Bcl XL Human

B-Cell Lymphoma Extra Large Human Recombinant
Cat. No.
BT23725
Source
Escherichia Coli.
Synonyms
BclXL, Bcl-X(L), Bcl-XL.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 95.0% as determined 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-XL Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing amino acids 1-210.
The Bcl-XL is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Bcl-XL, a transmembrane protein residing in the mitochondrial membranes of long-lived and postmitotic cells like adult brain cells, participates in the FAS-Ligand signal transduction pathway. As an anti-apoptotic protein within the Bcl-2 family, Bcl-XL forms heterodimers, playing a crucial role in apoptosis regulation. Notably, BCL-XL contributes to cancer cell survival. Its primary function involves monitoring and suppressing apoptosis, effectively acting as a pro-survival protein.
Description
Recombinant human Bcl-XL, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising amino acids 1 to 210. The purification of Bcl-XL is achieved through proprietary chromatographic techniques.
Physical Appearance
White lyophilized (freeze-dried) powder, sterile filtered.
Formulation
The protein is supplied in a buffer containing 10mM Tris-HCl (pH 8), 1mM EDTA, and 250mM NaCl.
Solubility
To reconstitute, suspend Bcl-XL in 1000µl of sterile, 18M-cm H2O and allow it to dissolve overnight at 4°C. Dilute the reconstituted protein 10-fold into the desired buffer system. Due to Bcl-XL's propensity to form intramolecular disulfide bonds, the addition of 5mM DTT to the assay buffer is recommended. For SDS-PAGE analysis, 10mM DTT is advised.
Stability
Lyophilized Bcl-XL remains stable at room temperature for up to 3 weeks; however, it is recommended to store the desiccated product below -18°C. After reconstitution, Bcl-XL should be stored at 4°C for 2-7 days. For long-term storage, aliquot and freeze at -18°C. Adding a carrier protein like HSA or BSA (0.1%) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
The purity of Bcl-XL is greater than 95% as determined by SDS-PAGE analysis.
Synonyms
BclXL, Bcl-X(L), Bcl-XL.
Source
Escherichia Coli.

Product Science Overview

Introduction

B-Cell Lymphoma Extra Large (BCL-xL) is a member of the BCL-2 protein family, which plays a crucial role in regulating cell death and survival. BCL-xL is encoded by the BCL2L1 gene and is known for its anti-apoptotic properties, making it a significant target in cancer research and therapy. The recombinant form of BCL-xL, produced through genetic engineering, allows for detailed studies and potential therapeutic applications.

BCL-2 Protein Family

The BCL-2 protein family consists of several proteins that regulate apoptosis, a form of programmed cell death essential for maintaining cellular homeostasis. The family is divided into three subgroups based on their function and structure:

  1. Anti-apoptotic proteins: These include BCL-2, BCL-xL, and MCL-1, which prevent apoptosis by inhibiting pro-apoptotic proteins.
  2. Pro-apoptotic proteins: These include BAX and BAK, which promote apoptosis by forming pores in the mitochondrial membrane.
  3. BH3-only proteins: These include BID, BIM, and PUMA, which regulate the activity of both anti-apoptotic and pro-apoptotic proteins.
Structure and Function of BCL-xL

BCL-xL is a mitochondrial protein that inhibits apoptosis by preventing the release of cytochrome c from the mitochondria, a critical step in the apoptotic pathway. It achieves this by binding to and neutralizing pro-apoptotic proteins such as BAX and BAK. BCL-xL has also been implicated in other cellular processes, including autophagy and senescence, where it can have dual roles depending on the cellular context .

Role in Cancer

BCL-xL is overexpressed in various cancers, including B-cell lymphomas, where it contributes to tumor cell survival and resistance to chemotherapy. Its anti-apoptotic function allows cancer cells to evade programmed cell death, leading to uncontrolled cell proliferation. Targeting BCL-xL with specific inhibitors is a promising therapeutic strategy in cancer treatment .

Recombinant BCL-xL

The recombinant form of BCL-xL is produced using recombinant DNA technology, where the BCL2L1 gene is inserted into an expression vector and introduced into host cells, such as bacteria or yeast. These host cells then produce the BCL-xL protein, which can be purified and used for research or therapeutic purposes. Recombinant BCL-xL allows for detailed structural and functional studies, aiding in the development of targeted therapies.

Therapeutic Applications

Given its role in cancer cell survival, BCL-xL is a potential target for cancer therapy. Several small-molecule inhibitors of BCL-xL have been developed, aiming to restore the apoptotic pathway in cancer cells. These inhibitors can sensitize cancer cells to chemotherapy and improve treatment outcomes. Additionally, understanding the dual roles of BCL-xL in autophagy and senescence may provide insights into novel therapeutic approaches .

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