Novel HIF2A mutations disrupt oxygen sensing, leading to polycythemia, paragangliomas, and somatostatinomas Blood, Mar 2013; 121: 2563 - 2566.
[anti-HA]
Regulation of the PI3-K/Akt Survival Pathway in the Rat Endometrium Biol Reprod, Mar 2013; 88: 79.
[Akt3]
RNA elements directing in vivo assembly of the 7SK/MePCE/Larp7 transcriptional regulatory snRNP Nucleic Acids Res., Mar 2013; 10.1093/nar/gkt159.
[LA]
Ruxolitinib as potential targeted therapy for patients with JAK2 rearrangements Haematologica, Mar 2013; 98: 404 - 408.
[JAK2]
A phospho-specific peptide corresponding to residues surrounding Threonine 366 and Serine 370 of human PTEN was used as an immunogen. The antibody only detects PTEN phosphorylated on T366 or S370.
Buffer
Store at -20 C. Buffer: 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA. Stable for 12 months from date of receipt.
PTEN is a protein tyrosine phosphatase that acts as a tumor suppressor, as a lipid phosphatase that dephosphorylates the D3 position of phosphatidylinositol 3,4,5-trisphosphate and as an antagonist of the PI3k/AKT signaling pathway (1-3). PTEN structural domains includes an N-terminal phosphatase domain, a lipid binding C2 domain and a 50-amino acid C-terminal tail that contains a PDZ biding sequence. Phosphorylation of the tail suppresses the activity of PTEN by controlling its recruitment into the PTEN-associated complex (4). PTEN is phosphorylated in vitro on Threonine 366 and Serine 370 by glycogen synthase kindase 3 (GSK3) and casein kinase 2 (CK2) respectively. Prior phosphorylation of PTEN at Serine 370 by CK2 strongly increased its phosphorylation at Threonine 366 by GSK3, suggesting that the two may synergize. Generally, phosphorylation in the C-terminal tail of PTEN is thought to enhance stability and to decrease membrane localization and activity. However, phosphorylation at Threonine 366 is linked to destabilization of PTEN (5).
Related Pathway
Focal Adhesion
Senescence and Autophagy
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