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Rat Anti-AHSA1 Recombinant Antibody (V2-634174) (CBMAB-AP209LY)

Published Data

Summary

Host Animal
Rat
Specificity
Human, Mouse, Rat
Clone
V2-634174
Antibody Isotype
IgG2a, κ
Application
ICC/IF, ELISA, IHC, IP, WB

Basic Information

Immunogen
Recombinant Full Length Mouse Aha1 Protein.
Host Species
Rat
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG2a, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:1,000
IP1:1,000
IF(ICC)1:1,000
IHC1:100

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS
Preservative
None
Concentration
1.2 mg/ml
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
Activator Of HSP90 ATPase Activity 1
Introduction
Acts as a co-chaperone of HSP90AA1. Activates the ATPase activity of HSP90AA1 leading to increase in its chaperone activity. Competes with the inhibitory co-chaperone FNIP1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (PubMed:27353360).
Entrez Gene ID
Human10598
Mouse217737
Rat681996
UniProt ID
HumanO95433
MouseQ8BK64
RatB0BN63
Alternative Names
Activator Of HSP90 ATPase Activity 1; C14orf3; AHA1; P38; AHA1, Activator Of Heat Shock 90kDa Protein ATPase Homolog 1 (Yeast); AHA1, Activator Of Heat Shock 90kDa Protein ATPase Homolog 1; Activator Of 90 KDa Heat Shock Protein ATPase Homolog 1; Chromosome 14 Open Reading Frame 3; HAha1;
Function
Acts as a co-chaperone of HSP90AA1 (PubMed:29127155). Activates the ATPase activity of HSP90AA1 leading to increase in its chaperone activity (PubMed:29127155). Competes with the inhibitory co-chaperone FNIP1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (PubMed:27353360). Competes with the inhibitory co-chaperone TSC1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (PubMed:29127155).
Biological Process
Positive regulation of ATPase activity
Protein folding
Viral process
Cellular Location
Cytosol; Endoplasmic reticulum. May transiently interact with the endoplasmic reticulum.
PTM
Phosphorylation at Tyr-223 enhances binding to chaperone HSP90AA1.
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For research use only. Not intended for any clinical use.

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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