As a pioneer and undisputed global leader in membrane protein production, scientists from Creative Biostructure can offer customized Mempro™ peptidase clan AA superfamily production services using detergent-free expression system.
Peptidase clan AA is a superfamily which is composed of two families: Aspartic peptidase family contained aspartyl protease family protein, Beta-secretase 1, Beta-secretase 2 and uncharacterized protein, and Retroviral-like aspartic protease family contained only retroviral-like aspartic protease 1. Beta-secretase 1 (BACE1) is encoded by the BACE1 gene in humans, however, it is also called aspartyl protease 2, ASP2, and beta-site APP cleaving enzyme 1. BACE1 is an aspartic-acid protease which has two active site aspartate residues in its extracellular protein domain and may function as a dimmer, besides, it’s crucial in the formation of myelin sheaths in peripheral nerve cells. It’s reported that BACE proteases, especially BACE1, are essential for the proper function of muscle spindles.
Figure 1. Tm1631 protein surface conservation analysis by ProBiS. (PLoS Comput. Biol., 2013)
Creative Biostructure has rich professional experience in high quality peptidase clan AA superfamily production using detergent-free membrane protein expression system, we can perform various strategies for Mempro™ detergent-free protein production, including:
On account of the structural characteristics, nanodiscs can magically make membrane proteins stabilized. They are composed of membrane scaffold proteins (MSPs) which can offer two surface, one is a hydrophilic at the outside, the other is facing the lipids. Nanodiscs are generally used for structural, enzymatic and biophysical researches.
Amphipols are portmanteaus of amphiphilic polymers, projecting to maintain transmembrane proteins (TMPs) solvable in aqueous solutions without detergent. They are synthesized by forming amide bonds between octylamine and, sometimes, isopropylamine. Besides amphipols are absolutely serviceable tools for handling membrane proteins in detergent-free aqueous solutions.
Using SMALPs can make detergent-free isolation of membrane proteins and retention of their crude lipid environment available. Recently, electron microscopy has quickly progressed, which leads to the highly development of data acquisition, together with the conformation and resolution information getable.
These novel detergent-free approaches for peptidase clan AA superfamily production can be obtained easily, and enabling more comprehensively structural and functional studies.
Creative Biostructure provides other various Mempro™ membrane protein production services. Please feel free to contact us for a detailed quote.
References:Bayburt, T. H., & Sligar, S. G. (2010). Membrane protein assembly into Nanodiscs. FEBS letters, 584(9), 1721-1727. Yan, N. (2015). Structural biology of the major facilitator superfamily transporters. Annual review of biophysics, 44, 257-283. Esch F S, Keim P S, Beattie E C, et al. Cleavage of amyloid beta peptide during constitutive processing of its precursor[J]. Science, 1990, 248(4959): 1122-1124.Haass C, Lemere C A, Capell A, et al. The Swedish mutation causes early-onset Alzheimer's disease by β-secretase cleavage within the secretory pathway[J]. Nature medicine, 1995, 1(12): 1291-1296.