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Conversion of the molecular chaperone Spy into a novel fusion tag to enhance recombinant protein expression.

J Biotechnol. 2020; 
Ruan A1, Ren C1, Quan S2.
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Catalog Antibody … The proteins were transferred onto polyvinylidene fluoride (PVDF) membranes, which<br> were then probed with anti-His antibody (Millipore, catalog # 05-949-KC or <b>GenScript</b><br> catalog # A00612). 2.3. Quantification of protein bands … Get A Quote

摘要

The soluble expression of recombinant proteins in Escherichia coli is vital for protein applications in biotechnology and pharmaceuticals. However, the use of E. coli for efficient heterologous protein expression is hampered by several factors, such as poor expression and protein aggregation. Changing the culture or purification conditions may alleviate these issues, but methods based on gene fusion technology offer unique opportunities to improve the production and purification of soluble proteins. Here, we develop a novel fusion tag based on Spy, a newly identified molecular chaperone that functions in the periplasm of E. coli in an ATP-independent manner to prevent protein aggregation and assist in protein f... More

关键词

Fusion tag; Molecular chaperone; Protein expression; Spy