Grp94 (Glucose-regulated protein 94) is an abundant resident endoplasmic reticulum (ER) lumenal stress protein, which together with cytosolic Hsp90 belongs to the Hsp90 family of molecular chaperones. Grp94 expression is upregulated by stress conditions such as glucose starvation and heat shock, which promote protein misfolding or unfolding. In addition to a homeostatic role in protein folding and assembly, Grp94 can function in the intracellular trafficking of peptides from the extracellular space to the MHC class I antigen processing pathway of antigen presentation cells.
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Product Details
Alternative Name |
Endoplasmin, Tra1, Hsp90B1, Gp96 |
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Application |
ICC, IHC (PS), IP, WB |
Application Notes |
Detects a band of ~94kDa by Western blot. |
Formulation |
Liquid. In PBS, pH 7.2, containing 50% glycerol and 0.09% sodium azide. |
Gene/Protein Identifier |
NP_035761 (RefSeq) |
Host |
Rabbit |
Immunogen |
Synthetic peptide corresponding to the sequence near the C-terminus of mouse Grp94. |
Purity Detail |
Protein A affinity purified. |
Recommendation Dilutions/Conditions |
Immunoprecipitation (1:80)Western Blot (1:1,000)Suggested dilutions/conditions may not be available for all applications.Optimal conditions must be determined individually for each application. |
Source |
Purified from rabbit serum. |
Species Reactivity |
Bovine, Human, Mouse, Rat |
UniProt ID |
P08113 |
Worry-free Guarantee |
This antibody is covered by our Worry-Free Guarantee. |
Handling & Storage
Handling |
Avoid freeze/thaw cycles. |
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Long Term Storage |
-20°C |
Shipping |
Blue Ice |
Regulatory Status |
RUO – Research Use Only |
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- CHIP Haploinsufficiency Exacerbates Hepatic Steatosis via Enhanced TXNIP Expression and Endoplasmic Reticulum Stress Responses: J.H. Han, et al.; Antioxidants 12, 458 (2023), Abstract
- Charcot-Marie-Tooth-1A and sciatic nerve crush rat models: insights from proteomics: Msheik, Z., Durand, S., et al.; Neural Regen. Res. 18, 1354 (2023), Abstract
- Viperin triggers ribosome collision-dependent translation inhibition to restrict viral replication: Hsu, J. C., Laurent-Rolle, M., et al.; Mol. Cell 82, 1631 (2022), Abstract
- Improved skeletal muscle fatigue resistance in experimental autoimmune myositis mice following high-intensity interval training: T. Yamdaa, et al.; Arthritis Res. Ther. 24, 156 (2022), Application(s): WB, Abstract
- PD-L1 in circulating exosomes of Merkel cell carcinoma: Zanella, A., Vautrot, V., et al.; Exp. Dermatol. 31, 869 (2022), Abstract
- Aberrant phosphorylation inactivates Numb in breast cancer causing expansion of the stem cell pool.: Filippone, M. G., Freddi, S., et al.; J. Cell Biol. 221, (2022), Application(s): WB, Abstract
- Suppression of ER-stress induction of GRP78 as an anti-neoplastic mechanism of the cardiac glycoside Lanatoside C in pancreatic cancer: Lanatoside C suppresses GRP78 stress inductio: D.P. Ha, et al.; Neoplasia 23, 1213 (2021), Abstract
- Endoplasmic reticulum oxidoreductase 1 alpha modulates prostate cancer hallmarks: Cornelius, J., Cavarretta, I., et al.; Transl. Androl. Urol. 10, 1110 (2021), Abstract
- Molecular adaptation to calsequestrin 2 (CASQ2) point mutations leading to catecholaminergic polymorphic ventricular tachycardia (CPVT): comparative analysis of R33Q and D307H mutants: G. Valle, et al.; J. Muscle Res. Cell Motil. 41, 251 (2020), Abstract — Full Text
- Cellular, Extracellular and Extracellular Vesicular miRNA Profiles of Pre-Ovulatory Follicles Indicate Signaling Disturbances in Polycystic Ovaries.: Fazeli, A., Andronowska, A., et al.; Int. J. Mol. Sci. 21, (2020), Application(s): WB / Reactant(s): Human, Abstract
- The HSP90 inhibitor, 17AAG, protects the intestinal stem cell niche and inhibits graft versus host disease development: A.L. Joly, et al.; Oncogene 35, 2842 (2016), Application(s): Western Blot, Abstract
- Characterization and Mechanism of Stress-induced Translocation of 78-kilodalton Glucose Regulated Protein (GRP78) to the Cell Surface: Y.L. Tsai, et al.; J. Biol. Chem. 290, 8049 (2015), Application(s): Western Blotting, Abstract — Full Text
- The molecular chaperone gp96/GRP94 interacts with Toll-like receptors and integrins via its C-terminal hydrophobic domain: S. Wu, et al.; J. Biol. Chem. 287, 6735 (2012), Abstract
- Heat shock protein gp96 is a master chaperone for toll-like receptors and is important in the innate function of macrophages: Z. Li, et al.; Immunity 26, 215 (2007), Application(s): WB, IP using mouse & human cell lysates & tissue culture, Abstract
- Induction of GRP78 by ischemic preconditioning reduces endoplasmic reticulum stress and prevents delayed neuronal cell death: P.H. Chan, et al.; J. Cereb. Blood Flow Metab. 23, 949 (2003), Application(s): WB, IHC using rat samples, Abstract
- Human U251MG glioma cells expressing the membrane form of macrophage colony-stimulating factor (mM-CSF) are killed by human monocytes in vitro and are rejected within immunodeficient mice via paraptosis that is associated with increased expression of three different heat shock proteins: M.R. Jadus, et al.; Cancer Gene Ther. 10, 411 (2003), Application(s): IHC using human tissue, Abstract
- Early intraneuronal Abeta deposition in the hippocampus of APP transgenic mice: L.W. Jin, et al.; Neuroreport 14, 123 (2003), Application(s): ICC using mouse samples, Abstract
- Overexpression of glucose-regulated protein94 (Grp94) in esophageal adenocarcinomas of a rat surgical model and humans: C.S. Yang, et al.; Carcinogenesis 23, 123 (2002), Application(s): IHC, WB using rat & human samples, Abstract
- The C-terminal domain of human grp94 protects the catalytic subunit of protein kinase CK2 (CK2 alpha) against thermal aggregation – role of disulfide bonds: E. Itarte, et al.; Eur. J. Biochem. 268, 429 (2001), Application(s): WB using human samples, Abstract
- Iodoacetate protects hippocampal neurons against excitotoxic and oxidative injury: involvement of heat-shock proteins and Bcl-2: M. Mattson, et al.; J. Neurochem. 79, 361 (2001), Application(s): WB using rat samples, Abstract
- A novel human cytomegalovirus glycoprotein, gpUS9, which promotes cell-to-cell spread in polarized epithelial cells, colocalizes with the cytoskeletal proteins E-cadherin and F-actin: L. Pereira, et al.; J. Virol. 72, 5717 (1998), Application(s): ICC using canine samples, Abstract
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