Glucose regulated protein 94 (GRP94), is an endoplasmic reticulum-resident member of the heat shock protein90 (HSP90). It plays a crucial role in regulating biological functions. This includes chaperoning cellular protein in the ER lumen and maintaining calcium homeostasis. 

Recent reports have highlighted the clinical and functional relevance of GRP94 expression in the progression and metastasis of a variety of cancers. The current review focuses on GRP94's physiological as well as pathophysiological functions in cancer cells. You can know more about GRP94 antibodies through this website.

GRP94, a 803-amino acid protein that belongs to the heat shock protein90 family, is an 803-amino acid protein. It functions as a molecular chaperone and aids in the transport and processing of secreted protein. GRP94 and its N terminal fragment stimulate CTL expansion, maturation and differentiation of human monocyte-derived Dendritic Cells (MDDC). 

It is involved in acquired and innate immunity, maturation, and chemotaxis dendritic cell maturation, Ab production, and cross-priming. GRP94 expression suppressed A23187-induced Apoptosis, and stabilized calcium homeostasis. GRP94 can be found in colon carcinoma or liver metastases cells and human gastric carcinoma BGC-823 cell lines.

Polysomes synthesize secretory proteins and they are translocated to the endoplasmic reticulum. These proteins can be modified in ER by amino-linked glycosylation, disulfide bond formation and folding. To ensure proper protein folding, the ER includes a number of molecular chaperones including Grp94. Grp94, a glucose-regulated protein, has sequence homology with Hsp90.