Bcl 2 Human (minus BH2 domain)
(b) Analysis by SDS-PAGE.
Description
The Bcl-2 is expressed as His-Tag fusion protein and purified by proprietary chromatographic techniques.
Product Specs
The Bcl-2 protein is purified by proprietary chromatographic techniques.
Note: Bcl-2 has a tendency to form intramolecular disulfide bonds. To prevent this, it is recommended to include 5mM DTT in the assay buffer. When performing SDS-PAGE analysis, it is recommended to use a buffer containing 10mM DTT.
Upon reconstitution, Bcl-2 should be stored at 4°C for 2-7 days. For extended storage, it is recommended to aliquot and freeze the reconstituted protein at -18°C or lower.
To enhance long-term stability during storage, the addition of a carrier protein (0.1% HSA or BSA) is recommended.
Avoid repeated freeze-thaw cycles to maintain protein integrity.
(b) Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE) analysis.
- An input marker or positive control in Western Blotting experiments.
- A tool to investigate the function of Bcl-2 in various cellular processes, including apoptosis and cell survival.
Product Science Overview
B-Cell Leukemia/Lymphoma 2 (Bcl-2) is a member of the Bcl-2 family of proteins, which play a crucial role in regulating apoptosis, or programmed cell death. The Bcl-2 family consists of both pro-apoptotic and anti-apoptotic proteins that interact to control cell survival and death. Bcl-2 itself is an anti-apoptotic protein that helps cells avoid apoptosis, thereby contributing to cell survival.
Bcl-2 proteins are characterized by the presence of up to four conserved sequence blocks known as Bcl-2 homology (BH) motifs or domains. These domains are crucial for the protein’s function and interactions. The Bcl-2 protein contains BH1, BH2, BH3, and BH4 domains, which form a binding groove that allows it to interact with pro-apoptotic proteins .
The primary function of Bcl-2 is to regulate mitochondrial outer membrane permeability (MOMP) and prevent the release of cytochrome c and other apoptotic factors from the mitochondria. By doing so, Bcl-2 inhibits the activation of caspases, the enzymes responsible for executing apoptosis .
Dysregulation of Bcl-2 is implicated in various diseases, particularly cancers. Overexpression of Bcl-2 can lead to the survival of cells that would otherwise undergo apoptosis, contributing to the development and progression of tumors. For example, in follicular lymphoma, a chromosomal translocation places the Bcl-2 gene next to the immunoglobulin heavy chain locus, resulting in the overexpression of Bcl-2 and the inhibition of apoptosis .
Recombinant human Bcl-2 proteins are produced using recombinant DNA technology, which involves inserting the Bcl-2 gene into a host organism, such as E. coli, to produce the protein. These recombinant proteins are used in research to study the function and interactions of Bcl-2, as well as to develop potential therapeutic agents targeting Bcl-2 .
Given its role in inhibiting apoptosis, Bcl-2 is a target for cancer therapy. Drugs known as BH3 mimetics are designed to mimic the action of pro-apoptotic BH3-only proteins, thereby neutralizing the anti-apoptotic function of Bcl-2 and inducing cell death in cancer cells. Clinical trials of BH3 mimetics have shown promise in treating various cancers by promoting apoptosis in tumor cells .
