Purification and Characterization of Calreticulin: a Ca²⁺-Binding Chaperone from Sheep Kidney
Purification and Characterization of Calreticulin: a Ca²⁺-Binding Chaperone from Sheep Kidney
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Boston: Springer-Verlag
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Language
English
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Publisher
Boston: Springer-Verlag
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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...
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Full title
Purification and Characterization of Calreticulin: a Ca²⁺-Binding Chaperone from Sheep Kidney
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TN_cdi_proquest_miscellaneous_1616482450
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_1616482450
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ISSN
0273-2289
E-ISSN
1559-0291
DOI
10.1007/s12010-014-1150-5