Anti-phospho PTEN (Ser385) Antibody

Evaluated by Western Blotting in MDA-MB-468 cells transfected with PTEN mutant (C124S) cell lysate.

Western Blotting Analysis: This antibody (0.2 µg/mL) detected Ser385 phosphorylation of the dual lipid and protein phosphatase dead C124S PTEN mutant in lysates of C124S PTEN-transfected MDA-MB-468 cells (Lysate courtesy of Dr James Hastie, University of Dundee, UK).

Peptide Inhibition Analysis: Target specificity of this antibody was confirmed by antibody blocking using the immunogen peptide and the corresponding non-phosphorylated peptide prior to Western blotting detection of Ser385 phosphorylated C124S PTEN mutant in lysate from transfected MDA-MB-468 cells. (Lysate courtesy of Dr James Hastie, University of Dundee, UK).

This Anti-phospho PTEN (Ser385) Antibody is validated for use in Western Blotting and Peptide Inhibition Assay for the detection of phospho PTEN (Ser385).

PTEN phosphorylated on Serine residue 385

Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (EC 3.1.3.16, EC 3.1.3.48, EC 3.1.3.67; UniProt P60484; also known as Mitochondrial PTENalpha, Phosphatase and tensin-like protein, Mutated in multiple advanced cancers 1, Mitochondrial phosphatase and tensin protein alpha, MMAC1 phosphatase and tensin homolog deleted on chromosome 10, Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN) is encoded by the PTEN (also known as 10q23del, BZS, CWS1, DEC, GLM2, TEP1, MMAC1, MHAM, PTEN1) gene (Gene ID 5728) in human. PTEN protein catalyzes the removal of phosphate from phosphoserine, phosphothreonine, and phosphotyrosine residues on substrate proteins, as well as the phosphate in the D3 position of the inositol ring from phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-diphosphate, phosphatidylinositol 3-phosphate and inositol 1,3,4,5-tetrakisphosphate. PTEN plays a major role in controlling cell growth and proliferation, and PTEN gene mutains are found in a large number of cancers at high frequency. PTEN activity, stability, localization, and conformation are controlled through complex regulatory mechanisms, including the reversible phosphorylations of several Ser/Thr (S/T) residues in its unfolded C-terminal tail region (PTEN-Ctail, residues 351–403). PTEN S370, S380, T382, T383 and S385 are known target sites by casein kinase II (CK2), while S361, T363, S362, and T366 are phosphorylated by glycogen synthase kinase-3 β (GSK3β). In addition, Polo-like kinase 1 (Plk1), Plk3, the microtubule associated serine/threonine (MAST) kinase family, the serine/threonine kinase 11 (STK11, LKB1), and the casein kinase 1 (CK1) have also been reported to phosphorylate PTEN.

~54 kDa observed

Peptide corresponding to amino acid region encompassing the human, mouse, and rat phospho-PTEN (Ser385).

Concentration: Please refer to lot specific datasheet.