BCL2-Associated Agonist of Cell Death (BAD) (BH3 Domain) Peptide

Details for Product No. ABIN691159
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Protein Name
Synonyms BBC2, BCL2L8, Bbc2, AI325008, bad, fa01b12, wu:fa01b12, wu:fa96d04, BAD
Protein Region
BH3 Domain
Application
Blocking Peptide (BP)
Pubmed 3 references available
Catalog no. ABIN691159
Quantity 0.1 mg
Price
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Immunogen Synthetic peptide
Specificity The synthetic peptide sequence used to generate the antibody AP1322a was selected from the region of human Bad BH3 Domain. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
Alternative Name Bad
Background Apoptosis or programmed cell death is a physiological cellular process characterized by cell shrinkage, membrane blebbing, DNA fragmentation, and release of Cytochrome C from the mitochondria. It is utilized by the organism to get rid of unwanted cells, which is critical for normal development and homeostasis of an organism. Disregulation of normal apoptosis process have been implicated in a variety of diseases, including cancer, autoimmune diseases, viral infections, etc. Programmed cell death occurs through complex cascades of cell signaling in which Bcl-2 family members, among others, play an important role.The Bcl-2 family of proteins regulate apoptosis as well as execute death signals at the mitochondrion. Members of this family include both pro- and anti-apoptotic proteins that hare homology sequences called Bcl-2 Homology domains (BH1-4) which mediate dimmer formation. The BH3 proteins, such as BID, NOXA, PUMA, BIK, BIM and BAD are all pro-apoptotic and share sequence homology within the amphipathic alpha-helical BH3 region, which is required for their apoptotic function. They may trigger release of death-inducing molecules such as Cytochrome C, Smac, and endonuclease G. Anti-apoptotic family members, including Bcl-2 and Bcl-XL, play inhibitory roles. Bcl-2 family proteins may form homodimers or heterodimers between pro- and anti-apoptotic members, the ratios of which determine the cell fate.
Comment

Background: Apoptosis or programmed cell death is a physiological cellular process characterized by cell shrinkage, membrane blebbing, DNA fragmentation, and release of Cytochrome C from the mitochondria. It is utilized by the organism to get rid of unwanted cells, which is critical for normal development and homeostasis of an organism. Disregulation of normal apoptosis process have been implicated in a variety of diseases, including cancer, autoimmune diseases, viral infections, etc. Programmed cell death occurs through complex cascades of cell signaling in which Bcl-2 family members, among others, play an important role.The Bcl-2 family of proteins regulate apoptosis as well as execute death signals at the mitochondrion. Members of this family include both pro- and anti-apoptotic proteins that hare homology sequences called Bcl-2 Homology domains (BH1-4) which mediate dimmer formation. The BH3 proteins, such as BID, NOXA, PUMA, BIK, BIM and BAD are all pro-apoptotic and share sequence homology within the amphipathic alpha-helical BH3 region, which is required for their apoptotic function. They may trigger release of death-inducing molecules such as Cytochrome C, Smac, and endonuclease G. Anti-apoptotic family members, including Bcl-2 and Bcl-XL, play inhibitory roles. Bcl-2 family proteins may form homodimers or heterodimers between pro- and anti-apoptotic members, the ratios of which determine the cell fate.

Restrictions For Research Use only
Storage 4 °C/-20 °C
Storage Comment Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles
Expiry Date 6 months
Background publications Mabuchi, Ohmichi, Kimura et al.: "Inhibition of phosphorylation of BAD and Raf-1 by Akt sensitizes human ovarian cancer cells to paclitaxel." in: The Journal of biological chemistry, Vol. 277, Issue 36, pp. 33490-500, 2002 (PubMed).

Cowburn, Cadwallader, Reed et al.: "Role of PI3-kinase-dependent Bad phosphorylation and altered transcription in cytokine-mediated neutrophil survival." in: Blood, Vol. 100, Issue 7, pp. 2607-16, 2002 (PubMed).

Won, Kim, La et al.: "Cleavage of 14-3-3 protein by caspase-3 facilitates bad interaction with Bcl-x(L) during apoptosis." in: The Journal of biological chemistry, Vol. 278, Issue 21, pp. 19347-51, 2003 (PubMed).

Reactivities (9), (2)
Request Want additional data for this product?

The Independent Validation Initiative strives to provide you with high quality data. Find out more

Order hotline:

  • +1 404 474 4654
  • +1 888 205 9894 (TF)
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