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Chemical Structure
Chemical Structure
Chemical Structure

H-8 . dihydrochloride [113276-94-1]

Research Use Only
AG-CR1-0001
AdipoGen Life Sciences
Estimated Purity>98% (NMR)
Product group Chemicals
Molecular Weight265.3 . 72.9
Price on request
Packing Size
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Overview

  • Supplier
    AdipoGen Life Sciences
  • Product Name
    H-8 . dihydrochloride [113276-94-1]
  • Delivery Days Customer
    10
  • Certification
    Research Use Only
  • Estimated Purity
    >98% (NMR)
  • Hazard Information
    Non-hazardous
  • Molecular Formula
    C12H15N3O2S . 2HCl
  • Molecular Weight
    265.3 . 72.9
  • Scientific Description
    Chemical. CAS: 113276-94-1. Formula: C12H15N3O2S . 2HCl. MW: 265.3 . 72.9. Potent cAMP- and cGMP-dependent protein kinase (PKA and PKG) inhibitor. Myosin light chain kinase (MLCK) inhibitor. Tool to study protein crystal structure-inhibitor interactions. - Potent cAMP- and cGMP-dependent protein kinase (PKA and PKG) inhibitor [1, 2, 4]. Myosin light chain kinase (MLCK) inhibitor [3]. Tool to study protein crystal structure-inhibitor interactions [5].
  • SMILES
    [Cl-].[Cl-].C[NH2+]CC[NH2+]S(=O)(=O)C1=CC=CC2=CN=CC=C12
  • Storage Instruction
    2°C to 8°C
  • UNSPSC
    12352200

References

  • Isoquinolinesulfonamides, novel and potent inhibitors of cyclic nucleotide dependent protein kinase and protein kinase C: H. Hidaka, et al.; Biochemistry 23, 5036 (1984)
  • Naphthalenesulfonamides as calmodulin antagonists and protein kinase inhibitors: M. Inagaki, et al.; Mol. Pharmacol. 29, 577 (1986)
  • Specific binding of a novel compound, N-[2-(methylamino)ethyl]-5-isoquinolinesulfonamide (H-8) to the active site of cAMP-dependent protein kinase: M. Hagiwara, et al.; Mol. Pharmacol. 31, 523 (1987)
  • Selective modulation of calcium-dependent myosin phosphorylation by novel protein kinase inhibitors, isoquinolinesulfonamide derivatives: M. Hagiwara, et al.; Mol. Pharmacol. 32, 7 (1987)
  • Crystal structures of catalytic subunit of cAMP-dependent protein kinase in complex with isoquinolinesulfonyl protein kinase inhibitors H7, H8, and H89. Structural implications for selectivity: R.A. Engh, et al.; J. Biol. Chem. 271, 26157 (1996)