Product: PTEN Antibody
Catalog: AF5447
Source: Rabbit
Application: WB, IHC, ELISA(peptide)
Reactivity: Human, Mouse, Rat
Prediction: Pig, Bovine, Horse, Rabbit, Dog, Chicken, Xenopus
Mol.Wt.: 47 kD, 55 kD; 47kD(Calculated).
Uniprot: P60484
RRID: AB_2837931

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Product Info

WB 1:500-1:2000, IHC 1:50-1:200, ELISA(peptide) 1:20000-1:40000
*The optimal dilutions should be determined by the end user.

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Pig(100%), Bovine(100%), Horse(100%), Rabbit(100%), Dog(100%), Chicken(100%), Xenopus(100%)
PTEN Antibody detects endogenous levels of total PTEN.
Cite Format: Affinity Biosciences Cat# AF5447, RRID:AB_2837931.
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.


10q23del; BZS; DEC; GLM2; MGC11227; MHAM; MMAC1; MMAC1 phosphatase and tensin homolog deleted on chromosome 10; Mutated in multiple advanced cancers 1; Phosphatase and tensin homolog; Phosphatase and tensin like protein; Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN; Pten; PTEN_HUMAN; PTEN1; TEP1;



Expressed at a relatively high level in all adult tissues, including heart, brain, placenta, lung, liver, muscle, kidney and pancreas.

Tumor 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



Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - P60484 As Substrate

Site PTM Type Enzyme
T2 Acetylation
K6 Acetylation
K6 Ubiquitination
K13 Ubiquitination
Y27 Phosphorylation P06213 (INSR)
Y46 Phosphorylation P12931 (SRC)
K66 Ubiquitination
Y68 Phosphorylation P12931 (SRC)
K80 Ubiquitination
S113 Phosphorylation Q13315 (ATM)
K125 Acetylation
K128 Acetylation
Y138 Phosphorylation
Y155 Phosphorylation P12931 (SRC)
K163 Acetylation
K164 Acetylation
Y174 Phosphorylation P12931 (SRC) , P06213 (INSR)
Y176 Phosphorylation
Y177 Phosphorylation
Y178 Phosphorylation
S179 Phosphorylation
Y180 Phosphorylation
K223 Ubiquitination
S227 Phosphorylation
S229 Phosphorylation Q13464 (ROCK1)
T232 Phosphorylation Q13464 (ROCK1)
Y240 Phosphorylation P12931 (SRC) , P21802 (FGFR2) , P07948 (LYN) , P22607 (FGFR3) , P06239 (LCK)
K254 Sumoylation
K266 Sumoylation
K289 Sumoylation
K289 Ubiquitination
S294 Phosphorylation
S302 Phosphorylation
Y315 Phosphorylation P12931 (SRC) , P06239 (LCK)
T319 Phosphorylation
T321 Phosphorylation
K332 Acetylation
Y336 Phosphorylation P42685 (FRK)
S362 Phosphorylation P49841 (GSK3B)
T366 Phosphorylation P49841 (GSK3B) , Q9H4B4 (PLK3)
S370 Phosphorylation P68400 (CSNK2A1) , Q9H4B4 (PLK3)
Y377 Phosphorylation P12931 (SRC)
S380 Phosphorylation Q15831 (STK11) , Q05513 (PRKCZ) , P68400 (CSNK2A1) , P53350 (PLK1)
T382 Phosphorylation Q15831 (STK11) , P68400 (CSNK2A1) , Q05513 (PRKCZ) , P53350 (PLK1)
T383 Phosphorylation P53350 (PLK1) , P68400 (CSNK2A1) , Q05513 (PRKCZ) , Q15831 (STK11)
S385 Phosphorylation Q15831 (STK11) , P68400 (CSNK2A1)
T398 Phosphorylation Q13315 (ATM)
T401 Phosphorylation
K402 Acetylation

Research Backgrounds


Tumor 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. In motile cells, suppresses the formation of lateral pseudopods and thereby promotes cell polarization and directed movement.

