Calreticulin is a Ca
2؉-binding chaperone that resides in the lumen of the endoplasmic reticulum and is involved in the regulation of intracellular Ca 2؉ homeostasis and in the folding of newly synthesized glycoproteins. In this study, we have used site-specific mutagenesis to map amino acid residues that are critical in calreticulin function.
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