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482732 Nitric Oxide Synthase, Constitutive, Bovine Endothelial, Recombinant, S. frugiperda

MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.

Synonyms: eNOS, NOS III, Endothelial Nitric Oxide Synthase

482732
  
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Overview

Replacement Information
Description
Overview

This product has been discontinued.





Recombinant bovine endothelial NOS expressed in S. frugiperda insect cells using a baculovirus expression system. eNOS undergoes several post-translational modifications, including myristoylation and palmitoylation, which causes the enzyme to become membrane-associated.
Catalogue Number482732
Brand Family Calbiochem®
SynonymseNOS, NOS III, Endothelial Nitric Oxide Synthase
References
ReferencesBusconi, L., and Michel, T. 1995. Mol. Pharmacol. 47, 655.
Hevel, J.M., and Marletta, M.A. 1994. Methods Enzymol. 233, 250.
Knowles, R.G., and Moncada, S. 1994. Biochem. J. 298, 249.
Product Information
Unit of DefinitionOne unit is defined as the amount of enzyme that will produce 1 nmol of nitric oxide per min at 37°C in a solution containing 50 mM HEPES, 5 µM oxyhemoglobin, 1 mM CaCl₂, 20 µl calmodulin, 0.1 mM NADPH, 50 µM arginine, 12 µM tetrahydrobiopterin, and 170 µM DTT, pH 7.5.
FormLiquid
FormulationIn 50 mM HEPES, 5 mM CHAPS, 100 µM DTT, 10% glycerol, pH 7.4.
Applications
Biological Information
Specific Activity~2 units/mg protein
Concentration Label Please refer to vial label for lot-specific concentration
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Storage and Shipping Information
Ship Code Dry Ice Only
Toxicity Standard Handling
Storage ≤ -70°C
Avoid freeze/thaw Avoid freeze/thaw
Do not freeze Ok to freeze
Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C).
Packaging Information
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
Catalogue Number GTIN
482732 0

Documentation

Nitric Oxide Synthase, Constitutive, Bovine Endothelial, Recombinant, S. frugiperda Certificates of Analysis

TitleLot Number
482732

References

Reference overview
Busconi, L., and Michel, T. 1995. Mol. Pharmacol. 47, 655.
Hevel, J.M., and Marletta, M.A. 1994. Methods Enzymol. 233, 250.
Knowles, R.G., and Moncada, S. 1994. Biochem. J. 298, 249.
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.

Revision13-August-2008 RFH
SynonymseNOS, NOS III, Endothelial Nitric Oxide Synthase
DescriptionRecombinant bovine endothelial NOS expressed in S. frugiperda insect cells using a baculovirus expression system. eNOS undergoes several post-translational modifications, including myristoylation and palmitoylation, which causes it to become associated with membrane. Useful for studies involving NOS regulation, inhibitor screening, and kinetic analysis.

Note: eNOS is an unstable enzyme. Keep the stock vial of the enzyme on ice at all times during the experiment. The enzyme should be added to the incubation medium just prior to the initiation of the experiment.
FormLiquid
FormulationIn 50 mM HEPES, 5 mM CHAPS, 100 µM DTT, 10% glycerol, pH 7.4.
Concentration Label Please refer to vial label for lot-specific concentration
Specific activity~2 units/mg protein
Unit definitionOne unit is defined as the amount of enzyme that will produce 1 nmol of nitric oxide per min at 37°C in a solution containing 50 mM HEPES, 5 µM oxyhemoglobin, 1 mM CaCl₂, 20 µl calmodulin, 0.1 mM NADPH, 50 µM arginine, 12 µM tetrahydrobiopterin, and 170 µM DTT, pH 7.5.
Storage Avoid freeze/thaw
≤ -70°C
Do Not Freeze Ok to freeze
Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C).
Toxicity Standard Handling
ReferencesBusconi, L., and Michel, T. 1995. Mol. Pharmacol. 47, 655.
Hevel, J.M., and Marletta, M.A. 1994. Methods Enzymol. 233, 250.
Knowles, R.G., and Moncada, S. 1994. Biochem. J. 298, 249.