|
|
| | Grp94 Antibody Chemical Properties |
| | Grp94 Antibody Usage And Synthesis |
| Source | Rabbit | | Reactivity | Human;Mouse;Rat;Monkey | | Background | Secretory proteins are synthesized on polysomes and translocated into the endoplasmic reticulum. 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 ensure correct protein folding. Grp94 is a glucose-regulated protein with sequence homology to Hsp90. In addition to its role in helping to facilitate folding of a number of secretory proteins to their correct conformation, studies suggest that Grp94 derived from cancer cells also induces anti-tumor immune responses in mouse tumor models. One way in which Grp94 promotes tumor immunogenicity is its ability to bind to and present tumor-derived peptides as antigens. Furthermore, Grp94 has also been shown to induce maturation of dendritic cells. Taken together, Grp94 functions both as a tumor-specific antigen and as an activator of antigen-presenting cells to elicit an anti-cancer immune response. | | References | [1] Lee, A.S. et al. (1981) Proc. Natl. Acad. Sci. USA 78, 4922-4925.
[2] Sorger, P.K. and Pelham, H.R. (1987) J. Mol. Biol. 194, 341-344.
[3] Argon, Y. and Simen, B.B. (1999) Semin. Cell Dev. Biol. 10, 495-505.
[4] Blachere, N.E. et al. (1997) J. Exp. Med. 186, 1315-1322.
[5] Tamura, Y. et al. (1997) Science 278, 117-120.
[6] Schild, H. and Rammensee, H.G. (2000) Nat. Immunol. 1, 100-101.
[7] Singh-Jasuja, H. et al. (2000) Eur. J. Immunol. 30, 2211-2215.
[8] Nicchitta, C.V. et al. (2004) Cell Stress Chaperones 9, 325-331. |
| | Grp94 Antibody Preparation Products And Raw materials |
|