gp96/HSP90B1/GRP94 ELISA Development Kit

ELISA: Human, Mouse, Rat, Canine gp96/HSP90B1/GRP94 ELISA Kit (Colorimetric) [NBP2-62146] - Dose-response curves from cell lysates and microsomes diluted into assay buffer were compared to the recombinant Canine Grp94 standard curve. Parallelism indicates that the antibody-binding characteristics of the native and standard proteins are similar,

Product Discontinued

gp96/HSP90B1/GRP94 ELISA Development Kit Summary

• Description: Grp94 ELISA development set contains sufficient reagents for the development of 5 x 96 well ELISA plates which provides analysis of ~200 samples in duplicate
• Specificity: Cross reactivity with human Calreticulin, PDI, HSP90alpha, HSP90beta, HSP70, hamster Grp78 and bovine Hsc70 is less than 0.035%.
• Standard Curve Range: 6.25 - 200 ng/ml
• Sensitivity: 1.29 ng/ml
• Inter-Assay: N/A
• Intra-Assay: N/A
• Spike Recovery: N/A
• Sample Volume: 100 uL
• Kit Type: ELISA Development Kit
• Gene: HSP90B1

Applications/Dilutions

• Dilutions:
  • ELISA

Packaging, Storage & Formulations

• Storage: Store at 4°C.

Alternate Names for gp96/HSP90B1/GRP94 ELISA Development Kit

• 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. Kits are guaranteed for 6 months from date of receipt.

Bioinformatics

• Gene Symbol: HSP90B1