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HSP90B1 Antibody (Center) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | P14625 |
|---|---|
| Clone Names | 101008126 |
| 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 | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. 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 chaperonesthat have key roles in signal transduction, protein folding,protein degradation, and morphologic evolution. HSP90 proteinsnormally associate with other cochaperones and play important rolesin folding newly synthesized proteins or stabilizing and refoldingdenatured proteins after stress. HSP90B1 is an endoplasmicreticulum 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
Bailey, S.D., et al. Diabetes Care 33(10):2250-2253(2010)Suzuki, S., et al. Biochem. Biophys. Res. Commun. 398(3):525-531(2010)Bloor, S., et al. Proc. Natl. Acad. Sci. U.S.A. 107(15):6970-6975(2010)Davila, S., et al. Genes Immun. 11(3):232-238(2010)Wang, X., et al. Clin. Dev. Immunol. 2010, 212537 (2010) :
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