Preparation And Storage
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
The proto-oncogene c-abl was first isolated from the mouse genome as a gene with similarity to the v-abl oncogene of Abelson murine leukemia virus. The c-abl gene encodes a protein tyrosine kinase that is localized in the cytoplasm and nucleus. The c-abl protein shares several common features with other cytoplasmic tyrosine kinases, including the src-homology domains 2 (SH2) and 3 (SH3). The SH2 domain is believed to bind specifically to tyrosine residues of other proteins. The function of the SH3 domain is still unclear. Unique to the c-abl tyrosine kinase is a large C-terminal segment which seems to be essential for its biological function, since mice homozygous for a C-terminal deletion of c-abl have multiple defects at birth. The C-terminal fragment of c-abl contains a DNA-binding domain, and the DNA-binding affinity of this domain seems to be regulated by phosphorylation of critical serine/threonine residues. The c-abl proto-oncogene can be activated in a variety of ways. For example, in Philadelphia chromosome (Ph1)-positive leukemias the c-abl proto-oncogene on chromosome 9 becomes fused to the bcr gene on chromosome 22, and bcr-abl fusion proteins are produced. Ph1-positive cells express either the a-typical 210 kDa bcr-abl fusion protein or a smaller 185 kDa bcr-abl fusion protein. The bcr sequences activate the c-abl tyrosine kinase by deregulating its expression, and actin filament-binding function associated with c-abl is also activated. Expression of bcr-abl fusion proteins in vitro leads to transformation of pre-B lymphoid cells supporting their role as an oncogene. The phosphorylated form of c-abl is observed at ~145 kDa on SDS/PAGE. The 8E9 clone has been reported to react with an epitope in the tyrosine kinase domain of murine abl proteins [Wang et al.].
This antibody is routinely tested by western blot analysis. Other applications were tested at BD Biosciences Pharmingen during antibody development only or reported in the literature.
Development References (7)
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Guo JQ, Hirsch-Ginsberg CF, Xian YM, et al. Acute lymphoid leukemia molecular phenotype in a patient with benign-phase chronic myelogenous leukemia. Hematol Pathol. 1993; 7(2):91-106. (Clone-specific: Western blot). View Reference
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Guo JQ, Lian JY, Xian YM, et al. BCR-ABL protein expression in peripheral blood cells of chronic myelogenous leukemia patients undergoing therapy. Blood. 1994; 83(12):3629-3637. (Clone-specific: Western blot). View Reference
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Guo JQ, Wang JY, Arlinghaus RB. Detection of BCR-ABL proteins in blood cells of benign phase chronic myelogenous leukemia patients. Cancer Res. 1991; 51(11):3048-3051. (Clone-specific: Western blot). View Reference
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Kipreos ET, Lee GJ, Wang JY. Isolation of temperature-sensitive tyrosine kinase mutants of v-abl oncogene by screening with antibodies for phosphotyrosine. Proc Natl Acad Sci U S A. 1987; 84(5):1345-1349. (Clone-specific: Western blot). View Reference
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McWhirter JR, Wang JY. Activation of tyrosinase kinase and microfilament-binding functions of c-abl by bcr sequences in bcr/abl fusion proteins. Mol Cell Biol. 1991; 11(3):1553-1565. (Clone-specific: Immunofluorescence). View Reference
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McWhirter JR, Wang JY. An actin-binding function contributes to transformation by the Bcr-Abl oncoprotein of Philadelphia chromosome-positive human leukemias. EMBO J. 1993; 12(4):1533-1546. (Clone-specific: Immunofluorescence). View Reference
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Wang JY. Negative regulation of c-abl tyrosine kinase by its variable N-terminal amino acids. Oncogene Res. 1988; 3(3):293-298. (Clone-specific: Immunoprecipitation, Western blot). View Reference
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For Research Use Only. Not for use in diagnostic or therapeutic procedures.
