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ProductsBack/Antipain . dihydrochloride [37682-72-7]
Chemical Structure
Chemical Structure
Chemical Structure

Antipain . dihydrochloride [37682-72-7]

Research Use Only
AG-CP3-7002
AdipoGen Life Sciences
Estimated Purity>97% (HPLC)
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Product group Chemicals
Molecular Weight604.7 . 72.9
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Overview

  • Supplier
    AdipoGen Life Sciences
  • Product Name
    Antipain . dihydrochloride [37682-72-7]
  • Delivery Days Customer
    10
  • Certification
    Research Use Only
  • Estimated Purity
    >97% (HPLC)
  • Hazard Information
    Non-hazardous
  • Molecular Formula
    C27H44N10O6 . 2HCl
  • Molecular Weight
    604.7 . 72.9
  • Scientific Description
    Chemical. CAS: 37682-72-7. Formula: C27H44N10O6 . 2HCl. MW: 604.7 . 72.9. Synthetic. Potent reversible inhibitor of serine/cysteine proteases and some trypsin-like proteases. Inhibits papain, trypsin and trypsin-like serine proteases as well as cathepsin A, B and D. Similar activity spectrum comparable to leupeptin (AG-CP3-7000). Acts by forming a hemiacetal adduct between its aldehyde group and the active serine of the proteinase. Inhibits transformation of NIH3T3 cells after transfection with an activated H-ras oncogene. Used to evaluate the role of proteases in the process of malignant cell transformations. Shows antibacterial and antiparasitic activity. - Potent reversible inhibitor of serine/cysteine proteases and some trypsin-like proteases. Inhibits papain, trypsin and trypsin-like serine proteases as well as cathepsin A, B and D. Similar activity spectrum comparable to leupeptin (AG-CP3-7000). Acts by forming a hemiacetal adduct between its aldehyde group and the active serine of the proteinase. Inhibits transformation of NIH3T3 cells after transfection with an activated H-ras oncogene. Used to evaluate the role of proteases in the process of malignant cell transformations. Shows antibacterial and antiparasitic activity.
  • SMILES
    [Cl-].[Cl-].[H]C(=O)C(CCCNC(N)=[NH2+])NC(=O)[C@@H](NC(=O)[C@H](CCCNC(N)=[NH2+])NC(=O)NC(CC1=CC=CC=C1)C(O)=O)C(C)C
  • Storage Instruction
    2°C to 8°C,-20°C
  • UNSPSC
    12352200

References

  • Antipain, a new protease inhibitor isolated from actinomycetes: H. Suda, et al.; J. Antibiot. 25, 263 (1972)
  • Structures and activities of protease inhibitors of microbial origin: H. Umezawa; Methods Enzymol. 45, 678 (1976)
  • Inhibition of proteolytic activity of calcium activated neutral protease by leupeptin and antipain: T. Toyo-Oka, et al.; BBRC 82, 484 (1978)
  • Effects of antipain (a protease inhibitor) on respiration, viability, and excision of pyrimidine dimers in UV-irradiated Escherichia coli cells: P.A. Swenson & R.L. Schenley; J. Bacteriol. 135, 1167 (1978)
  • Effect of Ca2+ on the inhibition of calcium-activated neutral protease by leupeptin, antipain and epoxysuccinate derivatives: K. Suzuki, et al.; FEBS Lett. 136, 119 (1981)
  • Inhibition of Leishmania amastigote growth by antipain and leupeptin: G.H. Coombs & J. Baxter; Ann. Trop. Med. Parasitol. 78, 21 (1984)
  • Antipain or leupeptin in combination with aspirin or indomethacin synergistically inhibit human platelet activation by thrombin and trypsin: M. Ruggiero & E.G. Lapetina; Adv. Prostaglandin Thromboxane Leukot. Res. 17A, 563 (1987)
  • Inhibition of H-ras oncogene transformation of NIH3T3 cells by protease inhibitors: S.J. Garte, et al.; Cancer Res. 47, 3159 (1987)
  • Reversible conversion of tyrosine hydroxylase to an inactive form by antipain: S. Okuno & H. Fujisawa; BBRC 146, 1375 (1987)
  • Antipain-induced suppression of oncogene expression in H-ras-transformed NIH3T3 cells: L.R. Cox, et al.; Cancer Res. 51, 4810 (1991)