Recombinant human CDK7 + Cyclin H + MNAT1 protein (ab64303)

Overview

  • Product nameRecombinant human CDK7 + Cyclin H + MNAT1 protein
  • Protein lengthFull length protein

Description

  • NatureRecombinant
  • SourceBaculovirus infected Sf9 cells
  • Amino Acid Sequence
    • SpeciesHuman

Associated products

Specifications

Our Abpromise guarantee covers the use of ab64303 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Biological activitySpecific activity: 19 nmol/min/mg.
  • Applications

    SDS-PAGE

    Functional Studies

  • Purity> 90 % SDS-PAGE.

  • FormLiquid
  • Additional notes

    ab64311 (Myelin Basic Protein protein) can be utilized as a substrate for assessing kinase activity

  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.

    Preservative: 150mM Imidazole
    Constituents: 25% Glycerol, 50mM Sodium phosphate, 300mM Sodium chloride, 0.2mM DTT, 0.1mM PMSF, pH 7

    This product is an active protein and may elicit a biological response in vivo, handle with caution.

General Info

  • Alternative names
    • CAK
    • CAK1
    • CCNH
    • CDK activating kinase
    • Cyclin dependent kinase 7
    • Cyclin H
    • MAT1
    • MO15
    • MO15 associated protein
    • p34
    • p35
    • p36
    • p37
    • STK1
    see all
  • RelevanceCDK7: Cyclin-dependent kinases (CDKs) are activated by the binding to a cyclin and mediate the progression through the cell cycle. Each different complex controls a specific transition between two subsequent phases in the cell cycle. CDK7 is the catalytic subunit of the CDK-activating kinase (CAK) complex, a serine-threonine kinase. CAK activates the cyclin-associated kinases CDC2/CDK1, CDK2, CDK4 and CDK6 by threonine phosphorylation. CAK complexed to the core-TFIIH basal transcription factor activates RNA polymerase II by serine phosphorylation of the repetitive C-terminus domain (CTD) of its large subunit (POLR2A), allowing its escape from the promoter and elongation of the transcripts. Involved in cell cycle control and in RNA transcription by RNA polymerase II. Its expression and activity are constant throughout the cell cycle. Cyclin H: Regulates CDK7, the catalytic subunit of the CDK-activating kinase (CAK) enzymatic complex. CAK activates the cyclin-associated kinases CDC2/CDK1, CDK2, CDK4 and CDK6 by threonine phosphorylation. CAK complexed to the core-TFIIH basal transcription factor activates RNA polymerase II by serine phosphorylation of the repetitive C-terminus domain (CTD) of its large subunit (POLR2A), allowing its escape from the promoter and elongation of the transcripts. Involved in cell cycle control and in RNA transcription by RNA polymerase II. Its expression and activity are constant throughout the cell cycle. MNAT1: Stabilizes the cyclin H-CDK7 complex to form a functional CDK-activating kinase (CAK) enzymatic complex. CAK activates the cyclin-associated kinases CDC2/CDK1, CDK2, CDK4 and CDK6 by threonine phosphorylation. CAK complexed to the core-TFIIH basal transcription factor activates RNA polymerase II by serine phosphorylation of the repetitive C-terminus domain (CTD) of its large subunit (POLR2A), allowing its escape from the promoter and elongation of the transcripts. Involved in cell cycle control and in RNA transcription by RNA polymerase II.
  • Cellular localizationNuclear

Recombinant human CDK7 + Cyclin H + MNAT1 protein images

  • The specific activity of CDK7 + Cyclin H + MNAT1 (ab64303) was determined to be 19nmol/min/mg as per activity assay protocol.

  • SDS-PAGE analysis of ab64303. The purity of CDK7 + Cyclin H + MNAT1 (ab64303) was determined to be >90% by densitometry, CDK7 approx. MW 40kDa, CyclinH1 approx. MW 39kDa and MNAT1  approx. MW 37kDa

References for Recombinant human CDK7 + Cyclin H + MNAT1 protein (ab64303)

ab64303 has not yet been referenced specifically in any publications.

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