Bcl 2 Human (minus NWGR domain)

B-Cell Leukemia/Lymphoma 2 Human Recombinant (–NWGR)
Cat. No.
BT23646
Source
Escherichia Coli.
Synonyms
Apoptosis regulator Bcl-2, BCL2, B-cell CLL/lymphoma 2, Bcl-2.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

Bcl-2 Des NWGR domain (143-146 residues) Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 214 amino acids 1-142 and 147-218.
The Bcl-2 is expressed as His-Tag fusion protein and purified by proprietary chromatographic techniques.

Product Specs

Introduction
The BCL2 gene codes for a protein found within the outer membrane of mitochondria. This protein, known as BCL2, prevents certain cells like lymphocytes from undergoing apoptosis (programmed cell death). When BCL2 is constantly produced, for instance, due to its translocation to the immunoglobulin heavy chain locus, it can lead to a type of cancer called follicular lymphoma. The BCL2 gene produces two slightly different messenger RNA transcripts through a process called alternative splicing, resulting in two BCL2 protein variants with different ends.
Description
This product consists of a recombinant human Bcl-2 protein with a deleted NWGR domain (amino acid residues 143-146). It is produced in E. coli bacteria and purified to a single, non-glycosylated polypeptide chain comprising 214 amino acids (residues 1-142 and 147-218). The protein is engineered with a His-Tag for purification purposes and purified using proprietary chromatographic methods.
Physical Appearance
The product appears as a sterile, filtered white powder that has been freeze-dried (lyophilized).
Formulation
The protein is supplied in a buffer solution containing 10mM Tris-HCL (pH 8), 1mM EDTA, and 250mM NaCl.
Solubility
To reconstitute the lyophilized Bcl-2, suspend it in 100µl of 0.5M Acetic acid and allow it to dissolve overnight at 4°C. Subsequently, dilute the solution 10-fold with your chosen buffer. It is important to note that BCL-2 tends to form internal disulfide bonds, so adding 5mM DTT to the assay buffer is recommended. When performing SDS-PAGE, use a buffer containing 10mM DTT.
Stability
Lyophilized Bcl-2 remains stable for 3 weeks at room temperature but should be stored in a dry environment below -18°C. After reconstitution, store Bcl-2 at 4°C for 2-7 days. For long-term storage, freeze it below -18°C. To preserve protein stability during long-term storage, adding a carrier protein like HSA or BSA (0.1%) is advisable. Repeated freeze-thaw cycles should be avoided.
Purity
The purity of this product is greater than 95.0% as determined by two methods: (a) Reverse-Phase High-Performance Liquid Chromatography (RP-HPLC) and (b) Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE).
Applications
This product serves two primary applications: (a) as an input marker or positive control in Western Blotting experiments and (b) for studying protein function.
Synonyms
Apoptosis regulator Bcl-2, BCL2, B-cell CLL/lymphoma 2, Bcl-2.
Source
Escherichia Coli.

Product Science Overview

Introduction

B-Cell Leukemia/Lymphoma 2 (BCL-2) is a protein that plays a crucial role in regulating apoptosis, or programmed cell death. This protein is part of the BCL-2 family, which includes both pro-apoptotic and anti-apoptotic members. The balance between these proteins determines whether a cell will undergo apoptosis. BCL-2 itself is an anti-apoptotic protein, meaning it helps cells avoid programmed death, which can be beneficial in normal cellular processes but problematic in cancer.

Structure and Function

BCL-2 is located on the outer membrane of mitochondria, where it inhibits the release of cytochrome c, a key factor in the apoptotic pathway. By preventing cytochrome c release, BCL-2 effectively blocks the cascade of events leading to cell death. The protein has several domains, including BH1, BH2, BH3, and BH4, which are essential for its function and interactions with other proteins in the BCL-2 family.

Role in Cancer

The overexpression of BCL-2 is commonly observed in various types of cancer, including B-cell lymphomas and leukemias. This overexpression allows cancer cells to evade apoptosis, contributing to uncontrolled cell proliferation and tumor growth. Targeting BCL-2 has therefore become a strategy in cancer therapy, with several BCL-2 inhibitors being developed and tested in clinical trials.

Human Recombinant BCL-2 (–NWGR)

The human recombinant BCL-2 (–NWGR) refers to a specific variant of the BCL-2 protein that has been engineered for research and therapeutic purposes. The “–NWGR” notation indicates a mutation or modification in the protein sequence, which can affect its function or interactions with other molecules. Recombinant proteins are produced using genetic engineering techniques, allowing for the study of specific protein variants and their roles in disease.

Clinical Implications

BCL-2 inhibitors, such as venetoclax, have shown promise in treating cancers that overexpress BCL-2. These inhibitors work by binding to the BCL-2 protein, preventing it from blocking apoptosis and thereby promoting the death of cancer cells. Clinical trials have demonstrated the effectiveness of BCL-2 inhibitors in treating chronic lymphocytic leukemia (CLL) and other B-cell malignancies .

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