Product Name: KinSub1RHLSF
Product Number: PE-01AHQ95
Size: | 200 µg | | Price: | 99.00 |
| | | $US | |
Peptide Name: KinSub1RHLSF
Product Use: For assaying the phosphotransferase activity of MAP kinase-interacting serine/threonine-protein kinase 2 (MNK2, UniProt ID Q9HBH9). The KinSub1RHLSF peptide demonstrated medium phosphotransferase activity with PKCg, and exhibited medium specificity when assayed with over 200 other protein kinases. A listing of other kinases that show appreciable phosphotransferase activity towards this peptide are listed in Table 1.
Peptide Production Method: Solid-phase peptide synthesis
Peptide Origin: KinSub1RHLSF was originally identified using a microarray with peptides that were predicted as optimal substrates for 500 human protein kinases with a proprietary algorithm developed at Kinexus with our academic partners.
Peptide Sequence: GGLSRHLSFCPCGGG
Peptide Modifications N Terminus: Free amino
Peptide Modifications C Terminus: Amide
Peptide Molecular Mass Calculated: 1446.7 Da
Peptide Purity Percent after Synthesis and Purification: >95
Peptide Appearance: White powder
Peptide Form: Solid
Storage Conditions: -20°C
Peptide Recommended Enzyme: PKCg
Scientific Background: MNK2 is one of several protein kinases that can phosphorylate KinSub1RHLSF. Human MNK2 is a protein-serine/threonine kinase of 414 amino acid length, with a predicted molecular mass of 46,711 Da. It is a member of the CAMK group of protein kinases in the MAPKAPK family, and MNK subfamily. This kinase is highly expressed and widely distributed in most tested human tissues except apparently in the brain and spinal cord. Orthologues of MNK2 are highly conserved in vertebrates, including amphibians. MNK2 binds tightly to ERK1 and ERK2. MNK2 features a conserved C-terminal ERK-interacting domain, a catalytic domain with homology to the calcium/calmodulin-dependent family of kinases, and putative MAP kinase phosphorylation sites located within the T loop of the kinase domain. MNK2 is activated by phosphorylation at T244, T249 and T379 by ERK1, ERK2, and p38a MAPK. ERK and p38 phosphorylate MNK2, which stimulates its in vitro kinase activity toward eukaryotic initiation factor-4E (eIF-4E) (1). MNK2 interacts with dephosphorylated ERK1 and ERK2, and EIF4G1 and EIF4G2. A yeast two-hybrid screen showed the MNK2 protein interacted with the ligand-binding domain of estrogen receptor beta (ERbeta) (2).