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Casein Kinase 2 alpha Human Recombinant ( CSNK2A1 Human )

DescriptionCasein Kinase 2 alpha Human Recombinant is a non-glycosylated polypeptide having a molecular mass of 45.1 kDa. Casein Kinase 2 is purified by proprietary chromatographic techniques.SourceEscherichia Coli.Physical AppearanceSterile Filtered

$579.00

Data sheet

Formulation CSNK2A1 is supplied in 25mM Tris-HCl, 500mM NaCl, 1mM DTT, 500m PMSF, 50% glycerol, pH 8.5.
Purity Greater than 99% as determined by SDS-PAGE.
Description Casein Kinase 2 alpha 1 Human Recombinant is a non-glycosylated polypeptide having a molecular mass of 45.1 kDa. Casein Kinase 2 is purified by proprietary chromatographic techniques.
Protein Background The Casein kinase 2 (EC2.7.11.1) is a serine/threonine-selective protein kinasethat is a tetramer of two alpha subunits and two beta subunits. The alpha subunits have the catalytic kinase domain. Casein kinase 2 has been implicated in cell cyclecontrol, DNA repair, regulation of the circadian rhythmand other cellular processes. Casein kinase 2 activity has been reported to be activated following Wnt signaling pathwayactivation. A Pertussis toxin-sensitive G proteinand Disheveled appear to be an intermediary between Wnt-mediated activation of the Frizzled receptor and activation of casein kinase 2.Mice that lack casein kinase 2 alpha prime have a defect in the morphology of developing sperm.
Expression host Escherichia Coli.
Synonyms Casein kinase II subunit alpha, EC 2.7.11.1, CK II, CK2A1, CKII alpha, CSNK2A1, PKCK2, CSK21.
Reagent Appearance Sterile Filtered clear solution.
Unit Definition No protease activity detectable, specific activity > 1.320 U/mg (1U = 1umol/min at 37 degree C) using the synthetic peptide RRRDDDSDDD.
Storage Conditions Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
Advantages Starting material tested and certified negative for HIV I & II antibodies, Hepatitis B surface antigen, and Hepatitis C antibodies.

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