AMP-PCP

CAS No. 3469-78-1

AMP-PCP( —— )

Catalog No. M21917 CAS No. 3469-78-1

AMP-PCP is an ATP analogue and can bind to Hsp90 N-terminal domain with a Kd value of 3.8 μM. AMP-PCP binding favors the formation of the active homodimer of Hsp90.

Purity : >98% (HPLC)

COA Datasheet HNMR HPLC MSDS Handing Instructions
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Biological Information

  • Product Name
    AMP-PCP
  • Note
    Research use only, not for human use.
  • Brief Description
    AMP-PCP is an ATP analogue and can bind to Hsp90 N-terminal domain with a Kd value of 3.8 μM. AMP-PCP binding favors the formation of the active homodimer of Hsp90.
  • Description
    AMP-PCP is an ATP analogue and can bind to Hsp90 N-terminal domain with a Kd value of 3.8 μM. AMP-PCP binding favors the formation of the active homodimer of Hsp90.AMP-PCP binding favors the formation of the active homodimer of Hsp90 by enhancing the slow-motion featured conformational exchanges of those residues (A117-A141) within the lid segment (A111-G135) and around region. In total, 170 non-proline residues are identified for the triple-labeled Hsp90 bound with AMP-PCP.
  • In Vitro
    AMP-PCP binding favors the formation of the active homodimer of Hsp90 by enhancing the slow-motion featured conformational exchanges of those residues (A117-A141) within the lid segment (A111-G135) and around region. In total, 170 non-proline residues are identified for the triple-labeled Hsp90 bound with AMP-PCP.
  • In Vivo
    ——
  • Synonyms
    ——
  • Pathway
    Cytoskeleton/Cell Adhesion Molecules
  • Target
    HSP
  • Recptor
    HSP90
  • Research Area
    ——
  • Indication
    ——

Chemical Information

  • CAS Number
    3469-78-1
  • Formula Weight
    505.21
  • Molecular Formula
    C??H??N?O??P?
  • Purity
    >98% (HPLC)
  • Solubility
    ——
  • SMILES
    O[C@H]1[C@@H](O[C@H](COP(OP(CP(O)(O)=O)(O)=O)(O)=O)[C@H]1O)N2C3=C(C(N)=NC=N3)N=C2
  • Chemical Name
    ——

Shipping & Storage Information

  • Storage
    (-20℃)
  • Shipping
    With Ice Pack
  • Stability
    ≥ 2 years

Reference

1. Zhang H, et al. A dynamic view of ATP-coupled functioning cycle of Hsp90 N-terminal domain. Sci Rep. 2015 Apr 13;5:9542.
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