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Goat Anti-GPR94 / TRA1 Antibody
Peptide-affinity purified goat antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC, E |
|---|---|
| Primary Accession | P14625 |
| Other Accession | NP_003290, 7184, 22027 (mouse), 362862 (rat) |
| Reactivity | Mouse, Rat |
| Predicted | Human, Zebrafish, Pig, Dog, Cow |
| Host | Goat |
| Clonality | Polyclonal |
| Concentration | 100ug/200ul |
| Isotype | IgG |
| Calculated MW | 92469 Da |
| Gene ID | 7184 |
|---|---|
| Other Names | Endoplasmin, 94 kDa glucose-regulated protein, GRP-94, Heat shock protein 90 kDa beta member 1, Tumor rejection antigen 1, gp96 homolog, HSP90B1, GRP94, TRA1 |
| Format | 0.5 mg IgG/ml in Tris saline (20mM Tris pH7.3, 150mM NaCl), 0.02% sodium azide, with 0.5% bovine serum albumin |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | Goat Anti-GPR94 / TRA1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | HSP90B1 (HGNC:12028) |
|---|---|
| Synonyms | GRP94, TRA1 |
| Function | Molecular chaperone that functions in the processing and transport of secreted proteins (By similarity). When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD) (PubMed:18264092). Has ATPase activity (By similarity). May participate in the unfolding of cytosolic leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1 to facilitate their translocation into the ERGIC (endoplasmic reticulum- Golgi intermediate compartment) and secretion; the translocation process is mediated by the cargo receptor TMED10 (PubMed:32272059). |
| Cellular Location | Endoplasmic reticulum lumen. Sarcoplasmic reticulum lumen {ECO:0000250|UniProtKB:P41148}. Melanosome Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. |
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
HSP90 proteins are highly conserved molecular chaperones that have key roles in signal transduction, protein folding, protein degradation, and morphologic evolution. HSP90 proteins normally associate with other cochaperones and play important roles in folding newly synthesized proteins or stabilizing and refolding denatured proteins after stress. HSP90B1 is an endoplasmic reticulum HSP90 protein. Other HSP90 proteins are found in cytosol (see HSP90AA1; MIM 140571) and mitochondria (TRAP1; MIM 606219) (Chen et al., 2005 [PubMed 16269234]).
References
Variation at the NFATC2 Locus Increases the Risk of Thiazolinedinedione-Induced Edema in the Diabetes REduction Assessment with ramipril and rosiglitazone Medication (DREAM) Study. Bailey SD, et al. Diabetes Care, 2010 Jul 13. PMID 20628086.
Extracellular heat shock protein HSP90beta secreted by MG63 osteosarcoma cells inhibits activation of latent TGF-beta1. Suzuki S, et al. Biochem Biophys Res Commun, 2010 Jul 30. PMID 20599762.
Endoplasmic reticulum chaperone gp96 is essential for infection with vesicular stomatitis virus. Bloor S, et al. Proc Natl Acad Sci U S A, 2010 Apr 13. PMID 20351288.
Correlation between clinicopathology and expression of heat shock protein 72 and glycoprotein 96 in human esophageal squamous cell carcinoma. Wang X, et al. Clin Dev Immunol, 2010. PMID 20300187.
New genetic associations detected in a host response study to hepatitis B vaccine. Davila S, et al. Genes Immun, 2010 Apr. PMID 20237496.
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