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LRRKtide
Cat. No. KS-010
Structure:
Activity:
Jaleel et al (2007) LRRK2 phosphorylates moesin at threonine-558: characterization of how Parkinson's disease mutants affect kinase activity. Biochem. J. 405 (2) 307 PMID: 17447891
Anand and Braithwaite (2009) LRRK2 in Parkinson’s disease: biochemical functions. FEBS J. 276 6428 doi:10.1111/j.1742-4658.2009.07341.x
Esteves et al (2014) LRRK2, a puzzling protein: Insights into Parkinson's disease pathogenesis. Exp. Neurol. 261 206 PMID: 24907399
Related areas
All kinases >
All substrate peptides >
All neuroscience categories >
Technical Data
| Structure | H-Arg-Leu-Gly-Arg-Asp-Lys-Tyr-Lys-Thr-Leu-Arg-Gln-Ile-Arg-Gln-OH |
| Molecular Weight | 1931.28 |
| Formula | C83H147N31O22 |
| Sequence | RLGRDKYKTLRQIRQ |
| Modifications | None |
Solubility and Storage
| Solubility | Soluble in dilute acid |
| Appearance | Freeze dried solid |
| Storage | Store dark, frozen and desiccated |
Batch Specific Data
| Purity | >95% by HPLC |
| Safety Data Sheet | LRRKtide MSDS_602bf65d835c6.pdf |
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Recent citations
A new publication from the University of Ljubljana uses MCA-AVLQSGFR-Lys(Dnp)-Lys-NH2, the FRET substrate for the severe acute respiratory syndrome coronavirus main protease (SARS-CoV Mpro), to determine the inhibitory potential of plant polyphenols
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