Product Pathways - Metabolism
Grp94 (D6X2Q) XP® Rabbit mAb #20292
94 kDa glucose-regulated protein ECGP Endoplasmin endothelial cell (HBMEC) glycoprotein ENPL glucose regulated protein. 94 kDa GP96 gp96 homolog GRP-94 GRP94 Heat shock protein 90 kDa beta member 1 heat shock protein 90kDa beta (Grp94). member 1 HSP90B1 TRA1 tumor rejection antigen (gp96) 1 Tumor rejection antigen 1 Tumor rejection antigen-1 (gp96)
|20292S||100 µl ( 10 western blots )||￥3,750.00 现货查询||购买询价|
|20292T||20 µl ( 2 western blots )||￥1,400.00 现货查询||购买询价|
|20292||carrier free & custom formulation / quantity||email request|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IHC-P=Immunohistochemistry (Paraffin), IF-IC=Immunofluorescence (Immunocytochemistry),
Specificity / Sensitivity
Grp94 (D6X2Q) XP® Rabbit mAb recognizes endogenous levels of total Grp94 protein.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Leu397 of human Grp94 protein.
Immunohistochemical analysis of paraffin-embedded human lung carcinoma using Grp94 (D6X2Q) XP® Rabbit mAb.
Immunohistochemical analysis of paraffin-embedded human colon carcinoma using Grp94 (D6X2Q) XP® Rabbit mAb.
Immunohistochemical analysis of paraffin-embedded human prostate carcinoma using Grp94 (D6X2Q) XP® Rabbit mAb in the presence of control peptide (left) or antigen-specific peptide (right).
Confocal immunofluorescent analysis of HeLa (left) and MCF7 (right) cells using Grp94 (D6X2Q) XP® Rabbit mAb (green). Blue pseudocolor = DRAQ5® #4084 (fluorescent DNA dye).
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 ensure correct protein folding. Grp94 is a glucose-regulated protein (1) with sequence homology to Hsp90 (2). In addition to its role in helping to facilitate folding of a number of secretory proteins 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 way in which Grp94 promotes tumor immunogenicity is its ability to bind to and present tumor-derived peptides as 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 an anti-cancer immune response (8).
- Lee, A.S. et al. (1981) Proc. Natl. Acad. Sci. USA 78, 4922-4925.
- Sorger, P.K. and Pelham, H.R. (1987) J. Mol. Biol. 194, 341-344.
- Argon, Y. and Simen, B.B. (1999) Semin. Cell Dev. Biol. 10, 495-505.
- Blachere, N.E. et al. (1997) J. Exp. Med. 186, 1315-1322.
- Tamura, Y. et al. (1997) Science 278, 117-120.
- Schild, H. and Rammensee, H.G. (2000) Nat. Immunol. 1, 100-101.
- Singh-Jasuja, H. et al. (2000) Eur. J. Immunol. 30, 2211-2215.
- Nicchitta, C.V. et al. (2004) Cell Stress Chaperones 9, 325-331.
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For Research Use Only. Not For Use In Diagnostic Procedures.
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