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361523 GSK-3α, GST-Fusion, Human, Recombinant, S. frugiperda

361523
  
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Přehled

Replacement Information
Description
Overview

This product has been discontinued.





Full-length, recombinant, human GSK3α fused at the N-terninus to GST and expressed in S. frugiperda insect cells using a baculovirus expression system. GSK3α is unique in its preference for a priming phosphate at n+4 (where n is the site of phosphorylation by GSK3α) in order to phosphorylate many of its substrates. This motif is found in several well-established substrates of GSK3α, such as glycogen synthase, the epsilon subunit of eIF2B, and ATP citrate-lyase. The active kinase is useful in the study of GSK3α regulation and for inhibitor screening.
Catalogue Number361523
Brand Family Calbiochem®
SynonymsGlycogen Synthase Kinase 3α
References
ReferencesMeijer, L., et al. 2004. Trends Pharmacol Sci. 25, 471.
Patel, S., et al. 2004. Biochem Soc. Trans. 32, 803.
Product Information
Unit of DefinitionOne unit is defined as the amount of enzyme that will phosphorylate 1 nmol glycogen synthase peptide substrate (YRRAAVPPSPSLSRHSSPHQSEDEEE) per min at 30°C, pH 7.4.
FormLiquid
FormulationIn 100 mM NaCl, 25 mM Tris-HCl, 10 mM reduced glutathione, 3 mM DTT, 50% glycerol, 0.05% Tween®-20 detergent, pH 8.0.
Applications
Biological Information
Purity≥80% by SDS-PAGE
Specific Activity≥700 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
S PhraseS: 26

In case of contact with eyes, rinse immediately with plenty of water and seek medical advice.
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 intitial thaw, aliquot and freeze (-70°C).
Packaging Information
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
Katalogové číslo GTIN
361523 0

Documentation

GSK-3α, GST-Fusion, Human, Recombinant, S. frugiperda Certificates of Analysis

TitleLot Number
361523

References

Přehled odkazů
Meijer, L., et al. 2004. Trends Pharmacol Sci. 25, 471.
Patel, S., et al. 2004. Biochem Soc. Trans. 32, 803.
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 JSW
SynonymsGlycogen Synthase Kinase 3α
DescriptionFull-length, recombinant, human GSK3α fused at the N-terninus to GST and expressed in S. frugiperda insect cells using a baculovirus expression system. GSK3α is unique in its preference for a priming phosphate at n+4 (where n is the site of phosphorylation by GSK3α) in order to phosphorylate many of its substrates. This motif is found in several well-established substrates of GSK3α, such as glycogen synthase, the epsilon subunit of eIF2B, and ATP citrate-lyase. The active kinase is useful in the study of GSK3α regulation and for inhibitor screening.
FormLiquid
FormulationIn 100 mM NaCl, 25 mM Tris-HCl, 10 mM reduced glutathione, 3 mM DTT, 50% glycerol, 0.05% Tween®-20 detergent, pH 8.0.
Concentration Label Please refer to vial label for lot-specific concentration
Recommended reaction conditions
50 mM HEPES, 3 mM MgCl2, 3 mM MnCl2, 1 mM DTT, 100 µM ATP, 20 µM peptide substrate (YRRAAVPPSPSLSRHSSPHQSEDEEE), 3 µM sodium orthovanadate, and 100 µg enzyme.
Purity≥80% by SDS-PAGE
Specific activity≥700 units/mg protein
Unit definitionOne unit is defined as the amount of enzyme that will phosphorylate 1 nmol glycogen synthase peptide substrate (YRRAAVPPSPSLSRHSSPHQSEDEEE) per min at 30°C, pH 7.4.
Storage Avoid freeze/thaw
≤ -70°C
Do Not Freeze Ok to freeze
Special InstructionsFollowing intitial thaw, aliquot and freeze (-70°C).
Toxicity Standard Handling
ReferencesMeijer, L., et al. 2004. Trends Pharmacol Sci. 25, 471.
Patel, S., et al. 2004. Biochem Soc. Trans. 32, 803.