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

Code CSB-YP001483HU
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Source Yeast
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Code CSB-EP001483HU-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP001483HU
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Source Baculovirus
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Code CSB-MP001483HU
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Source Mammalian cell
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Product Details

Purity >85% (SDS-PAGE)
Target Names AHSA1
Uniprot No. O95433
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)
Expression Region 2-338
Target Protein Sequence AKWGEGDPR WIVEERADAT NVNNWHWTER DASNWSTDKL KTLFLAVQVQ NEEGKCEVTE VSKLDGEASI NNRKGKLIFF YEWSVKLNWT GTSKSGVQYK GHVEIPNLSD ENSVDEVEIS VSLAKDEPDT NLVALMKEEG VKLLREAMGI YISTLKTEFT QGMILPTMNG ESVDPVGQPA LKTEERKAKP APSKTQARPV GVKIPTCKIT LKETFLTSPE ELYRVFTTQE LVQAFTHAPA TLEADRGGKF HMVDGNVSGE FTDLVPEKHI VMKWRFKSWP EGHFATITLT FIDKNGETEL CMEGRGIPAP EEERTRQGWQ RYYFEGIKQT FGYGARLF
Protein Length Full Length of Mature Protein
Tag Info The following tags are available.
N-terminal His-tagged
Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form Lyophilized powder
Buffer before Lyophilization 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℃/-80℃. 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.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet 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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