Recombinant Human Activator of 90 kDa heat shock protein ATPase homolog 1(AHSA1)

Code CSB-RP054544h
Size US$1726
Image
  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

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Product Details

Purity Greater than 90% as determined by SDS-PAGE.
Target Names AHSA1
Uniprot No. O95433
Research Area Neuroscience
Alternative Names Activator of 90 kDa heat shock protein ATPase homolog 1; Activator of heat shock 90kDa protein ATPase homolog 1; AHA 1; AHA1; AHSA 1; Ahsa1; AHSA1_HUMAN; C14orf3; HSPC322; p38
Species Homo sapiens (Human)
Source E.coli
Expression Region 1-338aa
Target Protein Sequence MAKWGEGDPRWIVEERADATNVNNWHWTERDASNWSTDKLKTLFLAVQVQNEEGKCEVTEVSKLDGEASINNRKGKLIFFYEWSVKLNWTGTSKSGVQYKGHVEIPNLSDENSVDEVEISVSLAKDEPDTNLVALMKEEGVKLLREAMGIYISTLKTEFTQGMILPTMNGESVDPVGQPALKTEERKAKPAPSKTQARPVGVKIPTCKITLKETFLTSPEELYRVFTTQELVQAFTHAPATLEADRGGKFHMVDGNVSGEFTDLVPEKHIVMKWRFKSWPEGHFATITLTFIDKNGETELCMEGRGIPAPEEERTRQGWQRYYFEGIKQTFGYGARLF
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight 65.3kDa
Protein Length Full Length
Tag Info N-terminal GST-tagged
Form Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting
and FAQs
Protein FAQs
Storage Condition Store at -20°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA Please contact us to get it.

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Target Data

Function 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
Gene References into Functions
  1. Aha1 colocalized with tau pathology in brain tissue, and this association positively correlated with Alzheimer disease progression. PMID: 28827321
  2. These results suggest that differences in the middle domain of Hsp90alpha and Hsp90beta may be responsible for the isoform-specific interactions with selected proteins. PMID: 25486457
  3. Aha1 may promote disposal of folding defective proteins by the cellular protein quality control. PMID: 25378400
  4. a monoallelic mutation of p53 was sufficient to activate the Aha1/Hsp90 ATPase axis leading to stimulation of Wnt signaling and increased expression of Wnt target genes. PMID: 24451373
  5. Modulation of Hsp90 activity by AHA1 regulates VEGF signaling to eNOS and angiogenesis. PMID: 22859491
  6. The interaction of Aha1 with Hsp90 and its co-chaperones in rabbit reticulocyte lysate (RRL) and in HeLa cell extracts, was characterized. PMID: 22504172
  7. Hsp90 phosphorylation on tyrosine313 promotes recruitment of AHA1, which stimulates Hsp90 ATPase activity, furthering the chaperoning process. PMID: 22727666
  8. Data propose a model for Aha1 in the Hsp90 ATPase cycle where Aha1 regulates dwell time of Hsp90, and suggest Aha1 activity integrates chaperone function with client folding energetics by modulating ATPase sensitive dimer structural transitions. PMID: 20089831
  9. stimulates the inherent ATPase activity of Hsp90 PMID: 12504007
  10. Hsp90 cochaperones modulate Hsp90-dependent stability of CFTR protein folding in the endoplasmic reticulum PMID: 17110338

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Subcellular Location Cytoplasm, cytosol, Endoplasmic reticulum
Protein Families AHA1 family
Tissue Specificity Expressed in numerous tissues, including brain, heart, skeletal muscle and kidney and, at lower levels, liver and placenta.
Database Links

HGNC: 1189

OMIM: 608466

KEGG: hsa:10598

STRING: 9606.ENSP00000216479

UniGene: Hs.204041

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