Recombinant Human CDK5&p25 Protein was resolved with SDS-PAGE under reducing (Lane 1) and non-reducing (Lane 2) conditions.
The activity of CDK5/p25 is based on the MSA technology, and the content and ratio of the substrate and the product are directly separated and detected in real time and dynamically by the different migration rates of the substrate and the product after the enzymatic reaction.
CDK5 belongs to the cyclin-dependent kinase family and is a proline-directed serine/threonine kinase, which was first identified as a CDK family member due to its similar structure to CDC2/CDK1 in humans. Even though CDK5 has a similar structure to other cyclin-dependent kinases, its activators are highly specific (CDK5R1 and CDK5R2). CDK5R1 encoded by the gene (p35) is a neuron-specific activator of CDK5. The p35 form is proteolytically cleaved by calpain, generating a p25 form. The cleavage of p35 into p25 results in relocalization of the protein from the cell periphery to nuclear and perinuclear regions. p25 deregulates CDK5 activity by prolonging its activation and changing its cellular location.
