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218701 Casein Kinase II, Human, Recombinant, E. coli

218701
Purchase on Sigma-Aldrich

Overview

Replacement Information

Products

Catalogue NumberPackaging Qty/Pack
218701-10KU Plastic ampoule 10 ku
Description
OverviewRecombinant, human casein kinase II expressed in E. coli. A cyclic nucleotide-independent serine/threonine protein kinase composed of catalytic α-subunits (M.W. 44 kDa) and regulatory β-subunits (M.W. 26 kDa) in an α2β2-tetramer. This material corresponds to one of several forms of native CKII. Suitable for in vitro phosphorylation of proteins and peptides, phosphopeptide synthesis, characterization of phosphorylating sites, screening of activators and inhibitors, and mechanistic studies.
Note: 1 KU = 1000 units.
Catalogue Number218701
Brand Family Calbiochem®
SynonymsrhCKII
References
ReferencesYamaguchi, Y., et al. 1998. Nucleic Acids Res. 26, 3854.
Chester, N., and Marshak, D.R. 1993. Anal. Biochem. 209, 284.
Russo, G.L., et al. 1992. J. Biol. Chem. 267, 20317.
Product Information
Activity≥500,000 units/ml
Unit of DefinitionOne unit is defined as the amount of enzyme that will catalyze the transfer of 1.0 pmol of phosphate to RRRADDSDDDDD per min at 30°C, pH 7.5, in a total volume of 25 µl.
FormLiquid
FormulationIn 350 mM NaCl, 20 mM Tris-HCl, 2 mM DTT, 1 mM EDTA, 0.1% TRITON® X-100 Detergent, pH 7.5.
Quality LevelMQ100
Applications
Biological Information
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

Documentation

Casein Kinase II, Human, Recombinant, E. coli SDS

Title

Safety Data Sheet (SDS) 

Casein Kinase II, Human, Recombinant, E. coli Certificates of Analysis

TitleLot Number
218701

References

Reference overview
Yamaguchi, Y., et al. 1998. Nucleic Acids Res. 26, 3854.
Chester, N., and Marshak, D.R. 1993. Anal. Biochem. 209, 284.
Russo, G.L., et al. 1992. J. Biol. Chem. 267, 20317.
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.

Revision18-November-2008 JSW
SynonymsrhCKII
DescriptionRecombinant, human casein kinase II expressed in E. coli. A cyclic nucleotide-independent serine/threonine protein kinase composed of catalytic α-subunits (M.W. 44 kDa) and regulatory β-subunits (M.W. 26 kDa) in an α2β2- tetramer. This material is one of several forms of native CK-II. Suitable for in vitro phosphorylation of proteins and peptides, phosphopeptide synthesis, characterization of phosphorylating sites, screening of activators and inhibitors, and mechanistic studies. The following substrates have been characterized by CK-II both in vitro and in vivo: nucleolin, RNA polymerase, p53, and SV 40 large T antigen.
FormLiquid
FormulationIn 350 mM NaCl, 20 mM Tris-HCl, 2 mM DTT, 1 mM EDTA, 0.1% TRITON® X-100 Detergent, pH 7.5.
Recommended reaction conditions20 mM Tris-HCl, pH 7.5, 50 mM KCl, 10 mM MgCl2, and 200 μM ATP (200 μCi/μmol). GTP can be used as a phosphoryl donor in place of ATP. Incubate at 30°C. Note: optimal incubation times and enzyme concentrations must be determined empirically for each substrate.
Activity≥500,000 units/ml
Unit definitionOne unit is defined as the amount of enzyme that will catalyze the transfer of 1.0 pmol of phosphate to RRRADDSDDDDD per min at 30°C, pH 7.5, in a total volume of 25 µl.
Storage ≤ -70°C
Avoid freeze/thaw
Do Not Freeze Ok to freeze
Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C).
Toxicity Standard Handling
ReferencesYamaguchi, Y., et al. 1998. Nucleic Acids Res. 26, 3854.
Chester, N., and Marshak, D.R. 1993. Anal. Biochem. 209, 284.
Russo, G.L., et al. 1992. J. Biol. Chem. 267, 20317.