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Mouse Anti-AHSA1 Recombinant Antibody (V2-634175) (CBMAB-AP210LY)


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Summary

Host Animal
Mouse
Specificity
Human, Mouse
Clone
V2-634175
Antibody Isotype
IgG1, κ
Application
ICC/IF, ELISA, WB

Basic Information

Immunogen
Human Aha1, his tagged
Host Species
Mouse
Specificity
Human, Mouse
Antibody Isotype
IgG1, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:1,000
IF(ICC)1:100

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

Format
Liquid
Buffer
PBS, pH7.2, 50% glycerol
Preservative
0.09% sodium azide
Concentration
1 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
UniProt ID
HumanO95433
MouseQ8BK64
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.

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