Bid (S65) Blocking Peptide | BID blocking peptide

Phospho-Bid(S65) Antibody Blocking peptide

• Gene Names: BID; FP497
• Synonyms: Bid (S65); Phospho-Bid(S65) Antibody Blocking peptide; BH3-interacting domain death agonist; p22 BID; BID; BH3-interacting domain death agonist p15; p15 BID; BH3-interacting domain death agonist p13; p13 BID; BH3-interacting domain death agonist p11; p11 BID; BID blocking peptide

• Specificity: The synthetic peptide sequence used to generate the antibody was selected from the region of human Phospho-Bid-S65. 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: 195

• Cellular Location: Cytoplasm. Mitochondrion membrane. Note: When uncleaved, it is predominantly cytoplasmic. BH3-interacting domain death agonist p13: Mitochondrion membrane. Note: Associated with the mitochondrial membrane. Isoform 3: Cytoplasm.
• Tissue Location: Isoform 2 and isoform 3 are expressed in spleen, bone marrow, cerebral and cerebellar cortex. Isoform 2 is expressed in spleen, pancreas and placenta (at protein level) Isoform 3 is expressed in lung, pancreas and spleen (at protein level). Isoform 4 is expressed in lung and pancreas (at protein level).
• 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 BID blocking peptide

The major proteolytic product p15 BID allows the release of cytochrome c (By similarity). Isoform 1, isoform 2 and isoform 4 induce ICE-like proteases and apoptosis. Isoform 3 does not induce apoptosis. Counters the protective effect of Bcl-2.

NCBI and Uniprot Product Information

• NCBI GI #: 2493285
• NCBI GeneID: 637
• UniProt Accession #: P55957; Q549M7; Q71T04; Q7Z4M9; Q8IY86
• Molecular Weight: 11,263 Da
• NCBI Official Full Name: BH3-interacting domain death agonist
• NCBI Official Synonym Full Names: BH3 interacting domain death agonist
• NCBI Official Symbol: BID
• NCBI Official Synonym Symbols: FP497
• NCBI Protein Information: BH3-interacting domain death agonist
• UniProt Protein Name: BH3-interacting domain death agonist
• Protein Family: BH3-interacting domain death agonist
• UniProt Gene Name: BID
• UniProt Synonym Gene Names: BID
• UniProt Entry Name: BID_HUMAN

NCBI Description

This gene encodes a death agonist that heterodimerizes with either agonist BAX or antagonist BCL2. The encoded protein is a member of the BCL-2 family of cell death regulators. It is a mediator of mitochondrial damage induced by caspase-8 (CASP8); CASP8 cleaves this encoded protein, and the COOH-terminal part translocates to mitochondria where it triggers cytochrome c release. Multiple alternatively spliced transcript variants have been found, but the full-length nature of some variants has not been defined. [provided by RefSeq, Jul 2008]

Uniprot Description

BID: a pro-apoptotic member of the Bcl-2 superfamily. Targets intracellular membranes and contains a BH3 death domain. Heterodimerizes with either the pro-apoptotic protein BAX or the anti-apoptotic protein BCL2, antagonizing its protective effect. The activity of BID is regulated by Caspase 8-mediated cleavage, exposing the BH3 domain and significantly changing the surface charge and hydrophobicity, causing translocation to mitochondria where it triggers cytochrome c release. Multiple alternatively spliced variants have been found.

Protein type: Mitochondrial; Apoptosis

Chromosomal Location of Human Ortholog: 22q11.1

Cellular Component: cytosol; membrane; mitochondrial outer membrane; mitochondrion

Molecular Function: death receptor binding; protein binding

Biological Process: apoptotic mitochondrial changes; DNA damage response, signal transduction; induction of apoptosis via death domain receptors; neuron apoptosis; positive regulation of apoptosis; positive regulation of protein homooligomerization; positive regulation of protein oligomerization; regulation of apoptosis; release of cytochrome c from mitochondria