tBID Mouse
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Description
Product Specs
BID itself belongs to the Bcl-2 protein family and plays a role in apoptosis with only its BH3 domain. When apoptosis signaling occurs, BID interacts with Bax, another Bcl-2 family member involved in cell death regulation. They form a heterodimer, leading to Bax's insertion into the outer membrane of mitochondria. Bax then prompts the opening of the mitochondrial voltage-dependent anion channel. This action releases cytochrome c and other pro-apoptotic factors from the mitochondria, ultimately activating caspases. BID mediates the mitochondrial damage caused by caspase-8 (CASP8). CASP8 cleaves BID, and the COOH-terminal part moves to the mitochondria, initiating cytochrome c release. The primary proteolytic product, p15 BID, is responsible for releasing cytochrome c. Isoforms 1, 2, and 4 of BID induce ice-like proteases and apoptosis, while Isoform 3 does not.
Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage.
Repeated freezing and thawing should be avoided.
(a) Reverse-phase high-performance liquid chromatography (RP-HPLC) analysis.
(b) Sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis.
Product Science Overview
The Truncated BH3 Interacting Domain Death Agonist (tBID) is a truncated form of the pro-apoptotic protein BID (BH3 Interacting Domain Death Agonist). This protein is a member of the Bcl-2 family, which plays a crucial role in the regulation of apoptosis, or programmed cell death. The recombinant form of tBID is produced in Escherichia coli (E. coli) and is used extensively in laboratory research to study apoptosis mechanisms.
tBID is generated by the cleavage of full-length BID by Caspase-8, an enzyme that plays a pivotal role in the apoptotic signaling pathway . The truncated form of BID, known as tBID, translocates from the cytosol to the mitochondria, where it transduces apoptotic signals . The recombinant tBID protein is a single, non-glycosylated polypeptide chain containing 61-195 amino acids, with a molecular mass of approximately 15.4 kDa .
tBID is a potent pro-apoptotic molecule that interacts with other members of the Bcl-2 family, such as Bax. Upon apoptotic signaling, tBID forms a heterodimer with Bax, leading to the insertion of Bax into the outer mitochondrial membrane . This interaction induces the opening of the mitochondrial voltage-dependent anion channel, resulting in the release of cytochrome c and other pro-apoptotic factors from the mitochondria . The release of these factors activates caspases, which are proteases that execute the apoptotic program.
The primary mode of action of tBID involves its translocation to the mitochondria and interaction with Bax. This interaction is crucial for the permeabilization of the mitochondrial membrane and the subsequent release of cytochrome c . The release of cytochrome c into the cytosol triggers the formation of the apoptosome, a multiprotein complex that activates initiator caspases, such as Caspase-9. Activated Caspase-9 then cleaves and activates effector caspases, such as Caspase-3, leading to the execution of apoptosis .
The activity of tBID is tightly regulated by various cellular mechanisms. Anti-apoptotic proteins within the Bcl-2 family, such as Bcl-2 and Bcl-xL, can inhibit the pro-apoptotic activity of tBID by binding to it and preventing its interaction with Bax . Additionally, the expression of BID and its cleavage to form tBID can be regulated by various apoptotic stimuli, including death receptor signaling and DNA damage .
Recombinant tBID is widely used in laboratory research to study the mechanisms of apoptosis and the role of Bcl-2 family proteins in cell death regulation. It is also used to investigate the effects of various apoptotic stimuli and the interactions between pro-apoptotic and anti-apoptotic proteins .
