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C5240

Sigma-Aldrich

Anti-phospho-c-Abl (pTyr412) antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Synonym(s):

Anti-ABL, Anti-BCR-ABL, Anti-CHDSKM, Anti-JTK7, Anti-bcr/abl, Anti-c-ABL, Anti-c-ABL1, Anti-p150, Anti-v-abl

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.44

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

species reactivity

human

technique(s)

western blot: 1:1000 using fibroblasts transfected with oncogenic δSH3-Abl

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

phosphorylation (pTyr412)

Gene Information

human ... ABL1(25)

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.

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.

Physical form

Solution in Dulbecco′s phosphate buffered saline, pH 7.3, 50% glycerol,with 1 mg/mL BSA and 0.05% sodium azide

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.

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wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificates of Analysis (COA)

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Fabiola Rojas et al.
Frontiers in cellular neuroscience, 9, 203-203 (2015-06-25)
Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disease in which pathogenesis and death of motor neurons are triggered by non-cell-autonomous mechanisms. We showed earlier that exposing primary rat spinal cord cultures to conditioned media derived from primary mouse astrocyte
Jing Jin Gu et al.
Immunological reviews, 228(1), 170-183 (2009-03-18)
Stimulation of the T-cell antigen receptor (TCR) leads to the activation of signaling pathways that are essential for T-cell development and the response of mature T cells to antigens. The TCR has no intrinsic catalytic activity, but TCR engagement results
R Plattner et al.
Genes & development, 13(18), 2400-2411 (1999-09-29)
The c-Abl tyrosine kinase localizes to the cytoplasm and plasma membrane in addition to the nucleus. However, there is little information regarding a role for c-Abl in the cytoplasm/plasma membrane compartments. Here we report that a membrane pool of c-Abl
Jean Y J Wang
Nature cell biology, 6(1), 3-7 (2004-01-06)
Auto-inhibition describes the capacity of proteins to adopt a self-imposed latent conformation. Recently, a crystal structure of the Abl tyrosine kinase has revealed its ability to auto-inhibit. However, a separate body of work suggests that other cellular proteins also inhibit
Guilherme A P de Oliveira et al.
The Journal of biological chemistry, 288(39), 28331-28345 (2013-08-10)
c-Abl is a key regulator of cell signaling and is under strict control via intramolecular interactions. In this study, we address changes in the intramolecular dynamics coupling within the c-Abl regulatory unit by presenting its N-terminal segment (N-Cap) with an

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