protein

BID Protein, Mouse (His-GST)

HY-P72852

5 μg;10 μg;50 μg;100 μg;500 μg;1 mg

50;85;235;400;900;1530 USD

BID Protein, Mouse (His-GST)

proteins

E. coli

5 μg;10 μg;50 μg;100 μg;500 μg;1 mg

50;85;235;400;900;1530 USD

BID Protein, a pro-apoptotic member of the Bcl-2 family, is initially discovered through binding to both pro-apoptotic Bax and anti-apoptotic Bcl-2. BID is activated in the BCL-2-regulated or mitochondrial apoptosis pathway and acts as a switch between the extrinsic and intrinsic cell death pathways. BID is susceptible to proteolytic cleavage by caspases, calpains, Granzyme B and cathepsins. BID Protein, Mouse (His-GST) is the recombinant mouse-derived BID protein, expressed by E. coli , with N-His, N-GST labeled tag. The total length of BID Protein, Mouse (His-GST) is 195 a.a., with molecular weight of ~48 kDa.

Mouse

BH3-interacting domain death agonist (BID), a pro-apoptotic member of the Bcl-2 family, is initially discovered through binding to both pro-apoptotic Bax and anti-apoptotic Bcl-2. BID is activated in the BCL-2-regulated or mitochondrial apoptosis pathway and acts as a switch between the extrinsic and intrinsic cell death pathways. During apoptosis, BID can be cleaved not only by caspase-8 during death receptor apoptotic signaling, but also by other caspases, granzyme B, calpains and cathepsins. Protease-cleaved BID migrates to mitochondria where it induces permeabilization of the outer mitochondrial membrane that is dependent on the pro-apoptotic proteins Bax and/or Bak, and thus BID acts as a sentinel for protease-mediated death signals [1] [2] .

BH3-interacting domain death agonist; BID; p15 BID

Greater than 95% as determined by reducing SDS-PAGE

Lyophilized from a 0.22 μm filtered solution of 20 mM PB, 150 mM NaCl, pH 7.4.

Room temperature in continental US; may vary elsewhere.