For in vitro use only!
Shipping: shipped at ambient temperature
Storage Conditions: store at -20 °C
avoid freeze/thaw cycles
Shelf Life: 12 months
Molecular Formula: RRKDLHDDEEDEAMSITA
Molecular Weight: 2131 g/mol
Purity: 85 - 90 % (HPLC)
Form: lyophilised (reconstitution in ddH2O)
The synthetic peptide RRKDLHDDEEDEAMSITA can be used as a substrate for CK1 (casein kinase 1) in in vitro kinase assays. It is phosphorylated by CK1 with a Km of 172 μM.
In mammals and vertebrates, there are seven CK1 genes coding for a, b, g1, g2, g3, d, and e isoforms, and some of these genes generate several proteins through alternative splicing. The CK1 isoforms may have different functions, for instance, CK1e is involved in regulating circadian rhythm through phosphoration of period (per) proteins, and it has also been linked to the activity of group I metabotropic glutamate receptors. CK1d may be involved in neurodegenerative diseases. CK1a apparently participates in the phosphorylation of G protein-regulated receptors and nuclear factor for activated T cells 4 (NF-AT4) phosphorylation. However, in vitro studies with model peptides using different isoforms of CK1 have not shown significant differences in the preferred target sequences. Differences in functions of isoforms most probably involve differential expression and cellular localization and specific docking sites that confer substrate selectivity. CK1e and CK1d have an interesting regulatory mechanism where autophosphorylation of their carboxyl-terminal extensions inhibits their catalytic activity. Dephosphorylation of these carboxyl residues by calcineurin may be a mechanism for regulating the activity of these isoforms.
Marin et al. (1994) Design and synthesis of two new peptide substrates fort he spevcific and sensitive monitoring of casein kinase-1 and -2. Biochem. Biophys. Res. Commun. 198:898.
Marin et al. (2003) A noncanonical sequence phosphorylated by casein kinase 1 in beta-catenin may play a role in casein kinase 1 targeting of important signaling proteins. Proc. Natl. Acad. Sci. USA. 100:10193.