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Mempro™ Detergent-Free Peptidase AD Production

Creative Biostructure has years of experience in membrane protein production, our highly professional scientists can offer tailored Mempro™ Peptidase AD production services using detergent-free expression system.

Peptidase AD is a superfamily which consists of three families: Type IV leader peptidase, Presenilin and Gamma-secretase. Type IV leader peptidase family has two members: Peptidase A24B and FlaK domain protein, Presenilin family has one member: Intramembrane aspartate protease. While seven members are contained in Gamma-secretase family: Gamma-secretase complex, structure 1, Gamma-secretase complex, structure 2, Gamma-secretase complex, structure 3, Gamma-secretase complex, structure 4, Gamma-secretase complex, structure 5, Gamma-secretase complex, structure 6 and Nicastrin, TM helix. Nicastrin is one of the members of Peptidase AD superfamily and it is a portion of the gamma secretase protein complex. In addition, PSEN1 (presenilin-1), APH-1 (anterior pharynx-defective 1) and PEN-2 (presenilin enhancer 2) are in the complex as well. Nicastrin has been proved as a monitor of neprilysin, which is related to the degradation of amyloid beta fragment.

Mempro™ Detergent-Free Peptidase AD Production Figure 1. The structure of Nicastrin, a protein of Peptidase AD superfamily.

Creative Biostructure has rich professional experience in high quality Peptidase AD production using detergent-free membrane protein expression system, we can perform various strategies for Mempro™ detergent-free protein production, including:

  • Mempro™ Peptidase AD Production Using Nanodiscs

Nanodiscs are generally used for structural, enzymatic and biophysical researches and can magically make membrane proteins stabilized due to its structural characteristics. In contrast with bicelles, detergent micelles and liposomes, a more native environment where proteins remain monodisperse and active can be offered.

  • Mempro™ Peptidase AD Production Using Amphipols

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.

  • Mempro™ Peptidase AD Production Using Poly (styrene-co-maleic acid) Lipid Particles (SMALPs)

SMALPs are disc like structures containing a protein in a lipid bilayer. By using this approach, there is no need to sift special detergents, the speed and economy of protein extraction can be significantly improved.

These novel detergent-free approaches for Peptidase AD production can be achieved effortless, 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:
Nagase, T., Seki, N., Ishikawa, K.-i., Ohira, M., Kawarabayasi, Y., Ohara, O., . . . Nomura, N. (1996). Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain. DNA Research, 3(5), 321-329.
Yu, G., Nishimura, M., Arawaka, S., Levitan, D., Zhang, L., Tandon, A., . . . Kawarai, T. (2000). Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and βAPP processing. Nature, 407(6800), 48-54.
Wheatley, M., Charlton, J., Jamshad, M., Routledge, S. J., Bailey, S., La-Borde, P. J., . . . Dafforn, T. R. (2016). GPCR–styrene maleic acid lipid particles (GPCR–SMALPs): their nature and potential. Biochemical Society Transactions, 44(2), 619-623.


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