Mempro™ Cell-Based BNip3 Protein Family Production

Creative Biostructure has built an excellent platform after years of membrane protein production experience. Our customized Mempro™ BNip3 production service is based on our advanced cell-based expression system.

Mempro™ cell-based protein production system is the one of our most applied and advanced method for membrane proteins production. The pro-apoptotic protein BNip3, as short for Bcl-2 Nineteen-kDa interacting protein 3, has a single Bcl-2 homology 3 (BH3) domain. Transmembrane protein BNip3 is the most intensively studied member of the Bcl-2 family. BNIP3 transmembrane domain forms tight homodimer in SDS–PAGE condition and associates strongly in the in vivo TOXCAT assays. BNip3 transmembrane domain homodimer is a right-handed parallel symmetric one due to intermonomeric helix-helix polar interactions and GXXXG motif. Loss of nutrient transportation causes a potent programmed death signal for all cells. BNip3 has a crucial role in hypoxic cell death for both normal and malignant ones. Hypoxia will induce BNip3 to express and accumulate in cytoplasmic domain or to loose from membrane. It is required to activate cell death pathway acidosis, however.

Figure 1. Spatial structure of the BNip3 transmembrane domain homodimer. (J. Biol. Chem., 2007)

Creative Biostructure is expertized in membrane protein production services. Mempro™ cell-based protein production platform provide multiple choices to accomplish your goal in different systems including:

•      Mempro™ BNip3 Production in Mammalian Cells System
Creative Biostructure can provide another great serviece-Mempro™ protein production in mammalian cells system. This system help to correct folding and post-translational modifications for membrane protein. Creative Biostructure provide different approaches to produce high quality membrane protein in mammalian cells:
1. Easy and rapid production-Transient transfection system;
2. Higher yield and reproducible production-Stable transfection system;
3. Adenovirus-assist protein expression.

•      Mempro™ BNip3 Production using Bacterial Cells System
For the production of membrane proteins, Escherichia coli (E. coli) is another widely applied bacterial host. We have optimized Lemo21 (DE3) strain for our Mempro™ protein production in E. coli system. Together with other host systems including Lactococcus lactis (L. lactis), Rodhobacter sphaeroides (R. sphaeroides), and Bacillus subtilis (B. subtilis), Creative Biostructure can provide Mempro™ cell-based BNip3 production in bacterial cells systems.

•      Mempro™ BNip3 Production in Insect Cells System
Creative Biostructure offers our advanced Mempro™ membrane protein production using insect cells system. This system is widely used for membrane protein production in cultured baculovirus system. According to similar codon usage rules, Mempro™ protein production using insect cells system can increase the expression level and reduce the truncated proteins compared to E. coli system.

•      Mempro™ BNip3 Production using Yeast Cells System
Single-celled yeast is quick, easy and economic to culture and capable to apply post-translational modification for eukaryotic membrane protein. With this popular membrane production alternative, Creative Biostructure can provide Mempro™ cell-based BNip3 production in yeast cells system.

Creative Biostructure provides Mempro™ cell-based protein production services including expressing, isolating, purifying and crystallizing BNip3 to promote its further studies on its structual and functional mechanism.

We provide an array of Mempro™ membrane protein production services. Please feel free to contact us for a detailed quote.

References:
K. Prabhakaran, et al. (2009). BNIP3 up-regulation and mitochondrial dysfunction in manganese-induced neurotoxicity. NeuroToxicology, 30(3): 414-422.
E. V. Bocharov, et al. (2007). Unique Dimeric Structure of BNip3 Transmembrane Domain Suggests Membrane Permeabilization as a Cell Death Trigger. J. Biol. Chem., 282(22): 16256-16266.
L. Li, et al. (2014). Sequence Dependence of BNIP3 Transmembrane Domain Dimerization Implicates Side-chain Hydrogen Bonding and a Tandem GxxxG Motif in Specific Helix–Helix Interactions. J. Mol. Biol., 364(5): 974-990.