PTEN Antibody (YA5512)

Cat. No.: HY-P85820: Data Sheet User Guide for Antibodies
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PTEN Antibody (YA5512) is a Mouse-derived and non-conjugated IgG monoclonal antibody, targeting to PTEN.

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사이즈	재고	수량
20 μL	견적 받기 2 - 3 weeks 1 - 2 Weeks 3 - 4 weeks 2 - 3 weeks	Estimated Time of Arrival: December 31
50 μL	견적 받기 2 - 3 weeks 1 - 2 Weeks 3 - 4 weeks 2 - 3 weeks	Estimated Time of Arrival: December 31
100 μL	견적 받기 2 - 3 weeks 1 - 2 Weeks 3 - 4 weeks 2 - 3 weeks	Estimated Time of Arrival: December 31
250 μL	견적 받기

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WB: Western Blot;
IHC-P: Immunohistochemistry-Paraffin;
IHC-F: Immunohistochemistry-Frozen;
ICC/IF: Immunocytochemistry/Immunofluorescence;
IF-Tissue: Immunofluorescence-Tissue;
mIHC: Multiplex Immunohistochemical;
IP: Immunoprecipitation;
ChIP: Chromatin Immunoprecipitation;
FC: Flow Cytometry;
ELISA: Enzyme Linked Immunosorbent Assay

Product Detail
Background
제품 설명
References

제품 설명

PTEN Antibody (YA5512) is a Mouse-derived and non-conjugated IgG monoclonal antibody, targeting to PTEN.

Host

Mouse

Clonality

Monoclonal

분자량

Predicted band size: 47 kDa;

Observed band size: 47 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.

Species Reactivity

Human

SwissProt ID

P60484

Gene ID

5728 [NCBI]

Immunogen

Synthesized peptide derived from human PTEN AA range: 300-403

Application &
Dilution Ratio

Application	Dilution Ratio
IHC-P IHC-P: Immunohistochemistry-Paraffin	1:200-1000
WB WB: Western Blot	1:500-2000
ICC/IF ICC/IF: Immunocytochemistry/Immunofluorescence	1:100-500
ELISA ELISA: Enzyme Linked Immunosorbent Assay	1:1000-5000

Purity	Protein G	Conjugation	Non-conjugated
Modification	Unmodified	Isotype	IgG

Appearance

Liquid

Formulation

Supplied in PBS, 50% glycerol, 0.05% Proclin 300, 0.05%BSA

Storage & Stability

Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.

선적

Shipping with blue ice.

Background

Function：Dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins (PubMed:9187108, PubMed:9256433, PubMed:9616126). 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 (PubMed:16824732, PubMed:26504226, PubMed:9593664, PubMed:9811831). 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 (PubMed:11418101, PubMed:15979280). Antagonizes the PI3K-AKT/PKB signaling pathway by dephosphorylating phosphoinositides and thereby modulating cell cycle progression and cell survival (PubMed:31492966, PubMed:37279284). The unphosphorylated form cooperates with MAGI2 to suppress AKT1 activation (PubMed:11707428). In motile cells, suppresses the formation of lateral pseudopods and thereby promotes cell polarization and directed movement (PubMed:22279049). Dephosphorylates tyrosine-phosphorylated focal adhesion kinase and inhibits cell migration and integrin-mediated cell spreading and focal adhesion formation (PubMed:22279049). 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 (PubMed:26166433). 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 (PubMed:26166433). 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 (PubMed:10468583, PubMed:18716620); Functional kinase, like isoform 1 it antagonizes the PI3K-AKT/PKB signaling pathway. Plays a role in mitochondrial energetic metabolism by promoting COX activity and ATP production, via collaboration with isoform 1 in increasing protein levels of PINK1

Subcellular Localization：Cytoplasm; Nucleus; Nucleus, PML body; Cell projection, dendritic spine; Postsynaptic density; Secreted

Expression：
Tissue_specificity:It is expressed at high levels in all adult tissues, including the heart, brain, placenta, lungs, liver, muscles, kidneys, and pancreas.

Induction:Down-regulated by TGFB1

Isoforms & Post-Translational Modification：P60484 has 3 isomers: P60484-1: 47166 Da (predicted); P60484-2: 64882 Da (predicted); P60484-3: 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 (PubMed:26166433);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 compartmentalization. Ubiquitinated by XIAP/BIRC4;Ubiquitinated by the DCX(DCAF13) E3 ubiquitin ligase complex, leading to its degradation;ISGylated. ISGylation promotes PTEN degradation

Subunit：Monomer. The unphosphorylated form interacts with the second PDZ domain of MAGI2 and with DLG1 and MAST2 in vitro (PubMed:10646847, PubMed:10760291, PubMed:11707428). Interacts with MAGI2, MAGI3, MAST1 and MAST3, but neither with MAST4 nor with DLG5; interaction with MAGI2 increases protein stability (PubMed:10748157, PubMed:15951562). Interacts with NEDD4 (PubMed:17218260). Interacts with NDFIP1 and NDFIP2; in the presence of NEDD4 or ITCH, this interaction promotes PTEN ubiquitination (PubMed:20534535, PubMed:25801959). Interacts (via C2 domain) with FRK (PubMed:19345329). Interacts with USP7; the interaction is direct (PubMed:18716620). Interacts with ROCK1 (By similarity). Interacts with XIAP/BIRC4 (PubMed:19473982). Interacts with STK11; the interaction phosphorylates PTEN (PubMed:15987703). Interacts with PPP1R16B (PubMed:25007873). Interacts with NOP53; regulates PTEN phosphorylation and increases its stability (PubMed:15355975). Interacts (via PDZ domain-binding motif) with DLG4; the interaction is induced by NMDA and is required for PTEN location at postsynaptic density (By similarity). Interacts with the regulatory p85 subunit of the PI3K kinase complex and with Rho GTPase-activating protein DLC1; in resting cells, interacts (via C2 tensin-type domain) with p85 but, following growth factor stimulation, PTEN is phosphorylated which leads to weakened interaction with p85 and enhanced interaction (via C2 tensin-type domain) with DLC1 while p85 interaction with TNS3 increases (PubMed:26166433)

각종 서류

User Guide for Antibodies (1077 KB)

References

[1]. /biology-dictionary/ramos-cell.html [Content Brief]