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AHA-1 antibody

Anti-AHA-1 antibody used in Western Blot (WB). GTX48723

Cat No. GTX48723

Host

Rabbit

Clonality

Polyclonal

Isotype

IgG

Application

WB, ELISA, IHC

Reactivity

Human, Chimpanzee
Package
50 μg ($289)

APPLICATION

Application Note

*Optimal dilutions/concentrations should be determined by the researcher.
Application Dilution
WB 1 μg/mL
ELISA 1:35000 - 1:185000
IHC Assay dependent
Not tested in other applications.

Calculated MW

38 kDa. ( Note )

PROPERTIES

Form

Liquid

Buffer

0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2 and 0.01% (w/v) Sodium Azide

Storage

Store as concentrated solution. Centrifuge briefly prior to opening vial. For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.

Concentration

1 mg/ml (Please refer to the vial label for the specific concentration.)

Antigen Species

Human

Immunogen

This affinity purified antibody was prepared from whole rabbit serum produced by repeated immunizations with a synthetic peptide corresponding to an internal region of human AHA1 protein.

Purification

Purified by antigen-affinity chromatography.

Conjugation

Unconjugated

Note

For laboratory use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.

TARGET

Synonyms

activator of HSP90 ATPase activity 1 , AHA1 , C14orf3 , hAha1 , p38

Cellular Localization

Cytoplasm, cytosol,Endoplasmic reticulum

Background

Activator of Hsp90 ATPase (AHA1) stimulates the inherent ATPase cycle of Hsp90, which is essential for its chaperone activity in vivo. The activation and/or stability of many of the key regulatory and signaling proteins of the eukaryotic cell depend on their interaction with the Hsp90 molecular chaperone. Hsp90 is assisted and regulated by co-chaperones that participate in an ordered series both to assist client-protein recruitment or release and to modulate progress through the ATPase coupled chaperone cycle. Structural analysis and mutagenesis show that binding of the N-terminal domain of AHA1 to Hsp90 promotes a conformational switch in the middle-segment catalytic loop (aa 370–390) of Hsp90 that exposes the catalytic Arg380 and enables its interaction with ATP in the N-terminal nucleotide-binding domain of the chaperone. Recent studies show that AHA1 modulates Hsp90-dependent stability of the folding of the cystic fibrosis transmembrane conductance regulator (CFTR) in the endoplasmic reticulum (ER). Down-regulation of AHA1 rescues misfolding of CFTR in cystic fibrosis.

Database

Research Area

DATA IMAGES

Anti-AHA-1 antibody used in Western Blot (WB). GTX48723

GTX48723 WB Image

Western blot using GeneTex's affinity purified anti-AHA1 antibody shows detection of AHA1 in Cos7 cells. For Lanes 2 and 4, Cos7 cells were transfected with pcDNA3-FLAG-AHA1. For Lanes 1 and 3, Cos7 cells were not transfected. Extracts (40 μg per lane) were electrophoresed and transferred to nitrocellulose. The membrane was probed with anti-AHA1 (lanes 1 and 2, 1:2,000 dilution) or anti-FLAG (lanes 3 and 4). The lower band seen in anti-AHA1 blotting (arrowhead) is endogenous AHA1.

REFERENCE

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REVIEW

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SDS
Sodium Azide.pdf