蛋白名称
Tyrosine-protein kinase ABL2
免疫原
Purified recombinant fragment of Arg expressed in E. Coli.
特异性
Arg Monoclonal Antibody detects endogenous levels of Arg protein.
组成
Ascitic fluid containing 0.03% sodium azide,0.5% BSA, 50%glycerol.
稀释比例
Western Blot: 1/500 - 1/2000. Immunofluorescence: 1/200 - 1/1000. ELISA: 1/10000. Not yet tested in other applications.
纯化工艺
Affinity purification
其他名称
ABL2; ABLL; ARG; Abelson tyrosine-protein kinase 2; Abelson murine leukemia viral oncogene homolog 2; Abelson-related gene protein; Tyrosine-protein kinase ARG
背景
This gene encodes a member of the Abelson family of nonreceptor tyrosine protein kinases. The protein is highly similar to the c-abl oncogene 1 protein, including the tyrosine kinase, SH2 and SH3 domains, and it plays a role in cytoskeletal rearrangements through its C-terminal F-actin- and microtubule-binding sequences. This gene is expressed in both normal and tumor cells, and is involved in translocation with the ets variant 6 gene in leukemia. Multiple alternatively spliced transcript variants encoding different protein isoforms have been found for this gene. [provided by RefSeq, Nov 2009],
功能
catalytic activity:ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.,caution:The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.,cofactor:Magnesium or manganese.,enzyme regulation:Stabilized in the inactive form by an association between the SH3 domain and the SH2-TK linker region, interactions of the amino-terminal cap, and contributions from an amino-terminal myristoyl group and phospholipids. Activated by autophosphorylation as well as by SRC-family kinase-mediated phosphorylation. Activated by RIN1 binding to the SH2 and SH3 domains. Inhibited by imatinib mesylate (Gleevec) which is used for the treatment of chronic myeloid leukemia (CML).,function:Regulates cytoskeleton remodeling during cell differentiation, cell division and cell adhesion. Localizes to dynamic actin structures, and phosph
