasts (MEFs) replicative senescence and suppressed in human lung carcinoma specimens and thyroid carcinomas. However, the molecular mechanism underlying the regulation of TARSH in tumorigenesis remains unclear.
ABL1/2 Antibody detects endogenous levels of total ABL1/2.
c-Abl belongs to the class of tyrosine kinases and is the prototype of a subfamily which includes two members, c-Abl and Arg (Abl-related gene). Both proteins are localized at the cell membrane, actin cytoskeleton and cytosol, and c-Abl is present in the nucleus as well. c-Abl is a non-receptor tyrosine kinase that participates in multiple signaling pathways linking the cell surface, cytoskeleton, and the nucleus. Recent in vitro studies have also linked c-Abl to amyloid-beta-induced toxicity and tau phosphorylation. c-Abl has been implicated in many cellular processes including differentiation, division, adhesion, death, and stress response. c-Abl is a latent tyrosine kinase that becomes activated in response to numerous extra- and intra-cellular stimuli. The c-Abl protein is a ubiquitously expressed nonreceptor tyrosine kinase involved in the development and function of many mammalian organ systems, including the immune system and bone. It regulates the cellular response to TAM through functional interaction with the estrogen receptor, which suggests c-Abl as a therapeutic target and a prognostic tumor marker for breast cancer. c-Abl also plays a key role in signaling chemokine-induced T-cell migration. In addition, c-Abl contains NLSs (nuclear localization signals) and DNA-binding sequences important for nuclear functions. c-Abl has become an important therapeutic target in human chronic myeloid leukaemia.
ABLIM1 Antibody detects endogenous levels of total ABLIM1.
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