Overview

  • Product nameAnti-PTEN antibodySee all PTEN primary antibodies ...
  • Description
    Sheep polyclonal to PTEN
  • Tested applicationsWB more details
  • Species reactivity
    Reacts with: Human
  • Immunogen

    Fusion protein, corresponding to amino acids 188-403 of Human PTEN.

Properties

Applications

Our Abpromise guarantee covers the use of ab16125 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

Application Notes
WB Use at an assay dependent dilution. Predicted molecular weight: 47 kDa.

Target

  • FunctionTumor suppressor. Acts as a dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins. Also acts as a lipid phosphatase, removing 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 with order of substrate preference in vitro PtdIns(3,4,5)P3 > PtdIns(3,4)P2 > PtdIns3P > Ins(1,3,4,5)P4. The lipid phosphatase activity is critical for its tumor suppressor function. Antagonizes the PI3K-AKT/PKB signaling pathway by dephosphorylating phosphoinositides and thereby modulating cell cycle progression and cell survival. The unphosphorylated form cooperates with AIP1 to suppress AKT1 activation. Dephosphorylates tyrosine-phosphorylated focal adhesion kinase and inhibits cell migration and integrin-mediated cell spreading and focal adhesion formation. Plays a role as a key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. May be 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 induces less tumor suppressive ability.
  • Tissue specificityExpressed at a relatively high level in all adult tissues, including heart, brain, placenta, lung, liver, muscle, kidney and pancreas.
  • Involvement in diseaseDefects in PTEN are a cause of Cowden disease (CD) [MIM:158350]; also known as Cowden syndrome (CS). CD is an autosomal dominant cancer predisposition syndrome associated with elevated risk for tumors of the breast, thyroid and skin. The predominant phenotype for CD is multiple hamartoma syndrome, in many organ systems including the breast (70% of CD patients), thyroid (40-60%), skin, CNS (40%), gastrointestinal tract. Affected individuals are at an increased risk of both breast and thyroid cancers. Trichilemmomas (benign tumors of the hair follicle infundibulum), and mucocutaneous papillomatosis (99%) are hallmarks of CD.
    Defects in PTEN are the cause of Lhermitte-Duclos disease (LDD) [MIM:158350]; also known as cerebelloparenchymal disorder VI. LDD is characterized by dysplastic gangliocytoma of the cerebellum which often results in cerebellar signs and seizures. LDD and CD seem to be the same entity, and are considered as hamartoma-neoplasia syndromes.
    Defects in PTEN are a cause of Bannayan-Zonana syndrome (BZS) [MIM:153480]; also known as Ruvalcaba-Myhre-Smith syndrome (RMSS) or Bannayan-Riley-Ruvalcaba syndrome (BRRS). In BZS there seems not to be an increased risk of malignancy. It has a partial clinical overlap with CD. BZS is characterized by the classic triad of macrocephaly, lipomatosis and pigmented macules of the gland penis.
    Defects in PTEN are a cause of head and neck squamous cell carcinomas (HNSCC) [MIM:275355]; also known as squamous cell carcinoma of the head and neck.
    Defects in PTEN are a cause of susceptibility to endometrial cancer [MIM:608089].
    Note=PTEN mutations are found in a subset of patients with Proteus syndrome, a genetically heterogeneous condition. The molecular diagnosis of PTEN mutation positive cases classifies Proteus syndrome patients as part of the PTEN hamartoma syndrome spectrum. As such, patients surviving the early years of Proteus syndrome are likely at a greater risk of developing malignancies.
    Defects in PTEN are a cause of susceptibility to glioma type 2 (GLM2) [MIM:613028]. Gliomas are central nervous system neoplasms derived from glial cells and comprise astrocytomas, glioblastoma multiforme, oligodendrogliomas, and ependymomas.
    Defects in PTEN are a cause of VACTERL association with hydrocephalus (VACTERL-H) [MIM:276950]. VACTERL is an acronym for vertebral anomalies, anal atresia, congenital cardiac disease, tracheoesophageal fistula, renal anomalies, radial dysplasia, and other limb defects.
    Defects in PTEN may be a cause of susceptibility to prostate cancer (PC) [MIM:176807]. It is a malignancy originating in tissues of the prostate. Most prostate cancers are adenocarcinomas that develop in the acini of the prostatic ducts. Other rare histopathologic types of prostate cancer that occur in approximately 5% of patients include small cell carcinoma, mucinous carcinoma, prostatic ductal carcinoma, transitional cell carcinoma, squamous cell carcinoma, basal cell carcinoma, adenoid cystic carcinoma (basaloid), signet-ring cell carcinoma and neuroendocrine carcinoma.
    Defects in PTEN are a cause of macrocephaly/autism syndrome (MCEPHAS) [MIM:605309]. Patients have autism spectrum disorders and macrocephaly, with head circumferences ranging from +2.5 to +8 SD for age and sex (average head circumference +4.0 SD).
    Note=A microdeletion of chromosome 10q23 involving BMPR1A and PTEN is a cause of chromosome 10q23 deletion syndrome, which shows overlapping features of the following three disorders: Bannayan-Zonana syndrome, Cowden disease and juvenile polyposis syndrome.
  • Sequence similaritiesContains 1 C2 tensin-type domain.
    Contains 1 phosphatase tensin-type domain.
  • DomainThe C2 domain binds phospholipid membranes in vitro in a Ca(2+)-independent manner; this binding is important for its tumor suppressor function.
  • Post-translational
    modifications
    Phosphorylated in vitro by MAST1, MAST2 and MAST3. Phosphorylation results in an inhibited activity towards PIP3. Phosphorylation can both inhibit or promote PDZ-binding. Phosphorylation at Tyr-336 by FRK/PTK5 protects this protein from ubiquitin-mediated degradation probably by inhibiting its binding to NEDD4.
    Monoubiquitinated; monoubiquitination is increased in presence of retinoic acid. Deubiquitinated by USP7; leading to its nuclear exclusion. Monoubiquitination of one of either Lys-13 and Lys-289 amino acid is sufficient to modulate PTEN comportmentalization.
  • Cellular localizationCytoplasm. Nucleus. Nucleus > PML body. Monoubiquitinated form is nuclear. Nonubiquitinated form is cytoplasmic. Colocalized with PML and USP7 in PML nuclear bodies.
  • Target information above from: UniProt accession P60484 The UniProt Consortium
    The Universal Protein Resource (UniProt) in 2010
    Nucleic Acids Res. 38:D142-D148 (2010) .