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.


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.

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.

Subcellular Location:

Cytoplasm. Nucleus. Nucleus>PML body.
Note: Monoubiquitinated form is nuclear. Nonubiquitinated form is cytoplasmic. Colocalized with PML and USP7 in PML nuclear bodies (PubMed:18716620). XIAP/BIRC4 promotes its nuclear localization (PubMed:19473982).

Note: May be secreted via a classical signal peptide and reenter into cells with the help of a poly-Arg motif.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

Expressed at a relatively high level in all adult tissues, including heart, brain, placenta, lung, liver, muscle, kidney and pancreas.

Subunit Structure:

Monomer. The unphosphorylated form interacts with the second PDZ domain of AIP1 and with DLG1 and MAST2 in vitro. Interacts with MAGI2, MAGI3, MAST1 and MAST3, but neither with MAST4 nor with DLG5; interaction with MAGI2 increases protein stability. Interacts with NEDD4. Interacts with NDFIP1 and NDFIP2; in the presence of NEDD4 or ITCH, this interaction promotes PTEN ubiquitination. Interacts (via C2 domain) with FRK. Interacts with USP7; the interaction is direct. Interacts with ROCK1 (By similarity). Interacts with XIAP/BIRC4. Interacts with STK11; the interaction phosphorylates PTEN. Interacts with PPP1R16B. Interacts with NOP53; regulates PTEN phosphorylation and increases its stability.


The C2 domain binds phospholipid membranes in vitro in a Ca(2+)-independent manner; this binding is important for its tumor suppressor function.

Belongs to the PTEN phosphatase protein family.

Research Fields

· Cellular Processes > Cell growth and death > p53 signaling pathway.   (View pathway)

· Cellular Processes > Transport and catabolism > Autophagy - animal.   (View pathway)

· Cellular Processes > Cell growth and death > Cellular senescence.   (View pathway)

· Cellular Processes > Cellular community - eukaryotes > Focal adhesion.   (View pathway)

· Environmental Information Processing > Signal transduction > FoxO signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > Phosphatidylinositol signaling system.

· Environmental Information Processing > Signal transduction > Sphingolipid signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > mTOR signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > PI3K-Akt signaling pathway.   (View pathway)

· Human Diseases > Drug resistance: Antineoplastic > EGFR tyrosine kinase inhibitor resistance.

· Human Diseases > Endocrine and metabolic diseases > Insulin resistance.

· Human Diseases > Infectious diseases: Viral > Hepatitis B.

· Human Diseases > Infectious diseases: Viral > Human papillomavirus infection.

· Human Diseases > Cancers: Overview > Pathways in cancer.   (View pathway)

· Human Diseases > Cancers: Overview > MicroRNAs in cancer.

· Human Diseases > Cancers: Specific types > Endometrial cancer.   (View pathway)

· Human Diseases > Cancers: Specific types > Glioma.   (View pathway)

· Human Diseases > Cancers: Specific types > Prostate cancer.   (View pathway)

· Human Diseases > Cancers: Specific types > Melanoma.   (View pathway)

· Human Diseases > Cancers: Specific types > Small cell lung cancer.   (View pathway)

· Human Diseases > Cancers: Specific types > Breast cancer.   (View pathway)

· Human Diseases > Cancers: Specific types > Hepatocellular carcinoma.   (View pathway)

· Human Diseases > Cancers: Overview > Central carbon metabolism in cancer.   (View pathway)

· Metabolism > Carbohydrate metabolism > Inositol phosphate metabolism.


