Expression Of The N-Terminal Segment Of Qbrn-2 In E. Coli And Tips On Preparation Of A Recombinant Protein

Authors: Liu W.; He R.; Xue Z.

Source: Protein and Peptide Letters, Volume 8, Number 1, February 2001 , pp. 27-32(6)

Publisher: Bentham Science Publishers

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Abstract:

POU box gene qBrn -2 exhibits restricted expression pattern in quail neurogenesis and myogenesis. Here we report isolation of a N-terminal segment (P207) of qBrn-2 expressed in E. coli and tips on preparation of a recombinant protein. Recombinant P207 was purified and migrated as a single band on SDS-PAGE with the same apparent molecular mass as predicted. In the expression of P207 by pET 3b vector, IPTG concentration for induction greatly affected the expression level. Further, fusion domain at N-terminus seemed to change the stability of P207. Those results suggest some useful tips on preparation of a recombinant protein.

Keywords: E.COLI; quail neurogenesis; myogenesis

Language: English

Document Type: Review article

DOI: http://dx.doi.org/10.2174/0929866013409733

Publication date: 2001-02-01

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Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.