Bad (S118) Blocking Peptide | BAD blocking peptide

Phospho-Bad(S118) Antibody Blocking peptide

• Gene Names: BAD; BBC2; BCL2L8
• Synonyms: Bad (S118); Phospho-Bad(S118) Antibody Blocking peptide; Bcl2-associated agonist of cell death; BAD; Bcl-2-binding component 6; Bcl-2-like protein 8; Bcl2-L-8; Bcl-xL/Bcl-2-associated death promoter; Bcl2 antagonist of cell death; BBC6; BCL2L8; BAD blocking peptide

• Specificity: The synthetic peptide sequence used to generate the antibody was selected from the region of human Phospho-Bad-S118. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
• Form/Format: The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.
• Sequence Length: 168

• Cellular Location: Mitochondrion outer membrane. Cytoplasm. Note: Upon phosphorylation, locates to the cytoplasm
• Tissue Location: Expressed in a wide variety of tissues.
• Preparation and Storage: Maintain refrigerated at 2-8 degree C for up to 6 months. For long term storage store at -20 degree C.

Related Product Information for BAD blocking peptide

Promotes cell death. Successfully competes for the binding to Bcl-X(L), Bcl-2 and Bcl-W, thereby affecting the level of heterodimerization of these proteins with BAX. Can reverse the death repressor activity of Bcl-X(L), but not that of Bcl-2 (By similarity). Appears to act as a link between growth factor receptor signaling and the apoptotic pathways.

NCBI and Uniprot Product Information

• NCBI GI #: 17371773
• NCBI GeneID: 572
• UniProt Accession #: Q92934; O14803; Q6FH21
• Molecular Weight: 18,392 Da
• NCBI Official Full Name: Bcl2-associated agonist of cell death
• NCBI Official Synonym Full Names: BCL2 associated agonist of cell death
• NCBI Official Symbol: BAD
• NCBI Official Synonym Symbols: BBC2; BCL2L8
• NCBI Protein Information: bcl2-associated agonist of cell death
• UniProt Protein Name: Bcl2-associated agonist of cell death
• Protein Family: Bcl2-associated agonist of cell death
• UniProt Gene Name: BAD
• UniProt Synonym Gene Names: BBC6; BCL2L8; BAD; Bcl2-L-8
• UniProt Entry Name: BAD_HUMAN

NCBI Description

The protein encoded by this gene is a member of the BCL-2 family. BCL-2 family members are known to be regulators of programmed cell death. This protein positively regulates cell apoptosis by forming heterodimers with BCL-xL and BCL-2, and reversing their death repressor activity. Proapoptotic activity of this protein is regulated through its phosphorylation. Protein kinases AKT and MAP kinase, as well as protein phosphatase calcineurin were found to be involved in the regulation of this protein. Alternative splicing of this gene results in two transcript variants which encode the same isoform. [provided by RefSeq, Jul 2008]

Uniprot Description

BAD: a proapoptotic member of the Bcl-2 family. Displaces Bax from binding to Bcl-2 and Bcl-xL, resulting in cell death. Survival factors such as IL-3 can inhibit the apoptotic activity of Bad inducing the phosphorylation of Bad by Akt and p90RSK. 14-3-3 proteins bind phosphorylated Bad, inhibiting its binding to Bcl-2 and Bcl-xL. Phosphorylation by mitochondria-anchored PKA in the BH3 domain can block the dimerization of Bad and Bcl-xL.

Protein type: Apoptosis

Chromosomal Location of Human Ortholog: 11q13.1

Cellular Component: cytosol; mitochondrial outer membrane; mitochondrion

Molecular Function: caspase activator activity; lipid binding; phospholipid binding; protein binding; protein kinase binding

Biological Process: ADP metabolic process; apoptosis; ATP metabolic process; caspase activation; glucose homeostasis; negative regulation of cytolysis; pore complex biogenesis; positive regulation of apoptosis; positive regulation of autophagy; positive regulation of caspase activity; positive regulation of epithelial cell proliferation; positive regulation of glucokinase activity; positive regulation of insulin secretion; positive regulation of proteolysis; protein insertion into mitochondrial membrane during induction of apoptosis; regulation of mitochondrial membrane permeability