anti-PTEN (human), Rabbit Monoclonal (RM265)

RevMAb Biosciences

anti-PTEN (human), Rabbit Monoclonal (RM265)

10

Western Blot, ImmunoHistoChemistry

Research Use Only

Monoclonal

RM265

PTEN

phosphatase and tensin homolog

10q23del; BZS; CWS1; DEC; GLM2; MHAM; mitochondrial phosphatase and tensin protein alpha; mitochondrial PTENalpha; MMAC1; MMAC1 phosphatase and tensin homolog deleted on chromosome 10; mutated in multiple advanced cancers 1; phosphatase and tensin-like protein; phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN; phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN; protein tyrosine phosphatase; PTEN variant PTEN-K267Rfs*9; PTEN variant PTEN-L247*; PTEN variant PTEN-R234Afs*11; PTEN1; PTENbeta; PTENepsilon; TEP1

Rabbit

IgG

Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN

PTEN (phosphatase and tensin homologue deleted on chromosome ten) is a tumor suppressor implicated in a wide variety of human cancers. PTEN encodes a 403 amino acid polypeptide and contains a tensin like domain as well as a catalytic domain similar to that of the dual specificity protein tyrosine phosphatases. PTEN preferentially dephosphorylates phosphoinositide substrates. PTEN negatively regulates intracellular levels of phosphatidylinositol-3, 4, 5-trisphosphate in cells and functions as a tumor suppressor by negatively regulating PI3K/Akt signaling pathway. PTEN possesses a carboxy-terminal, noncatalytic regulatory domain with three phosphorylation sites (Ser380, Thr382, and Thr383) that regulate PTEN stability and may affect its biological activity. PTEN regulates p53 protein levels and activity and is involved in G protein-coupled signaling during chemotaxis. PTEN plays a role as a key modulator in neurogenesis, including correct neuron positioning, dendritic development and synapse formation and it may be also a negative regulator of insulin signaling and glucose metabolism in adipose tissue. The nuclear monoubiquitinated form possesses greater apoptotic potential, whereas the cytoplasmic nonubiquitinated form of PTEN induces less tumor suppressive ability. - Recombinant Antibody. This antibody reacts to human Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and has dual-specificity to protein phosphatase PTEN. This antibody may also react to mouse PTEN, as predicted by immunogen homology. Applications: WB, IHC. Source: Rabbit. Liquid. 50% Glycerol/PBS with 1% BSA and 0.09% sodium azide. PTEN (phosphatase and tensin homologue deleted on chromosome ten) is a tumor suppressor implicated in a wide variety of human cancers. PTEN encodes a 403 amino acid polypeptide and contains a tensin like domain as well as a catalytic domain similar to that of the dual specificity protein tyrosine phosphatases. PTEN preferentially dephosphorylates phosphoinositide substrates. PTEN negatively regulates intracellular levels of phosphatidylinositol-3, 4, 5-trisphosphate in cells and functions as a tumor suppressor by negatively regulating PI3K/Akt signaling pathway. PTEN possesses a carboxy-terminal, noncatalytic regulatory domain with three phosphorylation sites (Ser380, Thr382, and Thr383) that regulate PTEN stability and may affect its biological activity. PTEN regulates p53 protein levels and activity and is involved in G protein-coupled signaling during chemotaxis. PTEN plays a role as a key modulator in neurogenesis, including correct neuron positioning, dendritic development and synapse formation and it may be also a negative regulator of insulin signaling and glucose metabolism in adipose tissue. The nuclear monoubiquitinated form possesses greater apoptotic potential, whereas the cytoplasmic nonubiquitinated form of PTEN induces less tumor suppressive ability.

-20°C

12352203