Bcl 2 Human (minus BH1 domain)
(b) Analysis by SDS-PAGE.
Description
Bcl-2 Des BH1 domain (136-155 residues) Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 198 amino acids 1-135 and 156-218.
The Bcl-2 is expressed as His-Tag fusion protein and purified by proprietary chromatographic techniques.
Product Specs
Bcl-2 Human (minus BH1 domain) Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 182 amino acids (1-135 & 156-218) and having a molecular mass of 20.6 kDa.
Bcl-2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
(b) Analysis by SDS-PAGE.
Product Science Overview
B-Cell Leukemia/Lymphoma 2 (Bcl-2) is a protein encoded by the BCL2 gene in humans. It is a key regulator of apoptosis, the process of programmed cell death, and plays a crucial role in maintaining cellular homeostasis. The recombinant form of Bcl-2, particularly the human recombinant (–BH1) variant, has been extensively studied for its biological properties and therapeutic potential.
Bcl-2 is a member of the Bcl-2 family of proteins, which includes both pro-apoptotic and anti-apoptotic members. The protein is characterized by the presence of Bcl-2 homology (BH) domains, which are critical for its function. The human recombinant (–BH1) variant lacks the BH1 domain, which is essential for its anti-apoptotic activity. This modification allows researchers to study the specific functions of other BH domains and their contributions to the overall activity of Bcl-2.
Bcl-2 functions primarily by regulating mitochondrial membrane permeability. It forms heterodimers with pro-apoptotic proteins such as BAX and BAK, inhibiting their activity and preventing the release of cytochrome c from the mitochondria. This inhibition blocks the activation of caspases, the enzymes responsible for executing apoptosis. By controlling apoptosis, Bcl-2 plays a vital role in various physiological processes, including immune response, development, and tissue homeostasis.
Bcl-2 is ubiquitously expressed in various tissues, with high levels observed in lymphoid tissues, such as the spleen and thymus. It is also expressed in other tissues, including the brain, heart, and kidneys. The expression of Bcl-2 is tightly regulated at both the transcriptional and post-transcriptional levels, ensuring that apoptosis is appropriately controlled in different cellular contexts.
The primary function of Bcl-2 is to inhibit apoptosis, thereby promoting cell survival. This function is particularly important in the immune system, where Bcl-2 helps maintain the survival of long-lived memory B cells and T cells. Additionally, Bcl-2 has been implicated in the regulation of autophagy, a cellular process that degrades and recycles damaged organelles and proteins. By modulating both apoptosis and autophagy, Bcl-2 ensures cellular homeostasis and prevents the accumulation of damaged cellular components.
The activity of Bcl-2 is regulated through various mechanisms, including post-translational modifications, interactions with other proteins, and changes in its expression levels. Phosphorylation of Bcl-2 can either enhance or inhibit its anti-apoptotic activity, depending on the specific phosphorylation sites. Additionally, Bcl-2 interacts with several regulatory proteins, such as the tumor suppressor p53, which can modulate its function in response to cellular stress.
Dysregulation of Bcl-2 expression and function is associated with various diseases, particularly cancers. Overexpression of Bcl-2 is commonly observed in B-cell lymphomas and leukemias, where it contributes to the resistance of cancer cells to apoptosis, leading to uncontrolled cell proliferation. Targeting Bcl-2 with specific inhibitors, such as venetoclax, has shown promising results in the treatment of certain cancers by restoring the apoptotic pathway and inducing cell death in cancer cells.
