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Type: | Book chapter |
Title: | Caspase-2 protocols |
Author: | Dorstyn, L. Kumar, S. |
Citation: | Caspases, paracaspases and metacaspases: methods and protocols, 2014 / Bozhkov, P., Salvasen, G. (ed./s), vol.1133, Ch.4, pp.71-87 |
Publisher: | Humana Press |
Issue Date: | 2014 |
Series/Report no.: | Methods in Molecular Biology; 1133 |
ISBN: | 149390356X 9781493903566 |
Editor: | Bozhkov, P. Salvasen, G. |
Statement of Responsibility: | Loretta Dorstyn and Sharad Kumar |
Abstract: | Caspase-2 has been shown to function in apoptosis and in some non-apoptotic pathways, including tumor suppression and aging. Caspase-2 has some unique features and is the only caspase that constitutively localizes to the nucleus, although its nuclear function remains unknown. During apoptosis signaling, caspase-2 rapidly homodimerizes, which leads to its activation and proteolytic processing. The activation of caspase-2 can be measured by assessing its dimerization and/or cleavage of the caspase-2 zymogen and its substrates. This chapter outlines commonly used methods to purify recombinant caspase-2 and assess its activity and function in vitro and in cultured cells or tissue extracts. |
Keywords: | Apoptosis; Caspase-2; Caspase activity; Peptide substrates; Recombinant protein; Immunoblotting |
Rights: | © Springer Science+Business Media New York 2014 |
DOI: | 10.1007/978-1-4939-0357-3_4 |
Grant ID: | http://purl.org/au-research/grants/nhmrc/1021456 http://purl.org/au-research/grants/nhmrc/1043057 |
Appears in Collections: | Aurora harvest 2 Medicine publications |
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