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475941 Myokinase, Yeast

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

Synonyms: Adenylate Kinase, ATP:AMP Phosphotransferase

475941
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Overview

Replacement Information

Products

Catalogue NumberPackaging Qty/Pack
475941-1KUCN Plastic ampoule 1 ku
Description
OverviewNative, yeast myokinase. Myokinase reversibly transfers phosphate from ATP to AMP, thus forming two molecules of ADP. The enzyme is specific for adenine nucleotides and catalyzes the reaction only in the presence of a divalent metal ion (e.g. Mg2+, Ca2+, Co2+, Mn2+, or Ni2+).
Note: 1 KU = 1000 units.
Catalogue Number475941
Brand Family Calbiochem®
SynonymsAdenylate Kinase, ATP:AMP Phosphotransferase
References
ReferencesMakarchikov, A.F., et al. 2002. Biochem. Biophys. Acta. 1592, 117.
Schricker, R., et al. 2002. J. Biol. Chem. 277, 28757.
Magdolen, V., et al. 1987. Curr. Genet. 12, 405.
Tomasselli, A.G., et al. 1986. Eur. J. Biochem. 155, 111.
Ito, Y., et al. 1980. Eur. J. Biochem. 105, 85.
Product Information
CAS number9013-02-9
Activity≥10 units/mg solid
Unit of DefinitionOne unit is defined as the amount of enzyme that will convert 1.0 µmol ATP and 1.0 µmol AMP to 2 µmol ADP per min at 25°C, pH 7.5. Note: 1 KU = 1000 units.
EC number2.7.4.3
FormLyophilized
FormulationLyophilized from potassium phosphate buffer.
Hygroscopic Hygroscopic
PI5.7
Quality LevelMQ100
Applications
Biological Information
Specific Activity≥200 units/mg
Physicochemical Information
ContaminantsATPase: ≤0.01%; Phosphoglycerate kinase: ≤0.1%
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Storage and Shipping Information
Ship Code Shipped with Blue Ice or with Dry Ice
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
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
Catalogue Number GTIN
475941-1KUCN 04055977184259

Documentation

Myokinase, Yeast SDS

Title

Safety Data Sheet (SDS) 

Myokinase, Yeast Certificates of Analysis

TitleLot Number
475941

References

Reference overview
Makarchikov, A.F., et al. 2002. Biochem. Biophys. Acta. 1592, 117.
Schricker, R., et al. 2002. J. Biol. Chem. 277, 28757.
Magdolen, V., et al. 1987. Curr. Genet. 12, 405.
Tomasselli, A.G., et al. 1986. Eur. J. Biochem. 155, 111.
Ito, Y., et al. 1980. Eur. J. Biochem. 105, 85.
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.

Revision17-September-2007 RFH
SynonymsAdenylate Kinase, ATP:AMP Phosphotransferase
DescriptionNative, yeast myokinase. Myokinase reversibly transfers phosphate from ATP to AMP, thus forming two molecules of ADP. The enzyme is specific for adenine nucleotides and catalyzes the reaction only in the presence of a divalent metal ion (e.g. Mg2+, Ca2+, Co2+, Mn2+, or Ni2+).
FormLyophilized
FormulationLyophilized from potassium phosphate buffer.
CAS number9013-02-9
EC number2.7.4.3
ContaminantsATPase: ≤0.01%; Phosphoglycerate kinase: ≤0.1%
Specific activity≥200 units/mg
Activity≥10 units/mg solid
Unit definitionOne unit is defined as the amount of enzyme that will convert 1.0 µmol ATP and 1.0 µmol AMP to 2 µmol ADP per min at 25°C, pH 7.5. Note: 1 KU = 1000 units.
SolubilityH₂O (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
ReferencesMakarchikov, A.F., et al. 2002. Biochem. Biophys. Acta. 1592, 117.
Schricker, R., et al. 2002. J. Biol. Chem. 277, 28757.
Magdolen, V., et al. 1987. Curr. Genet. 12, 405.
Tomasselli, A.G., et al. 1986. Eur. J. Biochem. 155, 111.
Ito, Y., et al. 1980. Eur. J. Biochem. 105, 85.