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AB245933

Recombinant Human AHA1 protein (His tag)

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Recombinant Human AHA1 protein (His tag) is a Human Full Length protein, in the 1 to 338 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, WB, FuncS.

View Alternative Names

C14orf3, HSPC322, AHSA1, Activator of 90 kDa heat shock protein ATPase homolog 1, AHA1, p38

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SDS-PAGE - Recombinant Human AHA1 protein (His tag) (AB245933)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human AHA1 protein (His tag) (AB245933)

SDS-PAGE analysis of ab245933.

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

WB, SDS-PAGE, FuncS

applications

Biologically active

No

Accession

O95433

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.2 Constituents: 10% Glycerol (glycerin, glycerine), 0.477% HEPES, 0.468% Sodium chloride

storage-buffer

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Complementary Products

Primary Antibodies

AB307716

Anti-AHA1 antibody [EPR26852-47]

20ul selling size|RabMAb|Recombinant|Trial Size

Immunoprecipitation - Anti-AHA1 antibody [EPR26852-47] (AB307716)

  • 0
  • 0
Secondary Antibodies

AB150077

Goat Anti-Rabbit IgG H&L (Alexa Fluor® 488)

Immunocytochemistry/ Immunofluorescence - Goat Anti-Rabbit IgG H&L (Alexa Fluor® 488) (AB150077)

  • 5
  • 20
Proteins & Peptides

AB84704

Recombinant Human Vimentin protein (Tagged-His Tag)

SDS-PAGE - Recombinant Human Vimentin protein (Tagged-His Tag) (AB84704)

  • 0
  • 0
Secondary Antibodies

AB191866

VHH Single Domain Anti-Rabbit IgG Fc (HRP)

Recombinant

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - VHH Single Domain Anti-Rabbit IgG Fc (HRP) (AB191866)

  • 5
  • 2
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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"SHMAKWGEGDPRWIVEERADATNVNNWHWTERDASNWSTDKLKTLFLAVQVQNEEGKCEVTEVSKLDGEASINNRKGKLIFFYEWSVKLNWTGTSKSGVQYKGHVEIPNLSDENSVDEVEISVSLAKDEPDTNLVALMKEEGVKLLREAMGIYISTLKTEFTQGMILPTMNGESVDPVGQPALKTEERKAKPAPSKTQARPVGVKIPTCKITLKETFLTSPEELYRVFTTQELVQAFTHAPATLEADRGGKFHMVDGNVSGEFTDLVPEKHIVMKWRFKSWPEGHFATITLTFIDKNGETELCMEGRGIPAPEEERTRQGWQRYYFEGIKQTFGYGARLF","proteinLength":"Full Length","predictedMolecularWeight":"38 kDa","actualMolecularWeight":null,"aminoAcidEnd":338,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"O95433","tags":[{"tag":"His","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

AHA1 also known as activator of heat shock 90kDa protein ATPase homolog 1 is a co-chaperone protein that plays a role in the regulation of HSP90 ATPase activity. This protein has a molecular weight of approximately 38 kDa. AHA1 expression occurs in various tissues with higher amounts seen in metabolically active tissues. It interacts directly with HSP90 enhancing the chaperone's ability to fold client proteins correctly by stimulating its ATPase activity.
Biological function summary

AHA1 modulates the function of the HSP90 chaperone complex. This complex is important for the stabilization and activation of many client proteins such as steroid hormone receptors and kinases. AHA1 binds to the middle domain of HSP90 contributing to conformational changes necessary for efficient ATP hydrolysis. By influencing these molecular processes AHA1 plays a role in maintaining cellular protein homeostasis under stress conditions.

Pathways

The HSP90-AHA1 interaction is significant in the signaling pathway of cellular stress responses and protein folding. AHA1's upregulating effect on HSP90 ATPase activity facilitates the correct folding and function of client proteins involved in the MAPK/ERK and PI3K/AKT pathways. These pathways commonly involve interactions with proteins such as RAF and PI3K which are important in cell proliferation and survival processes.

AHA1 influences the progression of cancer and neurodegenerative diseases. Altered expression or function of AHA1 is linked to the development and progression of cancer as it affects the stability of oncoproteins through its interaction with HSP90. The protein is also connected to neurodegenerative diseases with disruptions in its function or expression impacting the folding and maintenance of neuronal proteins. In these diseases the AHA1-HSP90 interaction remains a critical component of pathogenic pathways affecting disease manifestation and progression.
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Specifications

Form

Liquid

Additional notes

Affinity Purified

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General info

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).

Sequence similarities

Belongs to the AHA1 family.

Post-translational modifications

Phosphorylation at Tyr-223 enhances binding to chaperone HSP90AA1.

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Product protocols

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Target data

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).
See full target information AHSA1
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Product promise

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