Bcl-2 (124) Mouse mAb (BSA and Azide Free) #17447
- WB
- IHC
- F
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 26 |
| Source/Isotype | Mouse IgG1 |
Application Key:
- WB-Western Blotting
- IHC-Immunohistochemistry
- F-Flow Cytometry
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
This product is the carrier-free version of product #15071. All data were generated using the same antibody clone in the standard formulation which contains BSA and glycerol.
This formulation is ideal for use with technologies requiring specialized or custom antibody labeling, including fluorophores, metals, lanthanides, and oligonucleotides. It is not recommended for ChIP, ChIP-seq, CUT&RUN, or CUT&Tag assays. If you require a carrier-free formulation for chromatin profiling, please contact us. Optimal dilutions/concentrations should be determined by the end user.
Formulation
Supplied in 1X PBS, BSA and Azide Free.
For standard formulation of this product see product #15071.
Storage
Specificity / Sensitivity
Bcl-2 (124) Mouse mAb (BSA and Azide Free) recognizes endogenous levels of total Bcl-2 protein.
Species Reactivity:
Human
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gly47 of human Bcl-2 protein.
Background
Bcl-2 exerts a survival function in response to a wide range of apoptotic stimuli through inhibition of mitochondrial cytochrome c release (1). It has been implicated in modulating mitochondrial calcium homeostasis and proton flux (2). Several phosphorylation sites have been identified within Bcl-2, including Thr56, Ser70, Thr74, and Ser87 (3). It has been suggested that these phosphorylation sites may be targets of the ASK1/MKK7/JNK1 pathway and that phosphorylation of Bcl-2 may be a marker for mitotic events (4,5). Mutation of Bcl-2 at Thr56 or Ser87 inhibits its anti-apoptotic activity during glucocorticoid-induced apoptosis of T lymphocytes (6). Interleukin-3 and JNK-induced Bcl-2 phosphorylation at Ser70 may be required for its enhanced anti-apoptotic functions (7).
- Murphy, K.M. et al. (2000) Cell Death Differ 7, 102-11.
- Zhu, L. et al. (1999) J Biol Chem 274, 33267-73.
- Maundrell, K. et al. (1997) J Biol Chem 272, 25238-42.
- Yamamoto, K. et al. (1999) Mol Cell Biol 19, 8469-78.
- Ling, Y.H. et al. (1998) J Biol Chem 273, 18984-91.
- Huang, S.T. and Cidlowski, J.A. (2002) FASEB J 16, 825-32.
- Deng, X. et al. (2001) J Biol Chem 276, 23681-8.
Limited Uses
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