| Description: | Calreticulin/CALR protein, a calcium-binding chaperone, orchestrates crucial functions in the endoplasmic reticulum (ER) through the calreticulin/calnexin cycle, promoting the folding, oligomeric assembly, and quality control of glycoproteins. This lectin transiently interacts with nearly all monoglucosylated glycoproteins synthesized in the ER, contributing to their proper maturation and function. Beyond its role in glycoprotein processing, CALR is involved in diverse cellular processes. It interacts with the DNA-binding domain of NR3C1, mediating its nuclear export and influencing gene expression regulation. Furthermore, CALR may play a role in oocyte maturation by regulating calcium homeostasis and participating in the cortical reaction during oocyte activation, potentially contributing to the block against polyspermy. CALR forms complexes with various proteins, including GABARAP, PDIA3/ERp57, and TRIM21, highlighting its versatile interactions within cellular pathways. It also engages in intricate protein-protein interactions with PPIB, SPACA9, and CLCC1, underscoring its involvement in diverse cellular processes and protein complexes. Calreticulin/CALR Protein, Mouse (P.pastoris, His, solution) is the recombinant mouse-derived Calreticulin/CALR protein, expressed by P. pastoris , with N-6*His labeled tag. The total length of Calreticulin/CALR Protein, Mouse (P.pastoris, His, solution) is 399 a.a., with molecular weight of ~48.3 kDa. |
