recommended for detection of Thr 170 phosphorylated Cdk7 of human origin by WB, IP, IF, IHC(P) and ELISA
Modification
Phosphoralated
Modification Notes
Progression through the cell cycle requires activation of a series of enzymes designated cyclin dependent kinases (Cdks). The monomeric catalytic subunit Cdk2, a critical enzyme for initiation of cell cycle progression, is completely inactive. Partial activation is achieved by the binding of regulatory cyclins such as cyclin D1, while full activation requires additional phosphorylation at Thr 160. The enzyme responsible for the phosphorylation of Cdk2 on Thr 160 and also of Cdc2 p34 on Thr 161, designated Cdk-activating kinase (CAK), has been partially purified and shown to be comprised of a catalytic subunit and a regulatory subunit. The catalytic subunit, designated Cdk7, has been identified as the mammalian homolog of MO15, a protein kinase demonstrated in starfish and Xenopus. The regulatory subunit is a novel cyclin (cyclin H) and is required for activation of Cdk7. Like other Cdks, Cdk7 contains a conserved threonine residue required for full activity; mutation of this residue severely reduces CAK activity. Phosphorylation of human Cdk7 at Thr 170 is required for Cdk7 activity.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFIHCELISA
WB:1:500~1:2000 IP:1:100~1:500 IF:1:200~1:500 IHC:1:50~1:200 Notes:Optimal dilutions/concentrations should be determined by the researcher.
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
recommended for detection of Thr 170 phosphorylated Cdk7 of human origin by WB IP IF IHC(P) and ELISA
Tissue Specificity
recommended for detection of Thr 170 phosphorylated Cdk7 of human origin by WB, IP, IF, IHC(P) and ELISA