c-Abl [p Tyr412] Antibody Summary
| Immunogen |
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.
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| Modification |
p Tyr412
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| Localization |
Cytoplasmic and Nuclear
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| Specificity |
c-Abl [Tyr412]
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| Predicted Species |
Mouse (100%). Backed by our 100% Guarantee.
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| Clonality |
Polyclonal
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| Host |
Rabbit
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| Gene |
ABL1
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| Purity |
Immunogen affinity purified
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Applications/Dilutions
| Dilutions |
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| Application Notes |
WB: Use at a concentration of 0.1 – 1.0 ug/ml. Detects a band of approximately 140 kDa. Not tested in other applications.Optimal dilutions/concentrations should be determined by the end user.
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| Positive Control |
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| Publications |
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Reactivity Notes
Rat reactivity reported in the scientific literature (PMID: 23818519).
Packaging, Storage & Formulations
| Storage |
Store at -80C. Avoid freeze-thaw cycles.
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| Buffer |
Dulbeccos PBS (pH 7.3), 1.0 mg/ml and 50% Glycerol
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| Preservative |
0.05% Sodium Azide
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| Concentration |
0.5 mg/ml
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| Purity |
Immunogen affinity purified
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Alternate Names for c-Abl [p Tyr412] Antibody
- Abelson murine leukemia viral oncogene homolog 1
- ABL
- ABL1
- bcr/abl
- BCR-ABL1
- c-abl oncogene 1, non-receptor tyrosine kinase
- c-abl oncogene 1, receptor tyrosine kinase
- cAbl
- c-Abl
- EC 2.7.10
- EC 2.7.10.2
- JTK7
- JTK7bcr/abl
- p150bcr/c-abl oncogene protein
- Proto-oncogene c-Abl
- proto-oncogene tyrosine-protein kinase ABL1
- tyrosine-protein kinase ABL1
- v-abl Abelson murine leukemia viral oncogene homolog 1
- v-abl
Background
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.