gp96/HSP90B1/GRP94 Antibody (9G10) Summary
Immunogen |
Chick oviduct GRP94. |
Localization |
Endoplasmic reticulum |
Marker |
ER Stress Marker |
Specificity |
GRP94 (9G10) |
Isotype |
IgG2a |
Clonality |
Monoclonal |
Host |
Rat |
Gene |
HSP90B1 |
Purity |
Unpurified |
Innovator's Reward |
Test in a species/application not listed above to receive a full credit towards a future purchase. |
Applications/Dilutions
Dilutions |
- Immunocytochemistry
- Immunocytochemistry/Immunofluorescence 1:250
- Immunohistochemistry 1:10 - 1:500
- Immunohistochemistry-Paraffin 1:20
- Immunoprecipitation 1:10 - 1:500
- Western Blot 1:100 - 1:1000
|
Application Notes |
WB: Detects an approx. 108 kDa protein representing GRP94 in chick oviduct cytosol. |
Publications |
|
Packaging, Storage & Formulations
Storage |
Store at -20C. Avoid freeze-thaw cycles. |
Buffer |
Ascites |
Preservative |
0.05% Sodium Azide |
Purity |
Unpurified |
Alternate Names for gp96/HSP90B1/GRP94 Antibody (9G10)
Background
Glucose-regulated protein 94, also known as Grp94 or gp96, is an abundant resident endoplasmic reticulum (ER) lumenal stress protein which together with cytosolic Hsp90 belongs to the Hsp90 family of molecular chaperones. Grp94 and other resident soluble proteins of the ER such as members of the Ca(2+) binding protein subfamily (CaBP), CaBPI and CaBP2 as well as calreticulin, possess the COOH-terminal tetrapeptide Lys-Asp-Glu-Leu (KDEL) which is a sorting signal that is thought to lead to the retention of these proteins in the pre-Golgi compartments (1). Grp94 expression is upregulated by stress conditions such as lucose starvation and heat shock, which promote protein misfolding or unfolding (2). In addition to a homeostatic role in protein folding and assembly, Grp94 can function in the intracellular trafficking of peptides from the extracellular space to the MHC class I antigen processing pathway of antigen presentation cells (3,4). Grp94 and Hsp90 share high sequence identity and presumably identical adenosine nucleotide-dependent modes of regulation. Earlier data suggests that Hsp90 and Grp94 may differ in their nucleotide binding properties. The N-terminal domain of eukaryotic Hsp90 proteins contains a conserved adenosine nucleotide binding pocket which also serves as the inding site for the Hsp90 inhibitors geldanamycin and radicicol. However, the molecular basis for adenosine nucleotide-dependent regulation of Grp94remains to be established. Recent data has entified a ligand dependent regulation of Grp94 function and suggest a model whereby Grp94 function is regulated through a ligand-dependent conversion of Grp94 from an inactive to an active conformation (5, 6).
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are
guaranteed for 1 year from date of receipt.
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Publications for gp96/HSP90B1/GRP94 Antibody (NB300-619)(1)
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