Casein Kinase-enzyme

Casein kinase has been widely used for decades to denote protein kinases sharing the ability to readily phosphorylate casein. The casein kinases (CK) belong to the serine/threonine kinases. There are two main classes: casein kinase 1 (CKI) and casein kinase 2 (CK2).

Casein kinase 1 (CK1) family is highly conserved in eukaryotic organisms from yeast to humans with the following family members. CK1 kinases are constitutively active in cells. Expression and activity of CK1 kinases can be stimulated by several mechanisms, including insulin and gamma-irradiation. The substrates of CK1 kinases include various intracellular proteins, such as enzymes, transcription factors and receptors. CK1 kinases play important roles in a variety of cellular events, including cell division, apoptosis and regulating the Wnt pathway. Deregulation of CK1 kinases have been observed in neurodegenerative disorders and cancer. Therefore the use of CK1 inhibitors attracts attentions and is under further investigations.

The Casein kinase 2 is a serine/threonine-selective protein kinase that is a tetramer of two alpha subunits and two beta subunits. The alpha subunits have the catalytic kinase domain. CK2 has been implicated in cell cycle control, DNA repair, regulation of the circadian rhythm and other cellular processes.

Sino biological offers a comprehensive set of tools for Casein kiinase related to biology research, including recombinant proteins, antibodies (mouse mAbs, rabbit mAbs, and rabbit pAbs), ELISA kits, and ORF cDNA clones.

CK belong to the serine/threonine protein kinase. There are two main classes: casein kinase 1 (CKI) and casein kinase 2 (CK2).

CK1 family