PTEN Antibody (YA119)(PBS only)
(Synonyms: MMAC1, TEP1, PTEN, Inositol polyphosphate 3-phosphatase, Mutated in multiple advanced cancers 1, Phosphatase and tensin homolog)PTEN Antibody (YA119) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to PTEN.
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Host:
Rabbit
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Isotype:
IgG
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Application:
WB, ICC/IF, IHC-P
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Reactivity :
Human, Mouse
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Formulation:
Supplied in PBS (pH7.4)..
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Conjugation:
Non-conjugated
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
Applications
| Application |
WB
WB: Western Blot
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ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
IHC-P
IHC-P: Immunohistochemistry-Paraffin
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|---|---|---|---|
| Dilution Ratio | 1:500-1:5000 | 1:100-1:500 | 1:50-1:200 |
Product Details
PTEN Antibody (YA119) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to PTEN.
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Host Rabbit
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Clonality Recombinant,Monoclonal
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Species ReactivityHuman, Mouse
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Observed Molecular WeightObserved band size: 55 kDa
Note: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 47 kDa
Synthetic peptide corresponding to Human PTEN.AA range:full length.
Endogenous
Protein A affinity purified.
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS (pH7.4)..
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
PTEN is a Dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins. Also functions as a lipid phosphatase, removing the phosphate in the D3 position of the inositol ring of PtdIns(3,4,5)P3/phosphatidylinositol 3,4,5-trisphosphate, PtdIns(3,4)P2/phosphatidylinositol 3,4-diphosphate and PtdIns3P/phosphatidylinositol 3-phosphate with a preference for PtdIns(3,4,5)P3. Furthermore, this enzyme can also act as a cytosolic inositol 3-phosphatase acting on Ins(1,3,4,5,6)P5/inositol 1,3,4,5,6 pentakisphosphate and possibly Ins(1,3,4,5)P4/1D-myo-inositol 1,3,4,5-tetrakisphosphate. Antagonizes the PI3K-AKT/PKB signaling pathway by dephosphorylating phosphoinositides and thereby modulating cell cycle progression and cell survival. The unphosphorylated form cooperates with MAGI2 to suppress AKT1 activation. In motile cells, suppresses the formation of lateral pseudopods and thereby promotes cell polarization and directed movement. Dephosphorylates tyrosine-phosphorylated focal adhesion kinase and inhibits cell migration and integrin-mediated cell spreading and focal adhesion formation. Required for growth factor-induced epithelial cell migration; growth factor stimulation induces PTEN phosphorylation which changes its binding preference from the p85 regulatory subunit of the PI3K kinase complex to DLC1 and results in translocation of the PTEN-DLC1 complex to the posterior of migrating cells to promote RHOA activation. Meanwhile, TNS3 switches binding preference from DLC1 to p85 and the TNS3-p85 complex translocates to the leading edge of migrating cells to activate RAC1 activation. 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 (By similarity). Involved in the regulation of synaptic function in excitatory hippocampal synapses. Recruited to the postsynaptic membrane upon NMDA receptor activation, is required for the modulation of synaptic activity during plasticity. Enhancement of lipid phosphatase activity is able to drive depression of AMPA receptor-mediated synaptic responses, activity required for NMDA receptor-dependent long-term depression (LTD) (By similarity). 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[1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16].
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Subcellular Localization
Cytoplasm; Nucleus; Nucleus, PML body; Cell projection, dendritic spine; Postsynaptic density
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Expression
Tissue_Specificity: Expressed at a relatively high level in all adult tissues, including heart, brain, placenta, lung, liver, muscle, kidney and pancreas.
Induction: Down-regulated by TGFB1. -
Isoforms & Post-Translational Modification
PTEN has 3 isoforms, P60484-1: amino acid length is 403, molecular weight is 47166 Da (predicted); P60484-2: amino acid length is 576, molecular weight is 64898 Da (predicted); P60484-3: amino acid length is 175, molecular weight is 19796 Da (predicted).
