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Journal article

Expression and purification of mammalian calreticulin in Pichia pastoris.

Abstract:

Calreticulin is a 46-kDa Ca(2+)-binding chaperone of the endoplasmic reticulum membranes. The protein binds Ca(2+) with high capacity, affects intracellular Ca(2+) homeostasis, and functions as a lectin-like chaperone. In this study, we describe expression and purification procedures for the isolation of recombinant rabbit calreticulin. The calreticulin was expressed in Pichia pastoris and purified to homogeneity by DEAE-Sepharose and Resource Q FPLC chromatography. The protein was not retain...

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Publication status:
Published

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Publisher copy:
10.1006/prep.2000.1291

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Journal:
Protein expression and purification
Volume:
20
Issue:
2
Pages:
207-215
Publication date:
2000-11-05
DOI:
EISSN:
1096-0279
ISSN:
1046-5928
URN:
uuid:08d129ab-377c-42d7-b0c1-5e0db180ce3e
Source identifiers:
156380
Local pid:
pubs:156380

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