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CLONING, EXPRESSION AND PURIFICATION OF HUMAN TRUNCATED SIRT1

Rahul Kewal Kumar, Abhay Kumar Singh, ROSHAN PANDEY, Sharmistha Dey

International Journal of Molecular Biology · 2012 · ▲ 4 citations

Deregulated nutrient-sensing Human

Abstract

Sirtuins belong to an evolutionarily conserved class of proteins that regulate a variety of cellular functions such as genome maintenance, longevity, and metabolism. The conserved part of amino acids residues 244-498 of full length human SIRT1 have the function- al activity. To construct a functional form of SIRT1 by DNA recombinant technology, we have expressed and purified truncated protein of 420 (193 to 611) amino acids of MW 47 kDa in prokaryotic system, Ecoli BL21 (DE3) strain. This functional protein has a potential to be used as a diagnostic tool and for the development of new therapeutic agent for age related disease.

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Provenance

Source: OpenAlex
DOI: 10.9735/0976-0482.3.2.49-54
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Fetched: 2026-10-23 MST

Cite this

APA

Kumar, R.K., Singh, A.K., PANDEY, R., & Dey, S. (2012). CLONING, EXPRESSION AND PURIFICATION OF HUMAN TRUNCATED SIRT1. <em>International Journal of Molecular Biology</em>. https://doi.org/10.9735/0976-0482.3.2.49-54

Vancouver

Kumar RK, Singh AK, PANDEY R, Dey S. CLONING, EXPRESSION AND PURIFICATION OF HUMAN TRUNCATED SIRT1. International Journal of Molecular Biology. 2012. doi:10.9735/0976-0482.3.2.49-54.

BibTeX

@article{rahul2012CLONIN, title = {CLONING, EXPRESSION AND PURIFICATION OF HUMAN TRUNCATED SIRT1}, author = {Rahul Kewal Kumar and Abhay Kumar Singh and ROSHAN PANDEY and Sharmistha Dey}, journal = {International Journal of Molecular Biology}, year = {2012}, doi = {10.9735/0976-0482.3.2.49-54}, }