Purified from rabbit serum by sequential epitope-specific chromatography. The antibody has been negatively preadsorbed using a non-phosphopeptide corresponding to the site of phosphorylation to remove antibody that is reactive with non-phosphorylated c-Abl. The final product is generated by affinity chromatography using a c-Abl -derived peptide that is phosphorylated at tyrosine 245.
c-Abl is a 140-150 kDa non-receptor protein tyrosine kinase whose precise functions are not known, but roles for Abl in growth factor and integrin signaling, cell cycle regulation, cytoskeletal reorganization, neurogenesis, and responses to DNA damage and oxidative stress have been suggested. c-Abl kinase activity is increased in vivo by diverse physiological stimuli including ionizing radiation, entry into S phase, integrin activation, and platelet-derived growth factor (PDGF) stimulation. c-Abl contains various protein binding domains that appear to enable it to regulate the functions of many proteins by forming complexes, most notably three isoforms of the oncogenic protein BCR/ABL. Tyrosine 245 is involved in the activation of c-Abl kinase activity, and phosphorylated by Src after PDGF stimulation.
The antiserum was produced against a chemically synthesized phosphopeptide derived from a region of human c-Abl that contains tyrosine 245. Note: there are two widely expressed forms of c-Abl produced by alternative splicing, known as 1a and 1b (the more commonly used form). The corresponding phosphorylation site from 1a is tyrosine 226.
Fibroblasts transfected with oncogenic ?SH3-Abl.
Provided as solution in phosphate buffered saline, pH 7.3, with 1% BSA and 0.08% sodium azide
Product should be stored at -80ºC. Aliquot to avoid freeze/thaw cycles
1. Cong, F., et al. (2002) Interaction between UV-damaged DNA binding activity proteins and the c-Abl tyrosine kinase. J. Biol. Chem. 277(38):34870-34878.2. Furstoss, O., et al. (2002) c-Abl is an effector of Src for growth factor-induced c-myc expression and DNA synthesis. EMBO J. 21(4):514-524.3. Brasher, B.B. and R.A. Van Etten (2000) c-Abl has high intrinsic tyrosine kinase activity that is stimulated by mutation of the Src homology 3 domain and by autophosphorylation at two distinct regulatory tyrosines. J. Biol. Chem. 275(45):35631-35637.4. Plattner, R., et al. (1999) c-Abl is activated by growth factors and Src family kinases and has a role in the cellular response to PDGF. Genes Dev. 13(18):2400-2411.