BCL2L2 Human

BCL2 Like 2 Human Recombinant
Cat. No.
BT24753
Source
Escherichia Coli.
Synonyms
B-Cell Lymphoma Protein 2, BCL2 Like 2, BCL2 Like protein 2, BCLW, Bcl2-L-2, Apoptosis regulator Bcl-W, BCL2L2, BCL-W, KIAA0271.
Appearance
Sterile Filtered clear solution.
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 products may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

Recombinant Human BCL2L2 produced in E.coli cells is a non-glycosylated, homodimeric protein containing 171 amino acid chain and having a molecular mass of 18.6kDa. The Human BCL2L2 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
BCL2L2, a member of the BCL-2 protein family, plays a crucial role in promoting cell survival. It functions by suppressing the death-promoting activity of BAX, thereby mediating the survival of postmitotic Sertoli cells. BCL2L2 forms hetero- or homodimers with other BCL-2 family members, acting as a key regulator of apoptosis. Its presence leads to reduced cell apoptosis under cytotoxic conditions. Additionally, BCL2L2 is involved in the survival of neurons dependent on NGF and BDNF and plays a vital role in adult spermatogenesis.
Description
Recombinant Human BCL2L2, expressed in E.coli cells, is a non-glycosylated protein with a homodimeric structure. It comprises 171 amino acids, resulting in a molecular weight of 18.6 kDa. The purification of Human BCL2L2 is achieved through proprietary chromatographic techniques.
Physical Appearance
Clear, sterile-filtered solution.
Formulation
The provided BCL2L2 solution is concentrated and has been filtered through a 0.2µm filter. It is formulated in a buffer consisting of 25 mM Hepes (pH 7.4), 100 mM KCl, 10% Glycerol, 5% Trehalose, and 0.02% Tween-80.
Stability
While BCL2L2 exhibits stability at room temperature for a period of 3 weeks, it is recommended to store it at 4°C for optimal preservation. For extended storage periods, the addition of a carrier protein, such as 0.1% HSA or BSA, is advisable.
Purity
The purity of BCL2L2 is determined to be greater than 95.0%, as confirmed by two methods: (a) analysis using Reverse-Phase High-Performance Liquid Chromatography (RP-HPLC), and (b) analysis using Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE).
Synonyms
B-Cell Lymphoma Protein 2, BCL2 Like 2, BCL2 Like protein 2, BCLW, Bcl2-L-2, Apoptosis regulator Bcl-W, BCL2L2, BCL-W, KIAA0271.
Source
Escherichia Coli.
Amino Acid Sequence
ATPASAPDTR ALVADFVGYK LRQKGYVCGA GPGEGPAADP LHQAMRAAGD EFETRFRRTF SDLAAQLHVT PGSAQQRFTQ VSDELFQGGP NWGRLVAFFV FGAALCAESV NKEMEPLVGQ VQEWMVAYLE TQLADWIHSS GGWAEFTALY GDGALEEARR LREGNWASVR T

Product Science Overview

Gene and Protein Structure

The BCL2L2 gene is located on chromosome 14 in humans and encodes the BCL-W protein . The protein itself is involved in promoting cell survival by inhibiting apoptosis. It achieves this by interacting with other proteins in the BCL-2 family, such as BAX, to suppress their death-promoting activities .

Function and Mechanism

BCL2L2 is known for its role in reducing cell apoptosis under cytotoxic conditions . This is particularly important in the survival of neurons that depend on nerve growth factor (NGF) and brain-derived neurotrophic factor (BDNF) . Additionally, BCL2L2 plays a significant role in adult spermatogenesis, ensuring the survival of postmitotic Sertoli cells .

Clinical Significance

Mutations or dysregulation of BCL2L2 can be associated with various diseases. For instance, it has been linked to oculopharyngeal muscular dystrophy 1 and certain hematologic cancers . Understanding the function and regulation of BCL2L2 is crucial for developing therapeutic strategies for these conditions.

Research and Applications

Recombinant BCL2L2 proteins are widely used in research to study apoptosis and cell survival mechanisms. These studies are essential for developing new treatments for diseases where cell death is a significant factor, such as neurodegenerative diseases and cancer .

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