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.
Related documents:
This repository does not currently have the full-text of this item.You may be able to access a copy if URLs are provided below. (Contact Author)
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 |
| Creators | Holbourn, K. P.and Acharya, K. R. |
| DOI | 10.1016/j.bbrc.2011.03.122 |
| Uncontrolled Keywords | heparin binding, protein domains, ccn protein, protein purification, extracellular matrix protein |
| Departments | Faculty of Science > Biology & Biochemistry |
| Refereed | Yes |
| Status | Published |
| ID Code | 23898 |
Export
Actions (login required)
| View Item |
