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

Antigen: BCL2-Associated Agonist of Cell Death (BAD)

Synonyms: BBC2, BCL2L8, wu:fa01b12, wu:fa96d04, MGC72439, BAD, MGC127164

Binding Site: BH3 Domain

Clonality: Polyclonal

Host: Rabbit

Reactivity: Human

Conjugate: Un-conjugated

Application: Western Blotting (WB), Immunohistochemistry (IHC), ELISA

Certificates: ISO 9001:2008

Catalog no.: ABIN388118

Additional Information

Alternative name: Bad

Gene ID: 572

UniProt: Q92934

Immunogen: This Bad BH3 Domain antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide selected within aa 100-130 (BH3 domain) of human Bad.

Isotype: Ig

Description: Other names: Bcl2-antagonist of cell death, BAD, Bcl-2 binding component 6, Bcl-XL/Bcl-2 associated death promoter, Bcl-2-like 8 protein

Characteristics: Purified Rabbit Polyclonal Antibody (Pab)

Specificity: This Bad BH3 Domain antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide selected within aa 100-130 (BH3 domain) of human Bad.

Molecular Weight: 18392 DA

Comments:

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.

Application Details

Application Notes: The suggested dilution will be: ELISA~~1:1,000 Western Blot~~ 1:100~500 Immunohistochemistry~~1:50~100

Concentration: 0.25 mg/ml

Purification: Purified

Buffer: Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein G column, eluted with high and low pH buffers and neutralized immediately, followed by dialysis against PBS.

Storage: Maintain refrigerated at 2-8 deg C for up to 6 months. For long term storage store at -20 deg C in small aliquots to prevent freeze-thaw cycles

Research Area: Apoptosis/Necrosis, Cell Signaling, Cell Structure, Cancer

Restrictions: For Research Use only

Images

Western blot analysis of Bad BH3 Domain antibody (ABIN388118) in mouse bladder tissue lysates (35ug/lane). Bad (arrow) was detected using the purified Pab.

Formalin-fixed and paraffin-embedded human cancer tissue reacted with the primary antibody, which was peroxidase-conjugated to the secondary antibody, followed by AEC staining. This data demonstrates the use of this antibody for immunohistochemistry. clinical relevance has not been evaluated. BC = breast carcinoma. HC = hepatocarcinoma.

Publications

Product: 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).