Constitutively phosphorylated by CK2 under normal conditions. Phosphorylated in vitro by MAST1, MAST2, MAST3 and STK11. 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. Phosphorylation by ROCK1 is essential for its stability and activity. Phosphorylation by PLK3 promotes its stability and prevents its degradation by the proteasome. Phosphorylated on Thr-319 and Thr-321 in the C2-type tensin domain following EGF stimulation which changes its binding preference from the p85 regulatory subunit of the PI3K kinase complex to DLC1. -
Subunit
Monomer.
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SwissProt ID
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Synonyms
MMAC1, TEP1, PTEN, Inositol polyphosphate 3-phosphatase, Mutated in multiple advanced cancers 1, Phosphatase and tensin homolog
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Research Field
Cell Biology
Documentation
References
[1]. Li DM, et al. TEP1, encoded by a candidate tumor suppressor locus, is a novel protein tyrosine phosphatase regulated by transforming growth factor beta. Cancer Res. 1997 Jun 1;57(11):2124-9. [Content Brief]
[2]. Myers MP, et al. P-TEN, the tumor suppressor from human chromosome 10q23, is a dual-specificity phosphatase. Proc Natl Acad Sci U S A. 1997 Aug 19;94(17):9052-7. [Content Brief]
[3]. Tamura M, et al. Inhibition of cell migration, spreading, and focal adhesions by tumor suppressor PTEN. Science. 1998 Jun 5;280(5369):1614-7. [Content Brief]
[4]. Vandeput F, et al. The influence of anionic lipids on SHIP2 phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase activity. Cell Signal. 2006 Dec;18(12):2193-9. [Content Brief]
[5]. Costa HA, et al. Discovery and functional characterization of a neomorphic PTEN mutation. Proc Natl Acad Sci U S A. 2015 Nov 10;112(45):13976-81. [Content Brief]
[6]. Maehama T, et al. The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate. J Biol Chem. 1998 May 29;273(22):13375-8. [Content Brief]
[7]. Myers MP, et al. The lipid phosphatase activity of PTEN is critical for its tumor supressor function. Proc Natl Acad Sci U S A. 1998 Nov 10;95(23):13513-8. [Content Brief]
[8]. Caffrey JJ, et al. Expanding coincident signaling by PTEN through its inositol 1,3,4,5,6-pentakisphosphate 3-phosphatase activity. FEBS Lett. 2001 Jun 15;499(1-2):6-10. [Content Brief]
[9]. Deleu S, et al. Physiological levels of PTEN control the size of the cellular Ins(1,3,4,5,6)P(5) pool. Cell Signal. 2006 Apr;18(4):488-98. [Content Brief]
[10]. Zhang J, et al. The CRL4-DCAF13 ubiquitin E3 ligase supports oocyte meiotic resumption by targeting PTEN degradation. Cell Mol Life Sci. 2020 Jun;77(11):2181-2197. [Content Brief]
[11]. Du X, et al. The E3 ligase HERC5 promotes antimycobacterial responses in macrophages by ISGylating the phosphatase PTEN. Sci Signal. 2023 Jun 6;16(788):eabm1756. [Content Brief]
[12]. Vazquez F, et al. Phosphorylation of the PTEN tail acts as an inhibitory switch by preventing its recruitment into a protein complex. J Biol Chem. 2001 Dec 28;276(52):48627-30. [Content Brief]
[13]. Stöhr N, et al. IGF2BP1 promotes cell migration by regulating MK5 and PTEN signaling. Genes Dev. 2012 Jan 15;26(2):176-89. [Content Brief]
[14]. Cao X, et al. A phosphorylation switch controls the spatiotemporal activation of Rho GTPases in directional cell migration. Nat Commun. 2015 Jul 13;6:7721. [Content Brief]
[15]. Georgescu MM, et al. The tumor-suppressor activity of PTEN is regulated by its carboxyl-terminal region. Proc Natl Acad Sci U S A. 1999 Aug 31;96(18):10182-7. [Content Brief]
[16]. Song MS, et al. The deubiquitinylation and localization of PTEN are regulated by a HAUSP-PML network. Nature. 2008 Oct 9;455(7214):813-7. [Content Brief]
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