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508512 SNX-482 - CAS 203460-30-4 - Calbiochem

A peptidyl toxin from venom of African tarantula, Hysterocrates gigas that acts as a high affinity, reversible blocker of Cav2.3 (α1E, R-type) channels (IC₅₀ = 15-30 nM).

SNX-482 - CAS 203460-30-4 - Calbiochem MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.
Primary Target: Cav2.3 channels
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508512
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Overview

Replacement Information

Key Spec Table

CAS #Empirical Formula
203460-30-4C₁₉₂H₂₇₄N₅₂O₆₀S₇

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      Description
      OverviewA peptidyl toxin present in the venom of African tarantula, Hysterocrates gigas that acts as a high affinity, reversible blocker of Cav2.3 (α1E, R-type) channels (IC50 = 15-30 nM). The inhibition appears to be voltage-dependent. At lower concentrations it is also shown to block native R-type Ca2+ current in rat neurohypophyseal nerve terminals, however, these effects are not observed at higher concentrations. Does not affect Na+ or K+ currents in several cultured cell types (~ 500 nM).
      Catalogue Number508512
      Brand Family Calbiochem®
      References
      ReferencesAbitbol, K. et al. 2012. J. Physiol. 590, 2977.
      Newcomb, R., et al., 1998. Biochemistry. 37, 15353.
      Product Information
      CAS number203460-30-4
      FormWhite solid
      Hill FormulaC₁₉₂H₂₇₄N₅₂O₆₀S₇
      Chemical formulaC₁₉₂H₂₇₄N₅₂O₆₀S₇
      Quality LevelMQ100
      Applications
      Biological Information
      Primary TargetCav2.3 channels
      Primary Target IC<sub>50</sub>15-30 nM
      Purity≥98% by HPLC
      Physicochemical Information
      Peptide SequenceGVDKAGCRYMFGGCSVNDDCCPRLGCHSLF→SYCAWDLTFSD (difulfid bond: 7-21, 14-26, 20-33)
      Dimensions
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Storage and Shipping Information
      Ship Code Shipped at Ambient Temperature or with Blue Ice or with Dry Ice
      Toxicity Standard Handling
      Storage -20°C
      Protect from Light Protect from light
      Do not freeze Ok to freeze
      Special InstructionsFollowing reconstitution, aliquot and freeze(-20°C). Stock solutions are stable for up to 3 months at -20°C.
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications
      Global Trade Item Number
      Catalogue Number GTIN
      5.08512.0001 04055977262049

      Documentation

      SNX-482 - CAS 203460-30-4 - Calbiochem SDS

      Title

      Safety Data Sheet (SDS) 

      References

      Reference overview
      Abitbol, K. et al. 2012. J. Physiol. 590, 2977.
      Newcomb, R., et al., 1998. Biochemistry. 37, 15353.
      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.

      Revision31-January-2014 JSW
      DescriptionA peptidyl toxin present in the venom of African tarantula, Hysterocrates gigas that acts as a high affinity, reversible blocker of Cav2.3 (α1E, R-type) channels (IC50 = 15-30 nM). The inhibition appears to be voltage-dependent. At lower concentrations it is also shown to block native R-type Ca2+ current in rat neurohypophyseal nerve terminals, however, these effects are not observed at higher concentrations. Does not affect Na+ or K+ currents in several cultured cell types (~ 500 nM).
      FormWhite solid
      CAS number203460-30-4
      Chemical formulaC₁₉₂H₂₇₄N₅₂O₆₀S₇
      Peptide SequenceGVDKAGCRYMFGGCSVNDDCCPRLGCHSLF→SYCAWDLTFSD (difulfid bond: 7-21, 14-26, 20-33)
      Purity≥98% by HPLC
      Storage Protect from light
      -20°C
      Do Not Freeze Ok to freeze
      Special InstructionsFollowing reconstitution, aliquot and freeze(-20°C). Stock solutions are stable for up to 3 months at -20°C.
      Toxicity Standard Handling
      ReferencesAbitbol, K. et al. 2012. J. Physiol. 590, 2977.
      Newcomb, R., et al., 1998. Biochemistry. 37, 15353.