Product Name: PKCMSubtide
Product Number: PE-01BIV90
Size: 200 µg      Price:43.00
1 mg      $US85.00
5 mg      201.00
Peptide Name: PKCMSubtide

Product Use: For assaying the phosphotransferase activity of Protein-serine kinase C mu (Protein kinase D) (UniProt ID Q15139).

Peptide Production Method: Solid-phase peptide synthesis

Peptide Sequence: FLRRRMSFVGFPA

Peptide Modifications N Terminus: Free amino

Peptide Modifications C Terminus: βAla-Cys

Peptide Molecular Mass Calculated: 1757.17 Da

Peptide Purity Percent after Synthesis and Purification: >90

Peptide Appearance: White powder

Peptide Form: Solid
Storage Conditions: -20°C

Peptide Recommended Enzyme: PKCM

Scientific Background: PKD1 (PRKD1, PKCm, PKC-mu) is a protein-serine/threonine kinase of the CAMK group and PKD family. It is a protein in the novel protein kinase C family. It is moderate to highly expressed in most tested human tissues, especially in the thymus, lung and peripheral blood mononuclear cells, but poorly expressed in the brain and spinal cord. It is dependent on acidic phospholipids (e.g. phosphatidylserine) and diacylglycerol (DAG) for full phosphotransferase activity, and does not require calcium. PKD1 is activated by DAG and phorbol esters, which via its phorbol-ester/DAG-type domain 1 binds DAG with high affinity and appears to play the dominant role in mediating translocation to the cell membrane and trans-Golgi network. Phorbol-ester/DAG-type domain 2 binds phorbol ester with higher affinity. Phosphorylation at Y95 increases kinase activity and induces interaction with PKC-delta. Phosphorylation at S249, Y463, S738, S742 and S910 increases kinase activity. Autophosphorylation of S742 and phosphorylation of S738 by PKC relieves auto-inhibition by the PH domain, and also induces interaction with ASK1, JNK1 and IKKb. Phosphorylation at S205, S208, S219 and S223 induces binding of 14-3-3 beta and tau to inhibit PKD1 phosphotransferase activity. Phosphorylation at S397 induces interaction with 14-3-3 beta. PKD1 forms a complex in vivo with a PI4-kinase and a PI4-phosphate 5-kinase. A region of PKD1 between the amino-terminal transmembrane domain and the pleckstrin homology domain has been shown to be involved in the association with the lipid kinases . PKD1 is thought to have a role in regulating cellular trafficking, actin remodeling, gene transcription and protection from oxidative stress. PKD1 is implicated in prostate cancer through phosphorylation of e-cadherin leading to increased malignancy and motility of tumours. PKD1 has also been linked with the development of colorectal adenocarcinomas, lung bronchoalveolar carcinomas and melanomas (metastatic).