C4733
BID, Caspase-8-cleaved from mouse
≥95% (SDS-PAGE), recombinant, expressed in E. coli, buffered aqueous solution
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About This Item
Prodotti consigliati
Ricombinante
expressed in E. coli
Livello qualitativo
Saggio
≥95% (SDS-PAGE)
Forma fisica
buffered aqueous solution
N° accesso UniProt
Condizioni di spedizione
dry ice
Temperatura di conservazione
−20°C
Informazioni sul gene
mouse ... Bid(12122)
Descrizione generale
Mouse BID cleaved with caspase-8 generates the amino-terminal fragment (amino acids 1-59, 7 kDa) and the carboxy-terminal fragment (amino acids 60-195, 15 kDa). On size exclusion chromatography cleaved BID elutes at 27 kDa indicating that the fragments remain associated.
Azioni biochim/fisiol
Caspase-8-cleaved BID relocates from the cytosol to the outer mitochondrial membrane where its interaction with Bak alters mitochondrial membrane permeability.
Stato fisico
0.2 μm filtered solution in 25 mM HEPES, pH 7.5, and 0.1 M KCl.
Risultati analitici
Measured by its ability to induce cytochrome c release from isolated mouse liver mitochondria.
Codice della classe di stoccaggio
10 - Combustible liquids
Classe di pericolosità dell'acqua (WGK)
nwg
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°C)
Not applicable
Certificati d'analisi (COA)
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Genes & development, 14(16), 2060-2071 (2000-08-19)
TNFR1/Fas engagement results in the cleavage of cytosolic BID to truncated tBID, which translocates to mitochondria. Immunodepletion and gene disruption indicate BID is required for cytochrome c release. Surprisingly, the three-dimensional structure of this BH3 domain-only molecule revealed two hydrophobic
Science (New York, N.Y.), 290(5497), 1761-1765 (2000-12-02)
Many apoptotic molecules relocate subcellularly in cells undergoing apoptosis. The pro-apoptotic protein BID underwent posttranslational (rather than classic cotranslational) N-myristoylation when cleavage by caspase 8 caused exposure of a glycine residue. N-myristoylation enabled the targeting of a complex of p7
Cell, 94(4), 481-490 (1998-09-04)
We report here the purification of a cytosolic protein that induces cytochrome c release from mitochondria in response to caspase-8, the apical caspase activated by cell surface death receptors such as Fas and TNF. Peptide mass fingerprinting identified this protein
Cell, 94(4), 491-501 (1998-09-04)
We report here that BID, a BH3 domain-containing proapoptotic Bcl2 family member, is a specific proximal substrate of Casp8 in the Fas apoptotic signaling pathway. While full-length BID is localized in cytosol, truncated BID (tBID) translocates to mitochondria and thus
BCL-2 family members and the mitochondria in apoptosis.
Genes & development, 13(15), 1899-1911 (1999-08-13)
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