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Your Position: ホーム > Protein > HSP90AA1 > HS1-H513x

Human HSP90AA1 / HSP86 Protein, GST Tag

  • Synonym
    HSP90AA1,HSP90A,HSP 86,HSP86,HSPC1,HSPCA,EL52,HSP89A,HSP90N,HSPCAL1,HSPCAL4,HSPN,Hsp89,Hsp90,LAP2
  • Source
    Human HSP90AA1, GST Tag(HS1-H513x) is expressed from E. coli cells. It contains AA Glu 535 - Asp 732 (Accession # NP_005339).
    Predicted N-terminus: Met
  • Molecular Characterization
    HSP90AA1 Structure

    This protein carries a GST tag at the N-terminus.

    The protein has a calculated MW of 49.3 kDa. The protein migrates as 27 kDa,29 kDa,31-32 kDa and 47-49 kDa under reducing (R) condition (SDS-PAGE).

  • Endotoxin
    Less than 1.0 EU per μg by the LAL method.
  • Purity

    >85% as determined by SDS-PAGE.

  • Formulation

    Lyophilized from 0.22 μm filtered solution in 50 mM HEPES, 150 mM NaCl, pH7.0 with trehalose as protectant.

    Contact us for customized product form or formulation.

  • Reconstitution

    Please see Certificate of Analysis for specific instructions.

    For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

  • Storage

    For long term storage, the product should be stored at lyophilized state at -20°C or lower.

    Please avoid repeated freeze-thaw cycles.

    This product is stable after storage at:

    1. -20°C to -70°C for 12 months in lyophilized state;
    2. -70°C for 3 months under sterile conditions after reconstitution.
SDS-PAGE
HSP90AA1 SDS-PAGE

Human HSP90AA1, GST Tag on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 85%.

  • Background
    Heat shock protein HSP 90-alpha (HSP90AA1 or HSP90A) is also known as Heat shock 86 kDa (HSP 86 or HSP86), Renal carcinoma antigen NY-REN-38, HSPC1, HSPCA, EL52, HSP89A, HSP90N, HSPCAL1, HSPCAL4, HSPN, Hsp89, Hsp90, LAP2, which belongs to the heat shock protein 90 family. HSP90AA1 undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. HSP90AA1 interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function.
  • Clinical and Translational Updates

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