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Purification and Characterization of Calreticulin: a Ca²⁺-Binding Chaperone from Sheep Kidney

Purification and Characterization of Calreticulin: a Ca²⁺-Binding Chaperone from Sheep Kidney

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_1616482450

Purification and Characterization of Calreticulin: a Ca²⁺-Binding Chaperone from Sheep Kidney

About this item

Full title

Purification and Characterization of Calreticulin: a Ca²⁺-Binding Chaperone from Sheep Kidney

Publisher

Boston: Springer-Verlag

Journal title

Applied biochemistry and biotechnology, 2014-11, Vol.174 (5), p.1771-1783

Language

English

Formats

Publication information

Publisher

Boston: Springer-Verlag

More information

Scope and Contents

Contents

Calreticulin (CRT) is a molecular chaperone with a molecular mass of 46 kDa present in the endoplasmic reticulum (ER). This protein is primarily involved in the regulation of intracellular Ca²⁺ homeostasis and Ca²⁺ storage in the ER. CRT also plays a significant role in autoimmunity and cancer. This protein contains three distinct structural domain...

Alternative Titles

Full title

Purification and Characterization of Calreticulin: a Ca²⁺-Binding Chaperone from Sheep Kidney

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_miscellaneous_1616482450

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_1616482450

Other Identifiers

ISSN

0273-2289

E-ISSN

1559-0291

DOI

10.1007/s12010-014-1150-5

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