1). Wang K et al. PTBP1 knockdown promotes neural differentiation of glioblastoma cells through UNC5B receptor. Theranostics 2022 May 9;12(8):3847-3861. (PubMed: 35664063) [IF=11.600]

2). Wen X et al. MiR-455-3p reduces apoptosis and alleviates degeneration of chondrocyte through regulating PI3K/AKT pathway. Life Sci 2020 Apr 25:117718 (PubMed: 32343998) [IF=6.780]

Application: IHC    Species: Mice    Sample:

Fig. 2. Different gene expression profile between healthy cartilage and OA cartilage. A–D: miR-455-3p, PTEN, COL2A1, and MMP13 expression in healthy and OA cartilage by qRT-PCR, *P < 0.05, **P < 0.01, ***P < 0.001. E–F: Immunohistochemical results of Alcian, COL2A1, MMP13, PTEN, and pAKT in healthy and OA cartilage. (Scale: 400 μm).

Application:    Species: Mice    Sample:

Fig. 3. IL-1β/TNF-α down-regulates miR-455-3p and miR-455-3p inhibits the expression of PTEN. A: qPCR analyzing chondrocytes treated with IL-1β/TNF-α: IL-1β/TNF-α results in down-regulation of miR-455-3p and up-regulation of PTEN. B: The western blotting results of healthy cartilage and IL-1β treated cartilage. C–D: qRT-PCR analyzing overexpressing or inhibiting miR-455-3p: miR-455-3p inhibits PTEN and regulates related mRNA. E: western blotting analyzing the changes of related protein after transfecting mimic/inhibitor. *P < 0.05, **P < 0.01, ***P < 0.001.

3). Li Y et al. circIQCH sponges miR-145 to promote breast cancer progression by upregulating DNMT3A expression. Aging (Albany NY) 2020 Aug 3;12(15):15532-15545. (PubMed: 32756009) [IF=5.955]

Application: WB    Species: Mouse    Sample: tumor

Figure 5 circIQCH promotes breast cancer progression via circIQCH-miR-145-DNMT3A axis. (A) Predicted binding sites of miR-145 within the 3’-UTR of DNMT3A mRNA according to TargetScan. (B) The relative expression level of DNMT3A in breast cancer cell lines. (C) Luciferase reporter assay of SKBR3 and BT474 cells co-transfected with miR-145 mimics and the 3’-UTR of DNMT3A wild type or mutant luciferase reporter. The putative miRNA binding site of 3’-UTR of DNMT3A was mutated. (D) Expression of DNMT3A was decreased after transfection with miR-145 mimics. Expression of DNMT3A was increased after transfection with miR-145 inhibitors. (E) Enrichment of circIQCH, DNMT3A and miR-145 on Ago2 assessed by RIP assay. (F) Enrichment of Ago2 to circIQCH was decreased while DNMT3A was increased after knockdown of circIQCH. (G) Knockdown of circIQCH resulted in the reduction of DNMT3A expression which was reversed by miR-145 inhibitors. PTEN and BRCA1 was upregulated after silencing circIQCH. (H) Cell proliferation rate was detected by CCK-8 assay after exogenously expressing DNMT3A or inhibiting miR-145 in circIQCH silencing SKBR3 and BT474 cells. (I) Cell migration ability was validated by transwell assay after exogenously expressing DNMT3A or inhibiting miR-145 in circIQCH silencing SKBR3 cells. *P<0.05; **P<0.01.

4). Li H et al. MicroRNA-181a regulates epithelial-mesenchymal transition by targeting PTEN in drug-resistant lung adenocarcinoma cells. Int J Oncol 2015 Oct;47(4):1379-92 (PubMed: 26323677) [IF=5.884]

Application: WB    Species: human    Sample: A549 cells

Figure 3. A549/DDP and A549/PTX cells showed molecular and morphological changes that were consistent with EMT. (A) microscopy at x200 magnification was used to assess cell morphology. The A549 cells (parental cells) had an epithelioid, rounded cobblestone appearance and there was limited formation of pseudopodia. A549/PTX and A549/DDP cells exhibited a spindle-shaped morphology and an increased formation of pseudopodia, indicating a loss of cell polarity. (B) E-cadherin, β-catenin, vimentin, MMP-2 and MMP-9 which are EMT-related proteins, were assessed in terms of expression levels. EMT-related transcription factors (Snail, Slug, Twist and ZEB1) were measured in A549/PTX and A549/DDP cells using western blot analysis. (C) The expression changes were confirmed at the mRNA level by qRT-PCR. Expression was standardized to the expression of GAPDH and normalized to 1.0 in the parental cells (compared with the parental A549 cells, means ± SEM, n=3, * P<0.05)

