Bak Antibody (BH3 Domain Specific) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | Q16611 |
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Clone Names | 2011001 |
Gene ID | 578 |
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Other Names | Bcl-2 homologous antagonist/killer, Apoptosis regulator BAK, Bcl-2-like protein 7, Bcl2-L-7, BAK1, BAK, BCL2L7, CDN1 |
Target/Specificity | The synthetic peptide sequence used to generate the antibody AP1301a was selected from the region of human Bak BH3 Domain. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
Name | BAK1 |
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Synonyms | BAK, BCL2L7, CDN1 |
Function | Plays a role in the mitochondrial apoptotic process. Upon arrival of cell death signals, promotes mitochondrial outer membrane (MOM) permeabilization by oligomerizing to form pores within the MOM. This releases apoptogenic factors into the cytosol, including cytochrome c, promoting the activation of caspase 9 which in turn processes and activates the effector caspases. |
Cellular Location | Mitochondrion outer membrane; Single-pass membrane protein |
Tissue Location | Expressed in a wide variety of tissues, with highest levels in the heart and skeletal muscle |
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Provided below are standard protocols that you may find useful for product applications.
Background
BAK belongs to the BCL2 protein family. BCL2 family members form oligomers or heterodimers and act as anti- or pro-apoptotic regulators that are involved in a wide variety of cellular activities. BAK localizes to mitochondria, and functions to induce apoptosis. It interacts with and accelerates the opening of the mitochondrial voltage-dependent anion channel, which leads to a loss in membrane potential and the release of cytochrome c. This protein also interacts with the tumor suppressor P53 after exposure to cell stress.
References
Cartron, P.F., et al., Mol. Cell. Biol. 23(13):4701-4712 (2003).Mikhailov, V., et al., J. Biol. Chem. 278(7):5367-5376 (2003).Werner, A.B., et al., J. Biol. Chem. 277(25):22781-22788 (2002).Bellosillo, B., et al., Blood 100(5):1810-1816 (2002).Grutkoski, P.S., et al., Shock 17(1):47-54 (2002).
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