Application

Anti-phospho-c-Abl [pTyr⁴¹²] may be used at a working dilultion of 1:1000 for immunoblotting in fibroblasts transfected with oncogenic δSH3-Abl. It may be used for immunodetection in HEK293 cells, cerebellar granule neuron cultures and primary cells from rat hippocampus. The antibody has been reported for immunoprecipitaion applications in HEK293T cells.

Disclaimer

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.

General description

c-Abl is a proto-oncogene of the Src family of non-receptor tyrosine kinases. It is a cellular homologue of Ablelson murine leukemia virus, and is implicated in many important cellular processes and tumorigenesis. In mammalian cells, c-Abl is expressed ubiquitously but its localization within a cell depends on the cell type and the environmental signals. c-Abl has distinct SH2 and SH3 domains that indicate high affinity for tyrosine and proline residues. Complete activation of c-Abl requires phosphorylation at two tyrosine residues at 412 and 245. Some of the downstream targets of c-Abl identified are ATM, DNA-PK, BRCA1, and transcription factors p73 and RFX1. Several reports implicate c-Abl in Apoptosis, DNA repair, T cell development and neuronal development. Anti-phospho-c-Abl [pTyr⁴¹²] specifically recognizes c-Abl phosphorylated at tyrosine 412 (~140-150 kDa). The antibody detects human c-Abl. Mouse c-Abl (100% homology) and rat c-Abl is expected to cross react.

Immunogen

synthetic phosphopeptide derived from the region of c-Abl that contains tyrosine 412.

Physical form

Solution in Dulbecco′s phosphate buffered saline (without Mg²⁺ and Ca²⁺), pH 7.3, 50% glycerol, with 1.0 mg/mL BSA (IgG and protease free) and 0.05% sodium azide.