Phosphorylated LRRKtide
RLGRDKYK-[pT]-LRQIRQ-amide
Description
Application Data
Description
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Substrate for the leucine-rich repeat kinase 2 (LRRK2) with phosphorylated threonine residue
Application Data
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Data Sheet Material Safety Data Sheet (MSDS)Catalogue number crb1000466 Molecular Weight 2009.1 Sequence (one letter code) RLGRDKYK-[pT]-LRQIRQ-amide
Sequence (three letter code) H-Arg-Leu-Gly-Arg-Asp-Lys-Tyr-Lys-[pThr]-Leu-Arg-Gln-Ile-Arg-Gln-NH2, Where [pThr] is phospho Threonine
Aliase ERM peptide, ERMtide, Leucine-Rich Repeat Kinase substrate, Moesin Purity >95% References Esteves et al (2014) LRRK2, a puzzling protein: Insights into Parkinson's disease pathogenesis. Exp. Neurol. 261 206 PMID: 24907399
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
Manufactured in: United Kingdom LRRKtide (also called moesin) is a peptide substrate for leucine-rich repeat kinase 2 (LRRK2). The sequence of LRRKtide has been derived from the ERM proteins: Ezrin (amino acids 561-573), radixin (amino acids 558-570) and moesin (amino acids 539-553). These proteins influence cytoskeletal dynamics by anchoring the cytoskeleton to the plasma membrane. LRRK2 phosphorylates LRRKtide at its Thr558 site. This peptide contains the phosphorylated threonine residue.
LRRK2 is a large, ubiquitous protein of unknown function. LRRK2 has GTPase and kinase activity, and is located in multiple areas of the cell, associated with intracellular membranes and vesicular structures; suggesting LRRK2 may be involved in several cellular pathways. LRRK2 is also found in most organs and mutations in LRRK2 have been identified in Parkinson’s disease.
The threonine residue at position 9 of this peptide has been phosphorylated.