Product Name: KinSub1RDDYG
Product Number: PE-01AHH95
Size: 200 µg      Price:99.00
      $US
Peptide Name: KinSub1RDDYG

Product Use: For assaying the phosphotransferase activity of Yes-related protein-tyrosine kinase; Tyrosine-protein kinase Lyn (LynA, UniProt ID P07948). The KinSub1RDDYG peptide demonstrated medium phosphotransferase activity with LynA, and exhibited very high 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: KinSub1RDDYG 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: GGRERDDYGRGEGGG

Peptide Modifications N Terminus: Free amino

Peptide Modifications C Terminus: Amide

Peptide Molecular Mass Calculated: 1536.5 Da

Peptide Purity Percent after Synthesis and Purification: >95

Peptide Appearance: White powder

Peptide Form: Solid

Storage Conditions: -20°C

Peptide Recommended Enzyme: LynA

Scientific Background: LynA is one of several protein kinases that can phosphorylate KinSub1RDDYG. Human LynA is a protein-tyrosine kinase of 512 amino acid length, with a predicted molecular mass of 58,574 Da. It is a member of the TK group of protein kinases in the Src family. This kinase is highly expressed and widely distributed in most tested human tissues. Orthologues of Lyn are highly conserved in vertebrates, including amphibians. Lyn interacts with phosphorylated LIME1 and with CD79A upon BCR activation. Lyn is inhibited by phosphorylation at T503. It interacts with a variety of cell surface receptors on the cytoplasmic side of the plasma membrane (1,2). Lyn is biosynthetically transported to the plasma membrane via the Golgi pool of caveolin along the secretory pathway that requires its catalytic domain, but not activity. Lyn is expressed preferentially in B cells and can be bound in the plasma membrane with IgM, where it participates in antigen-mediated signal transduction (3). Crosslinking of membrane-bound IgM with antibody induces rapid increase in activities of Lyn and Lyn-associated PI 3-kinase. Lyn may be involved in the changes that are related to tumour pathogenesis (2). It has been linked with the development of acute myeloid leukemia and breast carcinomas.