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The antiserum was produced against a chemically synthesized phosphopeptide derived from a region of human c-Abl 1b that contains tyrosine 412. Note: there are two widely expressed forms of c-Abl produced by alternative splicing, designated 1b (the more common form) and 1a. The corresponding phosphorylation site from 1a is tyrosine 393.
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. c-Abl becomes fully activated by sequential phosphorylation of tyrosines 412 and 245.
Our Abpromise guarantee covers the use of ab4717 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|WB||Use a concentration of 0.1 - 1 µg/ml. Detects a band of approximately 140 kDa.|
Fibroblasts transfected with oncogenic ∆SH3-Abl were resolved by SDS-PAGE on a 10% polyacrylamide gel and transferred to PVDF. Membranes were blocked with a 5% BSA-TBST buffer overnight at 4°C, then were incubated with 0.50