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Mempro™ Cell-Based CRAL-TRIO Domain-Containing Protein Production

Creative Biostructure can provide custom Mempro™ CRAL-TRIO domain-containing protein production services using cell-based expression system.

Mempro™ cell-based protein production system is the most popularly used for the production of membrane proteins.CRAL-TRIO domains are the protein structural domains that can bind small lipophilic ligands. The structure of this domain contains several alpha helices as well as a beta sheet composed of 6 strands. Strands 2,3,4 and 5 form a parallel beta sheet with strands 1 and 6 being anti-parallel. CRAL-TRIO domain is originally identified in GTPase-activating proteins (GAPs), a guanine nucleotide exchange factors (GEFs) and a family of hydrophobic ligand binding proteins. CRAL binding protein carries 11-cis-retinol or 11-cis-retinaldehyde. TRIO protein involved in coordinating actin remodeling, which is necessary for cell migration and growth.

Figure 1. The structural model of CRAL-TRIO domain. (OPM database)

Creative Biostructure produces high-yield CRAL-TRIO domain-containing proteins, we can perform various strategies for Mempro™ cell-based protein production, including:

Escherichia coli (E. coli) is the powerful bacterial host for the production of CRAL-TRIO domain-containing proteins. Yeast cells (such as saccharomyces cerevisiae and pichia pastoris) system, combines prokaryotic as well as eukaryotic characteristics. It is a perfect eukaryotic host due to single cells, fast growth rates, inexpensive media, high cell densities. Insect cells (such as Sf9, Sf21 and High Five) are also the major system for CRAL-TRIO domain-containing protein expression, which are developed from transfected insect cells in combination with vectors derived from the baculovirus species AcMNPV. Mammalian cells present another eukaryotic system for CRAL-TRIO domain-containing protein expression, which provide near-native cell environment. Cell lines derived from COS, CHO, BHK-21, HEK293, HeLa and GH3 can be generally used for membrane protein expression.

With the Mempro™ cell-based protein production platform, Creative Biostructure is capable of expressing, isolating, purifying and crystallizing CRAL-TRIO domain-containing proteins to facilitate the study of their physiological functions.

We provide other various Mempro™ membrane protein production services. Please feel free to contact us for a detailed quote.

C. Trometer, and P. Falson (2010). Mammalian membrane protein expression in baculovirus-infected insect cells. Methods Mol. Biol., 601: 105-117.
F. Junge, et al. (2008) Large-scale production of functional membrane proteins. Cellular Mol. Life Sci., 65 (11): 1729-1755.
J. M. bomar, et al. (2003). Mutations in a novel gene encoding a CRAL-TRIO domain cause human Cayman ataxia and ataxia/dystonia in the jittery mouse. Nature Gen., 35: 264-269.
J. Petschnigg, et al. (2011). Using yeast as a model to study membrane proteins. Curr. Opin. Nephrol. Hypertens., 20(4): 425-432.
K. G. Johnson and K. Kornfeld (2010). The CRAL/TRIO and GOLD domain protein TAP-1 regulates RAF-1 activation. Dev. Biol., 341(2): 464-471.

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