HSP90B1-Polyclonal Antibodies

Secretory proteins are synthesized on polysomes and translocated into the endoplasmic reticulum (ER). Inside ER, these proteins are often modified by disulfide bond formation, amino-linked glycosylation and folding. The ER contains a pool of molecular chaperones, including Grp94, to help proteins fold properly. Grp94 is a glucose-regulated protein (1) with sequence homology to Hsp90 (2). In addition to its role to help some secretory proteins fold to their correct conformation (3), studies suggest that Grp94 derived from cancer cells also induces anti-tumor immune responses in mouse tumor models (4, 5). One reason for this tumor immunogenicity is that Grp94 binds to the peptides from proteins in cancer cells and can therefore present these peptides as tumor antigens (6). Furthermore, Grp94 has also been shown to induce maturation of dendritic cells (7). Taken together, Grp94 functions both as a tumor-specific antigen and as an activator of antigen-presenting cells to elicit immunity to cancers (8).

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