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Heat Shock Protein 90kDa beta (Grp94), Member 1 (HSP90B1) antibody

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Chicken, Cow (Bovine), Dog (Canine), Guinea Pig, Hamster, Horse (Equine), Human, Monkey, Mouse (Murine), Pig (Porcine), Rabbit, Rat (Rattus), Sheep (Ovine), Xenopus laevis
(267), (140), (98), (68), (58), (35), (34), (34), (33), (32), (31), (31), (29), (28), (5), (3), (2), (2), (1), (1)
(214), (71), (26), (18), (2)
Clonality (Clone)
Monoclonal ()
(17), (15), (12), (12), (9), (9), (4), (4), (4), (4), (4), (4), (4), (4), (4), (4), (4), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Immunocytochemistry (ICC), Flow Cytometry (FACS), Immunofluorescence (IF), Immunoprecipitation (IP), Western Blotting (WB)
(277), (139), (107), (96), (93), (91), (76), (67), (11), (7), (7), (3), (1), (1), (1)
Pubmed 14 references available
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Quantity 200 μg
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Availability Will be delivered in 3 to 4 Business Days
Immunogen Purified Grp94 isolated from chicken oviducts
Clone 9G10
Specificity Detects ~98 kDa. Does not detect human HSP90, Grp74, or GrpE from E.coli.
Sensitivity 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.
Purification Protein G Purified
Alternative Name GRP94 (HSP90B1 Antibody Abstract)
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).
Cellular Localization: Endoplasmic Reticulum| Endoplasmic Reticulum Lumen | Melanosome
Gene ID 7184
NCBI Accession NP_003290
UniProt P14625
Research Area Cancer, Organelles
Application Notes Recommended Dilution: WB (1:2000), ICC/IF (1:100), optimal dilutions for assays should be determined by the user.
Restrictions For Research Use only
Format Liquid
Concentration 1 mg/mL
Buffer PBS pH 7.2, 50 % glycerol, 0.09 % sodium azide
Preservative Sodium azide
Precaution of Use This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Background publications Chu, Maynard, Chiosis et al.: "Identification of novel quaternary domain interactions in the Hsp90 chaperone, GRP94." in: Protein science : a publication of the Protein Society, Vol. 15, Issue 6, pp. 1260-9, 2006 (PubMed).

Soldano, Jivan, Nicchitta et al.: "Structure of the N-terminal domain of GRP94. Basis for ligand specificity and regulation." in: The Journal of biological chemistry, Vol. 278, Issue 48, pp. 48330-8, 2003 (PubMed).

Sato, Torimoto, Tamura et al.: "Immunotherapy using heat-shock protein preparations of leukemia cells after syngeneic bone marrow transplantation in mice." in: Blood, Vol. 98, Issue 6, pp. 1852-7, 2001 (PubMed).

Gusarova, Caplan, Brodsky et al.: "Apoprotein B degradation is promoted by the molecular chaperones hsp90 and hsp70." in: The Journal of biological chemistry, Vol. 276, Issue 27, pp. 24891-900, 2001 (PubMed).

Yun, Gärtner, Arendt et al.: "Increase in vulnerability of middle-aged rat brain to lead by cerebral energy depletion." in: Brain research bulletin, Vol. 52, Issue 5, pp. 371-8, 2000 (PubMed).

Allen, Abuzenadah, Hinks et al.: "A novel von Willebrand disease-causing mutation (Arg273Trp) in the von Willebrand factor propeptide that results in defective multimerization and secretion." in: Blood, Vol. 96, Issue 2, pp. 560-8, 2000 (PubMed).

Riera, Roher, Miró et al.: "Association of protein kinase CK2 with eukaryotic translation initiation factor eIF-2 and with grp94/endoplasmin." in: Molecular and cellular biochemistry, Vol. 191, Issue 1-2, pp. 97-104, 1999 (PubMed).

Hoshino, Wang, Devetten et al.: "Molecular chaperone GRP94 binds to the Fanconi anemia group C protein and regulates its intracellular expression." in: Blood, Vol. 91, Issue 11, pp. 4379-86, 1998 (PubMed).

Choukhi, Ung, Wychowski et al.: "Involvement of endoplasmic reticulum chaperones in the folding of hepatitis C virus glycoproteins." in: Journal of virology, Vol. 72, Issue 5, pp. 3851-8, 1998 (PubMed).

Ruddon, Bedows: "Assisted protein folding." in: The Journal of biological chemistry, Vol. 272, Issue 6, pp. 3125-8, 1997 (PubMed).

Srivastava, Udono, Blachere et al.: "Heat shock proteins transfer peptides during antigen processing and CTL priming." in: Immunogenetics, Vol. 39, Issue 2, pp. 93-8, 1994 (PubMed).

Mazzarella, Green: "ERp99, an abundant, conserved glycoprotein of the endoplasmic reticulum, is homologous to the 90-kDa heat shock protein (hsp90) and the 94-kDa glucose regulated protein (GRP94)." in: The Journal of biological chemistry, Vol. 262, Issue 18, pp. 8875-83, 1987 (PubMed).

Kang, Welch: "Characterization and purification of the 94-kDa glucose-regulated protein." in: The Journal of biological chemistry, Vol. 266, Issue 9, pp. 5643-9, 1991 (PubMed).

Peter, Nguyen Van, Söling: "Different sorting of Lys-Asp-Glu-Leu proteins in rat liver." in: The Journal of biological chemistry, Vol. 267, Issue 15, pp. 10631-7, 1992 (PubMed).

Catalog No. ABIN361654
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