    Information by UniProt
  • Database links
  • Alternative names
    • 10q23del antibody
    • Bannayan Zonana syndrome antibody
    • BZS antibody
    • DEC antibody
    • GLM2 antibody
    • ITGA 2 antibody
    • MGC11227 antibody
    • MHAM antibody
    • MMAC 1 antibody
    • MMAC1 antibody
    • MMAC1 phosphatase and tensin homolog deleted on chromosome 10 antibody
    • Multiple hamartoma (Cowden syndrome) antibody
    • Mutated in multiple advanced cancers 1 antibody
    • Mutated in Mutiple Advanced Cancers 1 antibody
    • Phosphatase and Tensin Homolog antibody
    • Phosphatase and tensin like protein antibody
    • Phosphatidylinositol 345 trisphosphate 3 phosphatase and dual specificity protein phosphatase PTEN antibody
    • Phosphatidylinositol 345 trisphosphate 3 phosphatase antibody
    • Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN antibody
    • Platelet antigen BR antibody
    • PTEN 1 antibody
    • Pten antibody
    • PTEN_HUMAN antibody
    • PTEN1 antibody
    • Tensin homolog antibody
    • TEP 1 antibody
    • TEP1 antibody
    • VLA 2 Receptor Alpha Subunit antibody
    see all

Anti-PTEN antibody images



  • Predicted band size : 47 kDa


    ab16125 used at 20ug/ml in Western blot analysis of PTEN in various cell lines: Lane 1: ANA3CA (truncating mutations of PTEN). Lane 2: Hec 1A (wild-type PTEN). Lane 3: KLE (wild-type PTEN). Lane 4: MDA ((truncating mutations of PTEN). Lane 5: RL-95 (truncating mutations of PTEN). Lane 6: 293T (wild-type PTEN, low levels). Lane 7: 292T cells transfected with FLAG PTEN. Lane 8: Negative control.

References for Anti-PTEN antibody (ab16125)

ab16125 has not yet been referenced specifically in any publications.

Product Wall

Unfortunately, we do not have any more specific information regarding the Western blot image shown on the datasheet. This product was produced in collaboration with a researcher who did the testing for us and they did not provide any more information t...

Read More

Thank you for your recent phone call regarding our PTEN antibodies. After n extensive search on each datasheet I was unfortunately unable to find an antibody which would match your needs, I am still waiting to hear more information regarding ab13590....

Read More

Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"