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GRP94 Antibody
GRP94 Antibody, Clone 9G10
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, ICC, IP, FC |
|---|---|
| Primary Accession | P14625 |
| Other Accession | NP_003290.1 |
| Host | Rat |
| Isotype | IgG2a |
| Reactivity | Human, Mouse, Rat, Rabbit, Hamster, Monkey, Pig, Chicken, Xenopus, Bovine, Sheep, Horse, Guinea Pig, Dog |
| Clonality | Monoclonal |
| Description | Rat Anti-Chicken GRP94 Monoclonal IgG2a |
| Target/Specificity | Detects ~98kDa. Does not detect human HSP90, Grp74, or GrpE from E.coli. |
| Other Names | HSP90B1 Antibody, GP96 Antibody, TRA1 Antibody, ECGP Antibody |
| Clone Names | 9G10 |
| Immunogen | Purified Grp94 isolated from chicken oviducts |
| Purification | Protein G Purified |
| Storage | -20ºC |
| Storage Buffer | PBS pH7.2, 50% glycerol, 0.09% sodium azide |
| Shipping Temperature | Blue Ice or 4ºC |
| Certificate of Analysis | 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. |
| Cellular Localization | Endoplasmic Reticulum| Endoplasmic Reticulum Lumen | Melanosome |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Background
Grp94 (glucose regulated protein 94, gp96) is a constitutively expressed endoplasmic reticulum (ER) lumenal protein that is up-regulated in response to cellular stress such as heat shock, oxidative stress or glucose depletion. Grp94 is thought to play a role in protein translocation to the ER, in their subsequent folding and assembly, and in regulating protein secretion (1). Grp94 also plays a role in antigen presentation by accessing the endogenous pathway and eliciting specific CTL responses to chaperone bound peptides via MHC class I pathway (2). Grp94 is a member of the HSP90 family of stress proteins and shares sequence homology with its cytosolic equivalent, HSP90 (3). Both HSP90 and Grp94 are calcium binding proteins (4). Despite sharing 50% sequence homology over its N domains and complete conservation in its ligand binding domains with HSP90, Grp94 and HSP90 differ in their interactions with regulatory ligands as Grp94 has weak ATP binding and hydrolysis activity (5). Grp94 exists as a homodimer and the two subunits interact at two distinct intermolecular sites, C terminal dimerization domains and the N-terminal interacts with the middle domain of opposing subunits (6). Grp94 contains a carboxy terminal KDEL (Lys-Asp-Glu-Leu) sequence which is believed to aid in its retention in the ER (7).
References
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.
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