Recombinant Saccharomyces cerevisiae Hsp90 co-chaperone AHA1 (AHA1)

Code CSB-YP618602SVG
MSDS
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Source Yeast
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Code CSB-EP618602SVG
MSDS
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Source E.coli
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Code CSB-EP618602SVG-B
MSDS
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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-BP618602SVG
MSDS
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Source Baculovirus
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Code CSB-MP618602SVG
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
AHA1
Uniprot No.
Alternative Names
AHA1; YDR214W; YD8142.16; YD8142B.06Hsp90 co-chaperone AHA1; Activator of Hsp90 ATPase protein 1
Species
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Expression Region
1-350
Target Protein Sequence
MVVNNPNNWH WVDKNCIGWA KEYFKQKLVG VEAGSVKDKK YAKIKSVSSI EGDCEVNQRK GKVISLFDLK ITVLIEGHVD SKDGSALPFE GSINVPEVAF DSEASSYQFD ISIFKETSEL SEAKPLIRSE LLPKLRQIFQ QFGKDLLATH GNDIQVPESQ VKSNYTRGNQ KSSFTEIKDS ASKPKKNALP SSTSTSAPVS STNKVPQNGS GNSTSIYLEP TFNVPSSELY ETFLDKQRIL AWTRSAQFFN SGPKLETKEK FELFGGNVIS ELVSCEKDKK LVFHWKLKDW SAPFNSTIEM TFHESQEFHE TKLQVKWTGI PVGEEDRVRA NFEEYYVRSI KLTFGFGAVL
Protein Length
full length protein
Tag Info
Tag type will be determined during the manufacturing process.
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
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 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
Storage Condition
Store at -20°C/-80°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.

Customer Reviews and Q&A

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Target Background

Function
Co-chaperone that binds to the molecular chaperone HSP82 and stimulates its ATPase activity. Binding to HSP82 promotes a conformational switch in the catalytic loop of HSP82, facilitating the interaction of the catalytic 'Arg-380' with ATP in the N-terminal nucleotide-binding domain. Although not essential, it confers thermotolerance when intracellular levels of HSP82 are limiting.
Gene References into Functions
  1. A chemical compound inhibiting the Aha1-Hsp90 chaperone complex PMID: 28851842
  2. The work here suggests that both Hch1p and Aha1p regulate Hsp90 function through interaction with the catalytic loop but do so in different ways. PMID: 24726918
  3. Aha1 facilitates the progression of the Hsp90 co-chaperone cycle. PMID: 23396352
  4. an interaction between Aha1 and residues near the C terminus of Mal63 PMID: 20177068
  5. For maximum activation of Hsp90, the two domains of Aha1 bind to sites in the middle and N-terminal domains of Hsp90 in a sequential manner. PMID: 20159554
  6. binding of N-Aha1 promotes a conformational switch in the middle-segment catalytic loop (370-390) of Hsp90 that releases the catalytic Arg 380 PMID: 15039704

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Subcellular Location
Cytoplasm.
Protein Families
AHA1 family
Database Links

KEGG: sce:YDR214W

STRING: 4932.YDR214W

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