ELISA: Mouse gp96/HSP90B1/GRP94 ELISA Kit (Colorimetric) [NBP2-76452] - Samples were spiked with high concentrations of Mouse gp96/HSP90B1/GRP94 and diluted with Reference Standard & Sample Diluent to produce samples ...read more
Storage of components varies. See protocol for specific instructions.
Kit Components
Components
Biotinylated Detection Ab Diluent
Concentrated Biotinylated Detection Ab (100x)
Concentrated HRP Conjugate (100x)
Concentrated Wash Buffer (25x)
HRP Conjugate Diluent
Micro ELISA Plate (Dismountable)
Plate Sealer
Product Manual
Reference Standard
Sample Diluent
Stop Solution
Substrate Reagent
Alternate Names for Mouse gp96/HSP90B1/GRP94 ELISA Kit (Colorimetric)
94 kDa glucose-regulated protein
ECGP
Endoplasmin
endothelial cell (HBMEC) glycoprotein
glucose regulated protein, 94 kDa
gp96
GP96ECGP
Grp94
GRP-94
GRP94gp96 homolog
Heat shock protein 90 kDa beta member 1
heat shock protein 90kDa beta (Grp94), member 1
HSP90B1
TRA1endoplasmin
tumor rejection antigen (gp96) 1
Tumor rejection antigen 1
Tumor rejection antigen-1 (gp96)
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. ELISA Kits are guaranteed for 6 months from date of receipt.
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