产品名称
BID, Caspase-8-cleaved from mouse, ≥95% (SDS-PAGE), recombinant, expressed in E. coli, buffered aqueous solution
recombinant
expressed in E. coli
assay
≥95% (SDS-PAGE)
form
buffered aqueous solution
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
Quality Level
Gene Information
mouse ... Bid(12122)
Analysis Note
Measured by its ability to induce cytochrome c release from isolated mouse liver mitochondria.
Biochem/physiol Actions
Caspase-8-cleaved BID relocates from the cytosol to the outer mitochondrial membrane where its interaction with Bak alters mitochondrial membrane permeability.
General description
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.
Physical form
0.2 μm filtered solution in 25 mM HEPES, pH 7.5, and 0.1 M KCl.
存储类别
10 - Combustible liquids
wgk
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
新产品
此项目有
J Zha et al.
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
M C Wei et al.
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
X Luo et al.
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
H Li et al.
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.
A Gross et al.
Genes & development, 13(15), 1899-1911 (1999-08-13)
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