Antibody data
- Antibody Data
- Antigen structure
- References [14]
- Comments [0]
- Validations [0]
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- Product number
- ABIN361654 - Provider product page
- Provider
- antibodies-online
- Proper citation
- Antibodies-Online Cat#ABIN361654, RRID:AB_10772380
- Product name
- anti-Heat Shock Protein 90kDa beta (Grp94), Member 1 (HSP90B1) antibody
- Antibody type
- Monoclonal
- Description
- Protein G Purified
- Reactivity
- Human, Mouse, Rat, Bovine, Canine, Chicken/Avian, Guinea Pig, Hamster, Horse, Porcine, Rabbit, Sheep, Simian, Xenopus
- Host
- Rat
- Isotype
- IgG
- Antibody clone number
- 9G10
- Vial size
- 200 μg
- Storage
- -20°C
Submitted references Identification of novel quaternary domain interactions in the Hsp90 chaperone, GRP94.
Structure of the N-terminal domain of GRP94. Basis for ligand specificity and regulation.
Immunotherapy using heat-shock protein preparations of leukemia cells after syngeneic bone marrow transplantation in mice.
Apoprotein B degradation is promoted by the molecular chaperones hsp90 and hsp70.
A novel von Willebrand disease-causing mutation (Arg273Trp) in the von Willebrand factor propeptide that results in defective multimerization and secretion.
Increase in vulnerability of middle-aged rat brain to lead by cerebral energy depletion.
Association of protein kinase CK2 with eukaryotic translation initiation factor eIF-2 and with grp94/endoplasmin.
Involvement of endoplasmic reticulum chaperones in the folding of hepatitis C virus glycoproteins.
Molecular chaperone GRP94 binds to the Fanconi anemia group C protein and regulates its intracellular expression.
Assisted protein folding.
Heat shock proteins transfer peptides during antigen processing and CTL priming.
Different sorting of Lys-Asp-Glu-Leu proteins in rat liver.
Characterization and purification of the 94-kDa glucose-regulated protein.
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).
Chu F, Maynard JC, Chiosis G, Nicchitta CV, Burlingame AL
Protein science : a publication of the Protein Society 2006 Jun;15(6):1260-9
Protein science : a publication of the Protein Society 2006 Jun;15(6):1260-9
Structure of the N-terminal domain of GRP94. Basis for ligand specificity and regulation.
Soldano KL, Jivan A, Nicchitta CV, Gewirth DT
The Journal of biological chemistry 2003 Nov 28;278(48):48330-8
The Journal of biological chemistry 2003 Nov 28;278(48):48330-8
Immunotherapy using heat-shock protein preparations of leukemia cells after syngeneic bone marrow transplantation in mice.
Sato K, Torimoto Y, Tamura Y, Shindo M, Shinzaki H, Hirai K, Kohgo Y
Blood 2001 Sep 15;98(6):1852-7
Blood 2001 Sep 15;98(6):1852-7
Apoprotein B degradation is promoted by the molecular chaperones hsp90 and hsp70.
Gusarova V, Caplan AJ, Brodsky JL, Fisher EA
The Journal of biological chemistry 2001 Jul 6;276(27):24891-900
The Journal of biological chemistry 2001 Jul 6;276(27):24891-900
A novel von Willebrand disease-causing mutation (Arg273Trp) in the von Willebrand factor propeptide that results in defective multimerization and secretion.
Allen S, Abuzenadah AM, Hinks J, Blagg JL, Gursel T, Ingerslev J, Goodeve AC, Peake IR, Daly ME
Blood 2000 Jul 15;96(2):560-8
Blood 2000 Jul 15;96(2):560-8
Increase in vulnerability of middle-aged rat brain to lead by cerebral energy depletion.
Yun SW, Gärtner U, Arendt T, Hoyer S
Brain research bulletin 2000 Jul 15;52(5):371-8
Brain research bulletin 2000 Jul 15;52(5):371-8
Association of protein kinase CK2 with eukaryotic translation initiation factor eIF-2 and with grp94/endoplasmin.
Riera M, Roher N, Miró F, Gil C, Trujillo R, Aguilera J, Plana M, Itarte E
Molecular and cellular biochemistry 1999 Jan;191(1-2):97-104
Molecular and cellular biochemistry 1999 Jan;191(1-2):97-104
Involvement of endoplasmic reticulum chaperones in the folding of hepatitis C virus glycoproteins.
Choukhi A, Ung S, Wychowski C, Dubuisson J
Journal of virology 1998 May;72(5):3851-8
Journal of virology 1998 May;72(5):3851-8
Molecular chaperone GRP94 binds to the Fanconi anemia group C protein and regulates its intracellular expression.
Hoshino T, Wang J, Devetten MP, Iwata N, Kajigaya S, Wise RJ, Liu JM, Youssoufian H
Blood 1998 Jun 1;91(11):4379-86
Blood 1998 Jun 1;91(11):4379-86
Assisted protein folding.
Ruddon RW, Bedows E
The Journal of biological chemistry 1997 Feb 7;272(6):3125-8
The Journal of biological chemistry 1997 Feb 7;272(6):3125-8
Heat shock proteins transfer peptides during antigen processing and CTL priming.
Srivastava PK, Udono H, Blachere NE, Li Z
Immunogenetics 1994;39(2):93-8
Immunogenetics 1994;39(2):93-8
Different sorting of Lys-Asp-Glu-Leu proteins in rat liver.
Peter F, Nguyen Van P, Söling HD
The Journal of biological chemistry 1992 May 25;267(15):10631-7
The Journal of biological chemistry 1992 May 25;267(15):10631-7
Characterization and purification of the 94-kDa glucose-regulated protein.
Kang HS, Welch WJ
The Journal of biological chemistry 1991 Mar 25;266(9):5643-9
The Journal of biological chemistry 1991 Mar 25;266(9):5643-9
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).
Mazzarella RA, Green M
The Journal of biological chemistry 1987 Jun 25;262(18):8875-83
The Journal of biological chemistry 1987 Jun 25;262(18):8875-83
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