Product Name: KinSub9RRKSF
Product Number: PE-01ALQ95
Size: 200 µg      Price:99.00
      $US
Peptide Name: KinSub9RRKSF

Product Use: For assaying the phosphotransferase activity of Mammalian STE20-like protein-serine kinase 3; Serine-threonine-protein kinase 24 (MST3, UniProt ID Q9Y6E0). The KinSub9RRKSF peptide demonstrated high phosphotransferase activity with Pim1, and exhibited very low 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: KinSub9RRKSF 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: GGRSRRKSFRRIGHG

Peptide Modifications N Terminus: Free amino

Peptide Modifications C Terminus: Amide

Peptide Molecular Mass Calculated: 1726 Da

Peptide Purity Percent after Synthesis and Purification: >95

Peptide Appearance: White powder

Peptide Form: Solid

Storage Conditions: -20°C

Peptide Recommended Enzyme: Pim1

Scientific Background: MST3 is one of several protein kinases that can phosphorylate KinSub9RRKSF. Human Mst3 is a protein-serine/threonine kinase of 443 amino acid length, with a predicted molecular mass of 49,308 Da. It is a member of the STE group of protein kinases in the STE20 family, and YSK subfamily. This kinase is highly expressed and widely distributed in most tested human tissues. Orthologues of Mst3 are highly conserved in animals and plants. MST3 contains a conserved kinase domain at its N-terminus and a regulatory domain at its C-terminus. Caspase-mediated cleavage of the regulatory domain of MST3 activates its intrinsic kinase activity and leads to nuclear translocation. Expression of C-terminal truncated MST3 in cells results in DNA fragmentation and induction of apoptosis (1). MST3 can inhibit cell migration in a fashion dependent on autophosphorylation and can regulate paxillin phosphorylation through tyrosine phosphatase PTP-PEST (2).