Product Name: NDR1 (285-291) pY288
Product Number: PE-04ABN85
| Size: | 200 µg | Price: | 35.00 | |
| 1 mg | $US | 71.00 | ||
| 5 mg | 153.00 |
Peptide Name: NDR1 (285-291) pY288
Product Use: This phosphopeptide may be useful as a substrate for screening the phosphatase activity of protein phosphatases. The peptide sequence is located in the protein kinase catalytic domain activation T loop region between subdomains VII and VIII. T288 phosphorylation is predicted to be inhibitory for phosphotransferase activity.
Peptide Production Method: Solid-phase peptide synthesis
Peptide Origin: Homo sapiens
Peptide Sequence: TPD-pY-IAP
Peptide Modifications N Terminus: Free amino
Peptide Modifications C Terminus: βAla-Cys
Peptide Modifications Other: Phosphorylated
Product Use: This phosphopeptide may be useful as a substrate for screening the phosphatase activity of protein phosphatases. The peptide sequence is located in the protein kinase catalytic domain activation T loop region between subdomains VII and VIII. T288 phosphorylation is predicted to be inhibitory for phosphotransferase activity.
Peptide Production Method: Solid-phase peptide synthesis
Peptide Origin: Homo sapiens
Peptide Sequence: TPD-pY-IAP
Peptide Modifications N Terminus: Free amino
Peptide Modifications C Terminus: βAla-Cys
Peptide Modifications Other: Phosphorylated
Peptide Molecular Mass Calculated: 1041.1 Da
Peptide Purity Percent after Synthesis and Purification: >80
Peptide Appearance: White powder
Peptide Form: Solid
Storage Conditions: -20°C
Peptide Purity Percent after Synthesis and Purification: >80
Peptide Appearance: White powder
Peptide Form: Solid
Storage Conditions: -20°C
Scientific Background: NDR1 (STK38) is a protein-serine/threonine kinase of the AGC group and NDR family. It is activated by binding of S100B, which releases autoinhibitory N-lobe interactions, enabling ATP to bind and the autophosphorylation of S281. Phosphorylation at S281 increases phosphotransferase activity and interaction with MOBP. T444 then undergoes calcium-dependent phosphorylation by an upstream kinase. Interactions between phosphorylated T444 and the N-lobe promote additional structural changes that complete the activation of the kinase. Phosphorylation at T74 induces interaction with S100B. T444 then undergoes calcium-dependent phosphorylation by an upstream kinase. T74A, K118A, S281A, and T444A mutations are involved in decreased or loss of autophosphorylation and kinase activity. NDR1 is a negative regulator of MAP3K1/2 signalling. It converts MAP3K2 from its phosphorylated form to its nonphosphorylated form and inhibits autophosphorylation of MAP3K2. NDR1 is an important regulator of Myc's oncogenic activity in human B-cell lymphomas. It also regulates G/S cell cycle transition. The MAPK/ERK pathway has been implicated in oncogenesis as either a promoter or inhibitor depending on the cancer system.
© Kinexus Bioinformatics Corporation 2017