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Western blotAntibody data
- Antibody Data
- Antigen structure
- References [13]
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- Product number
- ABIN1686653 - Provider product page
- Provider
- antibodies-online
- Product name
- anti-Heat Shock Protein 90kDa beta (Grp94), Member 1 (HSP90B1) (C-Term) antibody
- Antibody type
- Polyclonal
- Description
- Peptide Affinity Purified
- Reactivity
- Human, Mouse, Rat, Bovine
- Host
- Rabbit
- Epitope
- C-Term
- Vial size
- 100 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.
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
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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