Optimization of expression and purification of HSPA6 protein from camelus dromedarius in E.coli

Abstract EN

The HSPA6, one of the members of large family of HSP70, is significantly up-regulated and has been targeted as a biomarker of cellular stress in several studies.

Herein, conditions were optimized to increase the yield of recombinant camel HSPA6 protein in its native state, primarily focusing on the optimization of upstream processing parameters that lead to an increase in the specific as well as volumetric yield of the protein.

The results showed that the production of cHSPA6 was increased proportionally with increased incubation temperature up to 37 C.

Induction with 10 lMIPTG was sufficient to induce the expression of cHSPA6 which was 100 times less than normally used IPTG concentration.

Furthermore, the results indicate that induction during early to late exponential phase produced relatively high levels of cHSPA6 in soluble form.

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