Date published: 2026-4-20

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Cdk5 substrate

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Alternate Names:
H-Pro-Lys-Thr-Pro-Lys-Lys-Ala-Lys-Lys-Leu-OH
Application:
Cdk5 Substrate is derived from the Histone H1 peptide sequence docked in the active site of Cdk5
Purity:
≥95%
Molecular Weight:
1138.5
Molecular Formula:
C53H99N15O12
For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.
* Refer to Certificate of Analysis for lot specific data.

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Cdk5 substrate, a pivotal component in the study of neuronal development and signaling pathways, is integral to research focused on the understanding of neuronal migration and cytoskeletal organization. Cyclin-dependent kinase 5 (Cdk5), activated by p35 or p39, primarily phosphorylates this substrate, which plays a critical role in the regulation of synaptic plasticity and neuronal structure. In research contexts, Cdk5 substrate is used to explain the kinase′s role in neurodevelopmental processes, where its abnormal regulation is linked to disruptions in neuronal signaling and morphology. Studies involving Cdk5 substrate often focus on its phosphorylation state and its interaction with various proteins that influence cytoskeletal dynamics and intracellular signaling cascades. This chemical is essential for examining the biochemical pathways that underlie synaptic function and the maintenance of neuronal networks. Additionally, it aids in the exploration of signaling mechanisms that govern cell cycle processes in post-mitotic neurons, providing insights into cellular mechanisms that could lead to neurodegeneration. This research is foundational for understanding complex neural behaviors and the molecular basis of neurobiological disorders, reinforcing the importance of Cdk5 substrate in basic neurological research.


Cdk5 substrate References

  1. Identification of substrate binding site of cyclin-dependent kinase 5.  |  Sharma, P., et al. 1999. J Biol Chem. 274: 9600-6. PMID: 10092646
  2. A scintillation proximity assay for studying inhibitors of human tau protein kinase II/cdk5 using a 96-well format.  |  Evans, DB., et al. 2002. J Biochem Biophys Methods. 50: 151-61. PMID: 11741704
  3. The amyloid-beta peptide binds to cyclin B1 and increases human cyclin-dependent kinase-1 activity.  |  Milton, NG. 2002. Neurosci Lett. 322: 131-3. PMID: 11958860
  4. Intragenic modifiers of hereditary spastic paraplegia due to spastin gene mutations.  |  Svenson, IK., et al. 2004. Neurogenetics. 5: 157-64. PMID: 15248095
  5. Design of a novel class of peptide inhibitors of cyclin-dependent kinase/cyclin activation.  |  Gondeau, C., et al. 2005. J Biol Chem. 280: 13793-800. PMID: 15649889
  6. Identification of an hexapeptide that binds to a surface pocket in cyclin A and inhibits the catalytic activity of the complex cyclin-dependent kinase 2-cyclin A.  |  Canela, N., et al. 2006. J Biol Chem. 281: 35942-53. PMID: 17001081
  7. Dynamics of Cdk1 substrate specificity during the cell cycle.  |  Kõivomägi, M., et al. 2011. Mol Cell. 42: 610-23. PMID: 21658602
  8. Determination of kinetic parameters and structure-activity relationships of ginsenosides as inhibitors of cyclin-dependent kinase 5/p25 using ultra-pressure liquid chromatography with triple quadrupole tandem mass spectrometry.  |  Chen, N., et al. 2013. Rapid Commun Mass Spectrom. 27: 985-92. PMID: 23592201
  9. Substrate specificity characterization of a cdc2-like protein kinase purified from bovine brain.  |  Beaudette, KN., et al. 1993. J Biol Chem. 268: 20825-30. PMID: 8407912
  10. Effect of heparin on phosphorylation site specificity of neuronal Cdc2-like kinase.  |  Qi, Z., et al. 1998. FEBS Lett. 423: 227-30. PMID: 9512362

Ordering Information

Product NameCatalog #UNITPriceQtyFAVORITES

Cdk5 substrate, 500 µg

sc-3066
500 µg
$91.00