Calcium is a universal signaling molecule involved in many cellular functions such as cell motility, metabolism, protein modification, protein folding, and apoptosis. Calcium is stored in the endoplasmic reticulum (ER), where it is buffered by calcium binding chaperones such as calnexin and calreticulin, and is released via the IP3 Receptor channel . Calreticulin also functions as an ER chaperone that ensures proper folding and quality control of newly synthesized glycoproteins. As such, calreticulin presumably does not alter protein folding but regulates proper timing for efficient folding and subunit assembly. Furthermore, calreticulin retains proteins in non-native conformation within the ER and targets them for degradation .
Western blot analysis of 1) Rat Skeletal Muscle Tissue Lysate, 2) Hela Cell Lysate , 3) 3T3 Cell Lysate using Calreticulin(EA366)Rabbit pAb diluted at 1:1000.
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