GRP94 Antibody, Clone 9G10: ATTO 390

GRP94 (also known as gp96) is a constitutively expressed ER-resident chaperone and a member of the HSP90 family. It is upregulated in response to cellular stressors such as heat shock, oxidative damage, and glucose deprivation—conditions frequently observed in neurodegenerative diseases. Functionally, GRP94 supports protein translocation, folding, and quality control within the ER. It also plays a key role in immune regulation by facilitating antigen presentation through the MHC class I pathway, linking ER stress to immune responses. In the nervous system, GRP94 contributes to proteostasis and immune surveillance, both of which are disrupted in diseases like Alzheimer’s and Parkinson’s. Structurally, GRP94 forms homodimers and contains a KDEL sequence that ensures ER retention. Despite its homology with cytosolic HSP90, GRP94 exhibits distinct ATP-binding and hydrolysis characteristics, making it a unique therapeutic target. Its dual role in stress adaptation and immune signaling positions GRP94 as a valuable biomarker and potential intervention point in neurodegenerative disease research.

HSP90B1, GP96, TRA1, ECGP, 94 kDa glucose regulated protein, 94 kDa glucose-regulated protein, Endoplasmin, Endothelial cell (HBMEC) glycoprotein, ENPL_HUMAN, Glucose regulated protein 94kDa, gp96, gp96 homolog, GRP 94, GRP-94, Heat shock protein 90 kDa beta member 1, heat shock protein 90kDa beta (Grp94), member 1, Heat shock protein, 90 kDa, beta, 1, Stress inducible tumor rejection antigen GP96, tumor rejection antigen (gp96) 1, Tumor rejection antigen 1, Tumor rejection antigen gp96, Tumor rejection antigen-1 (gp96)

Cancer | Heat Shock | Cell Signaling | Protein Trafficking | ER Proteins | Tags and Cell Markers | Organelle Markers | Cancer | Cancer Metabolism | Response to Hypoxia | Cell Signaling | Metabolism | Metabolism processes | Hypoxia

0.5 µg/ml of SMC-105 was sufficient for detection of Grp94 in 20 µg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-rat IgG:HRP as the secondary antibody.

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1. Rudolph R.W., and Bedows E. (1997) J Biol Chem 272: 3125-3128. 2. Srivastava P.K., et al. (1994) Immunogenetics. 39 (2) :93-98. 3. Mazzarella R.A., and Green M. (1987) J Biol Chem 262:8875-8883. 4. Kang, H.S. and Welch W.J. (1991) J Biol Chem 266 (9) :5643-5649. 5. Soldano K.L., et al. (2003) J Biol Chem 278 (48) : 48330-48338. 6. Chu F., et al. (2006) Protein Sci 15 (6) : 1260-1269. 7. Peter F., et al., (1992) J Biol Chem 267: 10631-10637. 8. Allen S. et al. (2000) Blood 96 (2) : 560-568. 9. Sato K et al. (2001) Blood 98 (6) : 1852-1857. 10. Yun S.-W. et al (2000) Brain Research Bulletin.52 (5) :371-378. 11. Choukhi A., et al. (1998) J. Virol. 72: 3851-3858. 12. Hoshino T., et al. (1998) Blood 91 (11) : 4379-4386. 13. Riera M. et al. (1999) Mol. Cell Biochem. 191: 97-104. 14. Gusarova V., et al. (2001) J. Biol. Chem. 276 (27) : 24891-24900.

Human | Mouse | Rat | Bovine | Dog | Chicken | Guinea Pig (Cavia porcellus) | Hamster | Horse | Monkey | Pig | Rabbit | Sheep | African clawed frog (Xenopus laevis)