Human Casein Kinase 2 alpha Alexa Fluor® 405-conjugated Antibody

Applications

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Preparation and Storage

Background: Casein Kinase 2 alpha

Casein kinase 2 (CK2) is a ubiquitous and constitutively active tetrameric serine/threonine kinase that is comprised of two catalytic subunits (CK2 alpha and/or CK2 alpha ‘) and two identical regulatory subunits (CK2 beta ). CK2 has been implicated in numerous cellular processes, including signal transduction, transcription, translation, replication, and metabolic pathways. CK2 is known to phosphorylate more than 300 different substrates. Phosphorylation of cell-cycle proteins such as p53, p34cdc2, p27KIP1, and MDM-2 account for the ability of CK2 to induce proliferation, while the phosphorylation of HS1, Bid, and Max account for its antiapoptotic role. The human CK2 alpha and CK2 alpha ‘ subunits are the products of two different genes. They have highly conserved catyalytic domains but divergent C-terminal regions. Within aa 253-391 (including the region of divergence between CK2 alpha and CK2 alpha ’), the 35-45 kDa human CK2 alpha shares 96% aa sequence identity with mouse and rat CK2 alpha. An alternatively spliced isoform of human CK2 alpha lacks the N-terminal 136 amino acids including a portion of the kinase domain. CK2 beta plays dual roles in the regulation of CK2 acivity. Its C-terminal domain is responsible for stable interactions with the catalytic subunit and increased catalytic activity following tetramer formation, while the N-terminal domain exerts negative regulation on the catalytic activity of CK2.

Product Datasheets

Related Research Areas

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