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[A Study of Recombinant Human Sestrin 1 and Sestrin 2 Proteins Produced in a Prokaryotic System]

[A Study of Recombinant Human Sestrin 1 and Sestrin 2 Proteins Produced in a Prokaryotic System]

N Rai, R Kumar, Md A Haque, Md I Hassan, S Dey

Mol Biol (Mosk). May-Jun 2017;51(3):473-482.

PMID: 28707664

Abstract:

Sestrins are highly conserved stress-inducible proteins capable of suppressing the production of ROS and signalling through mTORC1. Here we report a study of human sestrin1 (sesn1) and sestrin2 (sesn2) proteins produced in a pET28^(+) vector based prokaryotic system. Mass spectrometry analysis, western blot and surface plasmon resonance (SPR) of affinity purified sesn1 and sesn2 proteins confirmed their identity; biophysical characteristics were observed using circular dichroism (CD) showing that sesn1 and sesn2 have a predominant α-helical structure. Here we describe a simple, one step purification process to purify a large amount of sestrin proteins with significant yield. Further study of recombinant human sestrins may further facilitate the understanding of their roles in eukaryotic cells.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR42414875	Sestrin 1 human			Price

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