BID Mouse, GST
Greater than 95.0% as determined by: (a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Description
The Mouse BID is expressed as GST-Tag fusion protein and purified by proprietary chromatographic technique.
Product Specs
The Mouse GST-tagged BID protein solution is supplied in a buffer containing 10mM Tris-HCl at pH 8, 1mM EDTA, and 250mM NaCl.
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, freezing at -20°C is recommended. To ensure long-term stability, adding a carrier protein like HSA or BSA (0.1%) is advised. Repeated freeze-thaw cycles should be avoided.
The purity of this product is greater than 95%, as determined by two analytical methods: (a) Reverse-Phase High-Performance Liquid Chromatography (RP-HPLC) and (b) Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE).
Product Science Overview
The BH3 Interacting Domain Death Agonist (BID) is a pro-apoptotic member of the Bcl-2 protein family. This family of proteins plays a crucial role in regulating apoptosis, which is the process of programmed cell death. BID is particularly significant because it acts as a mediator of mitochondrial damage induced by caspase-8, leading to the release of cytochrome c and the activation of downstream apoptotic pathways .
BID contains a BH3 domain, which is essential for its pro-apoptotic activity. The BH3 domain allows BID to interact with other Bcl-2 family proteins, such as BAX and BCL-2. Upon activation by apoptotic signals, BID undergoes cleavage by caspase-8, resulting in a truncated form known as tBID. This truncated form translocates to the mitochondria, where it facilitates the release of cytochrome c, leading to the activation of caspases and the execution of apoptosis .
Recombinant BID proteins are often used in research to study the mechanisms of apoptosis. The mouse recombinant BID tagged with Glutathione S-Transferase (GST) is a commonly used variant. The GST tag aids in the purification and detection of the recombinant protein. This recombinant form retains the functional properties of the native BID protein, making it a valuable tool for investigating the role of BID in apoptosis .
BID plays a pivotal role in the intrinsic pathway of apoptosis. Upon receiving apoptotic signals, BID is cleaved by caspase-8, and the resulting tBID translocates to the mitochondria. Here, tBID interacts with BAX, promoting its oligomerization and insertion into the mitochondrial membrane. This interaction leads to the formation of pores in the mitochondrial membrane, resulting in the release of cytochrome c and other pro-apoptotic factors. The release of cytochrome c into the cytosol triggers the activation of caspase-9, which in turn activates caspase-3, leading to the execution phase of apoptosis .
The study of BID and its role in apoptosis has significant implications for understanding various diseases, including cancer and neurodegenerative disorders. By using recombinant BID proteins, researchers can dissect the molecular mechanisms underlying apoptosis and identify potential therapeutic targets. For instance, targeting BID or its interactions with other Bcl-2 family proteins could provide new strategies for inducing apoptosis in cancer cells .
