gp96/HSP90B1/GRP94 Antibody Blocking Peptide

Novus Biologicals, part of Bio-Techne | Catalog # NBP2-24698PEP

Novus Biologicals, part of Bio-Techne
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Key Product Details

Conjugate

Unconjugated

Applications

Antibody Competition

View all gp96/HSP90B1 Proteins and Enzymes »

Product Specifications

Description

Application Notes

This peptide is useful as a blocking peptide for NBP2-24698. For further blocking peptide related protocol, click here.

Specificity

This peptide is specific for NBP2-24698 only.

Protein / Peptide Type

Antibody Blocking Peptide

Formulation, Preparation and Storage

NBP2-24698PEP
Formulation Peptide dissolved in dH20. Contains no BSA.
Preservative No Preservative
Concentration 1 mg/ml
Shipping The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Store at -80C. Avoid freeze-thaw cycles.

Background: gp96/HSP90B1

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).

Long Name

Heat Shock Protein 90 beta 1

Alternate Names

ECGP, Endoplasmin, Grp94, HSP90B1

Gene Symbol

HSP90B1

Additional gp96/HSP90B1 Products

Product Documents for gp96/HSP90B1/GRP94 Antibody Blocking Peptide

Product Datasheets

Certificate of Analysis

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Product Specific Notices for gp96/HSP90B1/GRP94 Antibody Blocking Peptide

This product is for research use only and is not approved for use in humans or in clinical diagnosis. This product is guaranteed for 1 year from date of receipt.

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