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Description

Synonyms

Bcl-2-modifying factor, FLJ00065, BMF.

Bcl2 modifying factor, is a member of the Bcl2 protein family of apoptosis mediators. Bcl2 modifying factor is widely expressed in many tissues. Bcl2 modifying factor contains a single Bcl2 homology domain 3 (BH3), and binds Bcl2 proteins and functions as an apoptotic activator. Also, Bcl2 modifying factor is important for histone deacetylase (HDAC) inhibitors, which alters the balance between acetylation and deacetylation, significantly increasing histone acetylation, while strongly inducing apoptosis in a variety of cancer cell types. Bcl2 modifying factor supports Bim in regulating cell death processes in response to many stimuli. A synergistic role for bim and Bcl2 modifying factor in an apoptotic pathway has been suggested leading to the clearance of Neisseria gonorrhoeae -infected cells.

Description

Bcl2 modifying factor Human Recombinant produced in E. coli is a single, non-glycosylated, polypeptide chain containing 144 amino acids (1-129 a.a.) and having a molecular mass of 15.6 kDa. The Bcl2 modifying factor is fused to 15 amino acid His Tag at Nterminus and purified by proprietary chromatographic techniques.

Source

Escherichia coli

Physical Appearance

Sterile Filtered colorless solution.

Formulation

The Bcl2 modifying factor solution contains 20mM Tris pH-7.5, 1mM DTT & 10% glycerol.

Stability

Bcl2 modifying factor although stable 4°C for 4 weeks, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

Amino acid sequence

MASMTGGQQM GRGSHMEPSQ CVEELEDDVF QPEDGEPVTQ PGSLLSADLF AQSLLDCPLS RLQLFPLTHC CGPGLRPTSQ EDKATQTLSPASPSQGVMLP CGVTEEPQRL FYAPAEPKSC VVADPPLPAQ PCFEWRREQE RGRP

Usage

Bio-world 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.

Properties

Storage Temperature

-20°C

Purity

Greater than 90.0% as determined by SDS-PAGE