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Cloning, expression and purification of the CCN family of proteins in Escherichia coli


Reference:

Holbourn, K. P. and Acharya, K. R., 2011. Cloning, expression and purification of the CCN family of proteins in Escherichia coli. Biochemical and Biophysical Research Communications, 407 (4), pp. 837-841.

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Official URL:

http://dx.doi.org/10.1016/j.bbrc.2011.03.122

Abstract

The CCN proteins are extracellular matrix associated proteins involved in critical cell activities and several aggressive forms of cancer. The proteins share a modular structure of four discrete domains and 38 conserved cysteine residues. The absence of any structural information of these proteins has resulted in a need for the ability to produce substantial amounts of pure CCN protein. Through bacterial expression and inclusion body based purification, pure recombinant CCN proteins have been produced for use in structural and biochemical experiments.

Details

Item Type Articles
CreatorsHolbourn, K. P.and Acharya, K. R.
DOI10.1016/j.bbrc.2011.03.122
Uncontrolled Keywordsheparin binding, protein domains, ccn protein, protein purification, extracellular matrix protein
DepartmentsFaculty of Science > Biology & Biochemistry
RefereedYes
StatusPublished
ID Code23898

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