Application: WB    Species: human    Sample: lung adenocarcinoma cell

Figure 9.| miR-181a directly targets PTEN by binding to its 3'UTR. (A) The predicted miR-181a binding site within PTEN 3'UTR and its mutant version resulting from site mutagenesis are presented. Red indicates the nucleotides that were mutated to create a mismatch. (B) PTEN expression in lung adenocarcinoma cell lines was assessed by western blotting.

5). Li X et al. Notch1 contributes to TNF-α-induced proliferation and migration of airway smooth muscle cells through regulation of the Hes1/PTEN axis. Int Immunopharmacol 2020 Aug 29;88:106911. (PubMed: 32871474) [IF=5.714]

Application: WB    Species: mouse    Sample: ASM cells

Fig. 5.| Notch1 knockdown decreased Hes1 and increased PTEN expression in TNF-α-induced ASM cells. ASM cells were transfected with NC or Notch1 siRNA for 48 h and then stimulated with TNF-α for 24 h. (F, G) Protein expression of PTEN was measured by western blot. N = 3, **p < 0.01.

6). Liu D et al. MiR‐19b‐3p accelerates bone loss after spinal cord injury by suppressing osteogenesis via regulating PTEN/Akt/mTOR signalling. J Cell Mol Med 2020 Dec 17. (PubMed: 33332749) [IF=5.295]

Application: WB    Species: rat    Sample: BMSCs

FIGURE 3|MiR-19b-3p overexpression suppressed autophagy via binging to PTEN. (A) Dual-Luciferase reporter assay was conducted to verify the targeted relationship between miR-19b-3p and 3’-UTR of PTEN in HEK293T cells. Western blot for (B) PTEN, (C) p-Akt, (D)p-mTOR, (E) LC3II/I, (F) p62 and (G) Beclin-1 in BMSC-derived osteoblasts after transduction.

7). Zheng Y et al. HDAC6, modulated by miR-206, promotes endometrial cancer progression through the PTEN/AKT/mTOR pathway. Sci Rep 2020 Feb 27;10(1):3576 (PubMed: 32107418) [IF=4.996]

Application: WB    Species: Human    Sample: EC cells

Figure 6 Pathways modulated by HDAC6 in EC cells. (A) Western blotting showed the levels of differentially expressed proteins in Ishikawa cells following transfection with generated lentiviruses. (B) Putative working model depicting the role of miR-206/HDAC6 in EC progression. *P < 0.05, **P < 0.01, ***P < 0.001.

8). Cheng Y et al. Low Long Noncoding RNA Growth Arrest-Specific Transcript 5 Expression in the Exosomes of Lung Cancer Cells Promotes Tumor Angiogenesis. J Oncol 2019 May 2;2019:2476175 (PubMed: 31186629) [IF=4.501]

9). Ye Y et al. Anticancer Effect of Puerarin on Ovarian Cancer Progression Contributes to the Tumor Suppressor Gene Expression and Gut Microbiota Modulation. J Immunol Res 2022 Jul 28;2022:4472509. (PubMed: 35935578) [IF=4.493]

10). Niu Y et al. miR-183-5p Promotes HCC Migration/Invasion via Increasing Aerobic Glycolysis. Onco Targets Ther 2021 Jun 4;14:3649-3658. (PubMed: 34113130) [IF=4.345]

Application: WB    Species: human    Sample: HepG2 cells

Figure 5 |PTEN is a potential target gene of miR-183-5p.Notes: (A and B) mRNA levels of PTEN in HepG2 cells, as suggested by qPCR. (C–F) Protein levels of PTEN in HepG2 cells, as suggested by Western blot analysis. n=3,Student’s t-test. ****P<0.0001, ***P<0.001, *P<0.05.

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