HSP90B1 antibody
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Description
HSP90 proteins are highly conserved molecular chaperones, which normally associate with other cochaperones and play important roles in folding newly synthesized proteins or stabilizing and refolding denatured proteins after stress. HSP90B1(GP96 or GRP94) is an endoplasmic reticulum paralogue of the cytosolic HSP90. As a major ER chaperone to mediate the UPR and a master chaperone for Toll-like receptors(TLRs), HSP90b1 chaperones peptides to MHC class I molecules of dendritic cells and other antigen-presenting cells, as well as facilitating the assembly of immunoglobulin. The protein is also involved in many other bio-processes. This antibody was generated against the C-terminal region of full-length HSP90b1.
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Product specifications
| Category | Primary Antibodies |
| Immunogen Target | heat shock protein 90kDa beta(Grp94), member 1 (HSP90B1) |
| Host | Rabbit |
| Reactivity | Human, Mouse, Rat |
| Recommended Dilution | WB: 1:1000-1:4000; IP: 1:500-1:2000; IHC: 1:20-1:200; IF: 1:20-1:200 |
| Clonality | polyclonal |
| Conjugation | Unconjugated |
| Isotype | IgG |
| Observed MW | 94 kDa |
| Purity | ≥95% as determined by SDS-PAGE |
| Purification | Immunogen affinity purified |
| Size 1 | 100µg |
| Form | liquid |
| Tested Applications | ELISA, WB, IHC, FC, IF, IP |
| Storage | PBS with 0.02% sodium azide and 50% glycerol pH 7.3, -20℃ for 12 months(Avoid repeated freeze / thaw cycles.) |
| UniProt ID | P14625 |
| Alias | 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 |
| Background | Antibody anti-HSP90B1 |
| Status | RUO |
| Note | Mol. Weight 94 kDa |
Descripción
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HSP90B1 antibody
HSP90 proteins are highly conserved molecular chaperones, which normally associate with other cochaperones and play important roles in folding newly synthesized proteins or stabilizing and refolding denatured proteins after stress. HSP90B1(GP96 or GRP94) is an endoplasmic reticulum paralogue of the cytosolic HSP90. As a major ER chaperone to mediate the UPR and a master chaperone for Toll-like receptors(TLRs), HSP90b1 chaperones peptides to MHC class I molecules of dendritic cells and other antigen-presenting cells, as well as facilitating the assembly of immunoglobulin. The protein is also involved in many other bio-processes. This antibody was generated against the C-terminal region of full-length HSP90b1.
Ver Producto