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344931 Furin Inhibitor II - Calbiochem

The Furin Inhibitor II controls the biological activity of Furin. This small molecule/inhibitor is primarily used for Protease Inhibitors applications.

Furin Inhibitor II - Calbiochem MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.

Synonyms: Hexa-D-arginine, H-(D)RRRRRR-NH₂

Primary Target: furin
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344931
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Overview

Replacement Information

Key Spec Table

Empirical Formula
C₃₆H₇₅N₂₅O₆

Pricing & Availability

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344931-1MG
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      Description
      OverviewA polyarginine compound that acts as a potent, specific, and competitive inhibitor of furin (Ki = 106 nM). Inhibits Subtilisin-like proprotein convertase 4 (PACE4) and prohormone convertase 1 (PC1) at much higher concentration (Ki = 580 nM and 13 µM, respectively). Has a stimulatory effect on the activity of prohormone convertase 2 (PC2). The D-peptides are suggested to be more resistant to in vivo hydrolysis than L-peptides.
      Catalogue Number344931
      Brand Family Calbiochem®
      SynonymsHexa-D-arginine, H-(D)RRRRRR-NH₂
      References
      ReferencesCameron, A., et al. 2000. J. Biol. Chem. 275, 36741.
      Product Information
      ATP CompetitiveY
      FormWhite solid
      FormulationSupplied as a trifluoroacetate salt.
      Hill FormulaC₃₆H₇₅N₂₅O₆
      Chemical formulaC₃₆H₇₅N₂₅O₆
      Hygroscopic Hygroscopic
      ReversibleN
      Quality LevelMQ100
      Applications
      Biological Information
      Primary Targetfurin
      Primary Target K<sub>i</sub>106 nM against Furin
      Purity≥95% by HPLC
      Physicochemical Information
      Cell permeableN
      Peptide SequenceH-(D)Arg-Arg-Arg-Arg-Arg-Arg-NH₂
      Dimensions
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Storage and Shipping Information
      Ship Code Ambient Temperature Only
      Toxicity Standard Handling
      Storage -20°C
      Hygroscopic Hygroscopic
      Do not freeze Ok to freeze
      Special InstructionsFollowing reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 6 months at -20°C.
      Packaging Information
      Packaged under inert gas Packaged under inert gas
      Transport Information
      Supplemental Information
      Specifications
      Global Trade Item Number
      Catalogue Number GTIN
      344931-1MG 04055977194395

      Documentation

      Furin Inhibitor II - Calbiochem MSDS

      Title

      Safety Data Sheet (SDS) 

      Furin Inhibitor II - Calbiochem Certificates of Analysis

      TitleLot Number
      344931

      References

      Reference overview
      Cameron, A., et al. 2000. J. Biol. Chem. 275, 36741.
      Data Sheet

      Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.

      Revision27-June-2008 RFH
      SynonymsHexa-D-arginine, H-(D)RRRRRR-NH₂
      DescriptionA polyarginine that acts as a potent, specific, and competitive inhibitor of furin (Ki = 106 nM). Inhibits subtilisin-like proprotein convertase 4 (PACE4) and prohormone convertase 1 (PC1) at much higher concentration (Ki = 580 nM and 13 µM, respectively). Does not affect the activity of PC2. The D-peptides are suggested to be more resistant to in vivo hydrolysis than the L-peptides.
      FormWhite solid
      FormulationSupplied as a trifluoroacetate salt.
      Intert gas (Yes/No) Packaged under inert gas
      Chemical formulaC₃₆H₇₅N₂₅O₆
      Peptide SequenceH-(D)Arg-Arg-Arg-Arg-Arg-Arg-NH₂
      Purity≥95% by HPLC
      SolubilityDMSO or H₂O (1 mg/ml)
      Storage -20°C
      Hygroscopic
      Do Not Freeze Ok to freeze
      Special InstructionsFollowing reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 6 months at -20°C.
      Toxicity Standard Handling
      ReferencesCameron, A., et al. 2000. J. Biol. Chem. 275, 36741.