Molecular structure of Syntide-2, Protein Kinase Substrate, CAS Number: 108334-68-5
Syntide-2, Protein Kinase Substrate (CAS 108334-68-5)
Alternate Names:
Pro-leu-ala-arg-thr-leu-ser-val-ala-gly-leu-pro-gly-lys-lys
Application:
Syntide-2, Protein Kinase Substrate is a peptide substrate of protein kinase enzymes
CAS Number:
108334-68-5
Purity:
>97%
Molecular Weight:
1507.82
Molecular Formula:
C68H122N20O18
For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.
* Refer to Certificate of Analysis for lot specific data.
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Syntide-2, Protein Kinase Substrate is a synthetic peptide recognized as a substrate by CaMKII (Ca2+/calmodulin-dependent protein kinase II) enzymes. The sequence of Syntide-2 is homologous to phosphorylation site 2 on glycogen synthase, a target of CaMKII action. Syntide-2 has been used as a probe to assay localization of CaMKII activity and to study the effects of point mutations on phosphorylation activity. Numerous kinase enzymes including CaMKV and Raf-1 are reported to recognize Syntide-2 as a substrate as well, suggesting a wide scope of Syntide-2-assayable systems. Syntide-2, Protein Kinase Substrate is a substrate of Raf-1and PKC.
Syntide-2, Protein Kinase Substrate (CAS 108334-68-5) References
- Raf-1: a kinase currently without a cause but not lacking in effects. | Li, P., et al. 1991. Cell. 64: 479-82. PMID: 1846778
- Calcium. calmodulin-dependent protein kinase II and calcium. phospholipid-dependent protein kinase activities in rat tissues assayed with a synthetic peptide. | Hashimoto, Y. and Soderling, TR. 1987. Arch Biochem Biophys. 252: 418-25. PMID: 3028265
- The Metastasis Suppressor Protein Nme1 Is a Concentration-Dependent Modulator of Ca2+/Calmodulin-Dependent Protein Kinase II. | Royer, L., et al. 2019. Biochemistry. 58: 2710-2714. PMID: 31141673
- Calcium-dependent protein kinase 5 links calcium signaling with N-hydroxy-l-pipecolic acid- and SARD1-dependent immune memory in systemic acquired resistance. | Guerra, T., et al. 2020. New Phytol. 225: 310-325. PMID: 31469917
- Characterization of Calcium-Dependent Protein Kinases 3, a Protein Involved in Growth of Cryptosporidium parvum. | Zhang, Q., et al. 2020. Front Microbiol. 11: 907. PMID: 32457733
- Design, synthesis and biological evaluation of pyrazolo[3,4-d]pyrimidine-based protein kinase D inhibitors. | Gilles, P., et al. 2020. Eur J Med Chem. 205: 112638. PMID: 32835918
- Characterization of two group III potato CDPKs, StCDPK22 and StCDPK24, that contain three EF-Hand motifs in their CLDs. | Sciorra, MD., et al. 2021. Plant Physiol Biochem. 162: 716-729. PMID: 33799183
- Na+/Ca2+ exchanger mediates cold Ca2+ signaling conserved for temperature-compensated circadian rhythms. | Kon, N., et al. 2021. Sci Adv. 7: PMID: 33931447
- Mechanism of kinetin-induced death of Vicia faba ssp. minor root cortex cells. | Kaźmierczak, A., et al. 2021. Sci Rep. 11: 23746. PMID: 34887458
- Comparative Characterization of CpCDPK1 and CpCDPK9, Two Potential Drug Targets Against Cryptosporidiosis. | Su, J., et al. 2022. Microorganisms. 10: PMID: 35208789
- CaMKII binds both substrates and activators at the active site. | Özden, C., et al. 2022. Cell Rep. 40: 111064. PMID: 35830796
- Branch point strength controls species-specific CAMK2B alternative splicing and regulates LTP. | Franz, A., et al. 2023. Life Sci Alliance. 6: PMID: 36543542
- PKD autoinhibition in trans regulates activation loop autophosphorylation in cis. | Reinhardt, R., et al. 2023. Proc Natl Acad Sci U S A. 120: e2212909120. PMID: 36745811
- Stabilization of calmodulin-dependent protein kinase II through the autoinhibitory domain. | Ishida, A. and Fujisawa, H. 1995. J Biol Chem. 270: 2163-70. PMID: 7836445
- Purification and characterization of Ca2+/calmodulin-dependent protein kinase V from rat cerebrum. | Mochizuki, H., et al. 1993. J Biol Chem. 268: 9143-7. PMID: 8386178
Substrate of:
CaMKII, Peptide, PKC, and Raf-1.Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
Syntide-2, Protein Kinase Substrate, 1 mg | sc-201151 | 1 mg | $179.00 |