Overview

  • Product name
    Recombinant S. cerevisiae HSP82 protein
  • Protein length
    Full length protein

Description

  • Nature
    Recombinant
  • Source
    Escherichia coli
  • Amino Acid Sequence
    • Accession
    • Species
      Saccharomyces cerevisiae
    • Sequence
      MASETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYKSL SDPKQLETEPDLFIRITPKPEQKVLEIRDSGIGMTKAELINNLGTIAKSG TKAFMEALSAGADVSMIGQFGVGFYSLFLVADRVQVISKSNDDEQYIWES NAGGSFTVTLDEVNERIGRGTILRLFLKDDQLEYLEEKRIKEVIKRHSEF VAYPIQLVVTKEVEKEVPIPEEEKKDEEKKDEEKKDEDDKKPKLEEVDEE EEKKPKTKKVKEEVQEIEELNKTKPLWTRNPSDITQEEYNAFYKSISNDW EDPLYVKHFSVEGQLEFRAILFIPKRAPFDLFESKKKKNNIKLYVRRVFI TDEAEDLIPEWLSFVKGVVDSEDLPLNLSREMLQQNKIMKVIRKNIVKKL IEAFNEIAEDSEQFEKFYSAFSKNIKLGVHEDTQNRAALAKLLRYNSTKS VDELTSLTDYVTRMPEHQKNIYYITGESLKAVEKSPFLDALKAKNFEVLF LTDPIDEYAFTQLKEFEGKTLVDITKDFELEETDEEKAEREKEIKEYEPL TKALKEILGDQVEKVVVSYKLLDAPAAIRTGQFGWSANMERIMKAQALRD SSMSSYMSSKKTFEISPKSPIIKELKKRVDEGGAQDKTVKDLTKLLYETA LLTSGFSLDEPTSFASRINRLISLGLNIDEDEETETAPEASTAAPVEEVP ADTEMEEVD
    • Molecular weight
      81 kDa
    • Amino acids
      1 to 709
    • Tags
      His tag N-Terminus

Specifications

Our Abpromise guarantee covers the use of ab157058 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications

    Western blot

  • Purity
    >= 99 % .

  • Form
    Liquid
  • Additional notes
    For maximum product recovery after thawing, centrifuge the vial before opening the cap.
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.

    pH: 7.50
    Constituent: 1.12% Potassium chloride

General Info

  • Alternative names
    • 82 kDa heat shock protein
    • ATP-dependent molecular chaperone HSP82
    • Heat shock protein Hsp90 heat-inducible isoform
    • HSP90
    • YPL240C
    see all
  • Relevance
    Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. The nucleotide-free form of the dimer is found in an open conformation in which the N-termini are not dimerized and the complex is ready for client protein binding. Binding of ATP induces large conformational changes, resulting in the formation of a ring-like closed structure in which the N-terminal domains associate intramolecularly with the middle domain and also dimerize with each other, stimulating their intrinsic ATPase activity and acting as a clamp on the substrate. Finally, ATP hydrolysis results in the release of the substrate. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Required for growth at high temperatures.
  • Cellular localization
    Cytoplasmic

References

ab157058 has not yet been referenced specifically in any publications.

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Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"

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