CDK2/CyclinE1, GST-Tag Recombinant

Catalog #
40102
$410 *
Size: 10 µg
Qty
*US Pricing only. For international pricing, please contact your local distributor.
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Description

Recombinant human complex of CDK2 (cyclin dependent kinase 2), encompassing amino acids 2-298(end) and cyclinE1, encompassing amino acids 2-410(end). Both CDK2 and cyclinE1 constructs contain an N-terminal GST-tag, followed by a Thrombin Cleavage Site. The proteins were co-expressed in Sf9 cells and purified.

Synonyms
Cyclin-Dependent Kinase 2, CDK2: p33 (CDK2)
CyclinE1: CCNE1, CCNE, CDK-2
Product Info
Storage and Usage
Citations
Species
Human
Construct
CDK2 (GST-2-298(end)) / CyclinE1 (GST-2-410(end))
Host Species/Expression System
Sf9
Purity

≥80%

Format
Aqueous buffer solution
Formulation

40 mM Tris-HCl, pH 8.0, 110 mM NaCl, 2.2 mM KCl, 0.04% Tween-20, and 20% glycerol

MW
CDK2: 61 kDa; Cyclin E1: 74 kDa
Amino Acids
CDK2: 2-298(end) / CyclinE1: 2-410(end)
Specific Activity

84 pmol/min/µg

Genbank #
CDK2: NM_001798; Cyclin E1: NM_001238
UniProt #
CDK2: P24941; CyclinE1: P24864
Tag(s)
N-terminal GST-tag
Background

CDK2 (cyclin dependent kinase 2), also known as cell division protein kinase 2, is a member of the serine/threonine cyclin-dependent protein kinase family, and it is involved in cell cycle.  CDK2 is regulated by phosphorylation and can associate with either cyclin E during G1 phase and cyclin A during S phase. Its association with cyclins induces a conformational change that results in a dramatic increase of the kinase activity. Cyclin levels vary during the cell cycle, which allow cyclins to regulate CDK activity in the cell. Dissociation of the complex returns CDK to its basal activity, and CDK is degraded by ubiquitin-mediated proteolysis. CDK2 can phosphorylate several proteins, being part of DNA damage, protein degradation, signal transduction, and other crucial cellular pathways. Lack of regulation in cell cycle can result in cancer. In general, CDK2 is not itself upregulated or hyperactive in cancer, and its abnormal activity comes from dysregulation in its binding partners. For instance, cyclin E is overexpressed and/or has abnormal activity in many cancers, including breast, lung cancer and leukemia. The development of inhibitors specific for CDK2 has been difficult, as CDKs have similar active sites, and for instance inhibition of CDK1 can be highly detrimental. The understanding of the mechanisms involved in cell cycle regulation, and its control via the use of small molecule inhibitors alone or in combination therapy will open new therapeutic avenues for the treatment of cancer and neurodegenerative diseases.

References
1. Levkau, B. et al: Cleavage of p21(Cip1/Waf1) and p27(Kip1) mediates apoptosis in endothelial cells through activation of Cdk2: role of a caspase cascade. Molec. Cell1: 553-563, 1998.
2. Huang, H. et al: CDK2-dependent phosphorylation of FOXO1 as an apoptotic response to DNA damage. Science314: 294-297, 2006.