HSP90 (C45G5) Rabbit mAb (HRP Conjugate) #79641

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Supporting Data

REACTIVITY	H M R Mk
SENSITIVITY	Endogenous
MW (kDa)	90
Source/Isotype	Rabbit IgG

Application Key:

WB-Western Blotting

Species Cross-Reactivity Key:

H-Human
M-Mouse
R-Rat
Mk-Monkey

Product Information

Product Description

This Cell Signaling Technology antibody is conjugated to the carbohydrate groups of horseradish peroxidase (HRP) via its amine groups. The HRP conjugated antibody is expected to exhibit the same species cross-reactivity as the unconjugated HSP90 (C45G5) Rabbit mAb #4877.

MW (kDa)

Product Usage Information

Application	Dilution
Western Blotting	1:1000

Storage

Supplied in 136 mM NaCl, 2.6 mM KCl, 12 mM sodium phosphate (pH 7.4) dibasic, 2 mg/ml BSA, and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

Protocol

Specificity / Sensitivity

HSP90 (C45G5) Rabbit mAb (HRP Conjugate) detects endogenous levels of total HSP90 protein. This antibody does not cross-react with other HSPs.

Species Reactivity:

Human, Mouse, Rat, Monkey

The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.

Species predicted to react based on 100% sequence homology:

Bovine

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide surrounding Asn300 of human HSP90.

Background

HSP70 and HSP90 are molecular chaperones expressed constitutively under normal conditions to maintain protein homeostasis and are induced upon environmental stress (1). Both HSP70 and HSP90 are able to interact with unfolded proteins to prevent irreversible aggregation and catalyze the refolding of their substrates in an ATP- and co-chaperone-dependent manner (1). HSP70 has a broad range of substrates including newly synthesized and denatured proteins, while HSP90 tends to have a more limited subset of substrates, most of which are signaling molecules. HSP70 and HSP90 often function collaboratively in a multi-chaperone system, which requires a minimal set of co-chaperones: HSP40, Hop, and p23 (2,3). The co-chaperones either regulate the intrinsic ATPase activity of the chaperones or recruit chaperones to specific substrates or subcellular compartments (1,4). When the ubiquitin ligase CHIP associates with the HSP70/HSP90 complex as a cofactor, the unfolded substrates are subjected to degradation by the proteasome (4). The biological functions of HSP70/HSP90 extend beyond their chaperone activity. They are essential for the maturation and inactivation of nuclear hormones and other signaling molecules (1,3). They also play a role in vesicle formation and protein trafficking (2).

Database Links

UniProt ID: P08238 , P07900

Entrez-Gene Id: 3326 , 3320

Limited Uses

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For Research Use Only. Not For Use In Diagnostic Procedures.

Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.

U.S. Patent No. 7,429,487, foreign equivalents, and child patents deriving therefrom.

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