PTEN Antibody (N-term) Blocking Peptide

Peptides; Blocking Peptides

PTEN, (phosphatase and tensin homolog deleted on chromosome 10), also known as MMAC1 (mutated in multiple advanced cancers 1), is a tumor suppressor implicated in a large number of human tumors. The PTEN phosphatase incorporates the catalytic motif (HCXXGXXRS/T) that is a signature of the protein tyrosine phosphatase family. Recombinant human PTEN is a dual phosphatase with ability to dephosphorylate both tyrosine and serine/threonine residues. PTEN functions primarily as a lipid phosphatase to regulate signal transduction pathways, with a primary target identified as phosphatidylinositol 3, 4, 5 trisphosphate. In addition, PTEN presents weak tyrosine phosphatase activity, which may downregulate signaling pathways involving focal adhesion kinase or Shc. PTEN negatively regulates activation of the serine/threonine kinase Akt/PKB by blocking its phosphorylation, thereby inhibiting the PI 3 kinase Akt signaling pathway, which is important for cell survival. In vivo, the majority of PTEN missense mutations detected in tumor specimens target the phosphatase domain and cause a loss in PTEN phosphatase activity. Mutations in PTEN are associated with several common cancers including prostate, brain and breast cancer, and with Cowden's disease, an autosomal dominant disorder conferring susceptibility to benign and malignant tumors. Germline mutations of PTEN are also linked Lhermitte-Duclos disease and Bannayan-Zonana syndrome. Mutations of PTEN occur in 60 to 80% of prostate cancers. PTEN is also essential for embryonic development.

Synthetic peptide