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R&D Systems anti prl 3
Anti Prl 3, supplied by R&D Systems, used in various techniques. Bioz Stars score: 92/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/anti+prl+3/Human%2FMouse%2FRat+PRL-3+Antibody/bio_rxiv__2025__05__14__654016-118-41-42
Average 92 stars, based on 7 article reviews

anti prl 3 - by Bioz Stars, 2026-10

92/100 stars

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Article Title: Phosphatase activity is dispensable for PRL-3-mediated oncogenesis and tumor progression
Article Snippet: Proteins were transferred to PVDF membranes (Bio-Rad, 1620255) using a Trans-Blot® TurboTM system (Bio-Rad, 1704150EDU)( RRID:SCR_023156). .. Blots were blocked with 5% milk in 0.1% TBST (RPI, T32020) for one hour and incubated overnight at 4 °C with primary antibodies: anti-DYKDDDDK (Flag-Tag epitope) (Proteintech, 20543-1-AP; 1:10,000) (RRID:AB_11232216), anti-CNNM3 (Proteintech, 13976-1-AP; 1:1000) (RRID:AB_2082153), anti-α-tubulin (Proteintech, 66031-1-Ig; 1:10,000) (RRID:AB_11042766), or anti-PRL-3 (R&D Systems, MAB3219; 1:1000) (RRID:AB_2174662). .. After TBST washes, blots were incubated with HRP-conjugated secondary antibodies (anti-mouse IgG, Cell Signaling, 7076P2; anti-rabbit IgG, GE Healthcare, NA9340V) (RRID:AB_330924 and RRID:AB_772191) at 1:2000 in 5% milk for one hour.

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( A ) Expression of PTP4A3 was assessed in OVCAR 3, OVCAR 4 and Kuramochi cells by Western immunoblot and ( B ) this was quantified by densitometry, with PTP4A3 normalised to β-actin. ( C ) NCBI GEO repository RNA-seq data was analysed for gene expression in the three HGSOC cell lines, normalised to Kuramochi levels. ( D ) Cell lysates were analysed for phosphorylation of AKT/PKB (pSer473) and ERK1-2 (pThr202- Tyr204). Antibodies that recognise total AKT/PKB and ERK1-2 were used as controls. Expression of PTP4A3 is shown for comparison. ( E ) Turnover of PTP4A3 was analysed by incubating with or without either MG132 (2.5 µM, 2 h) or BafA1 (100 nM, 1 h) before lysates were collected with β-actin as loading control. Results are representative of at least three independent experiments. Error bars = ± S.E.M. **** p< 0.0001 by unpaired t -test.

Journal: bioRxiv

Article Title: Targeting of PTP4A3 overexpression sensitises HGSOC cells towards chemotherapeutic drugs

doi: 10.1101/2024.10.28.620719

Figure Lengend Snippet: ( A ) Expression of PTP4A3 was assessed in OVCAR 3, OVCAR 4 and Kuramochi cells by Western immunoblot and ( B ) this was quantified by densitometry, with PTP4A3 normalised to β-actin. ( C ) NCBI GEO repository RNA-seq data was analysed for gene expression in the three HGSOC cell lines, normalised to Kuramochi levels. ( D ) Cell lysates were analysed for phosphorylation of AKT/PKB (pSer473) and ERK1-2 (pThr202- Tyr204). Antibodies that recognise total AKT/PKB and ERK1-2 were used as controls. Expression of PTP4A3 is shown for comparison. ( E ) Turnover of PTP4A3 was analysed by incubating with or without either MG132 (2.5 µM, 2 h) or BafA1 (100 nM, 1 h) before lysates were collected with β-actin as loading control. Results are representative of at least three independent experiments. Error bars = ± S.E.M. **** p< 0.0001 by unpaired t -test.

Article Snippet: Membranes were incubated overnight at 4 °C on a rocker with the following antibodies in Blocking buffer: β-actin (Sigma-Aldrich, Gillingham, UK A5441), LC3B (Cell Signaling Technology, Leiden, Netherlands 2775), S6K1 (9202), p-S6K1 (9205), ERK1/2 (9102), p-ERK1/2 (9106), ULK1 (4773), p-ULK1 (6888), p-AKT (9271), PTP4A3 (Santa Cruz Biotechnology, Heidelberg, Germany sc-130355), AKT , pan-PTP4A3 (Bio-Techne MAB32191), and GFP (Thermo Fisher Scientific, Horsham, UK A-11122), then washed thrice with TBS-T and incubated with species-appropriate HRP- conjugated secondary antibodies (Thermo Fisher Scientific) diluted in Blocking buffer.

Techniques: Expressing, Western Blot, RNA Sequencing, Gene Expression, Phospho-proteomics, Comparison, Control

OVCAR 3 cells were transiently transfected with either pEGFP (empty vector), pEGFP-PTP4A1 or pEGFP-PTP4A3. ( A ) Cells were incubated with or without 100 nM BafA1 for 1 h. The phosphorylation of S6K1 (pThr389) was used to confirm the inhibition of mTORC1 signalling and β- actin was used as a loading control, while GFP was probed as a transfection efficiency control. ( B ) Basal autophagy activity was quantified by densitometry of LC3B-II and normalised to β-actin. ( C ) Alternatively, cells were incubated with or without EBSS for 2 h in the presence or absence of BafA1 (100 nM) for the last hour. ( D ) Activatable autophagy was quantified by densitometry of LC3B-II normalised to β-actin expression. Data was pooled from three independent experiments and error bars = ±S.E.M. * p< 0.05, *** p< 0.001, **** p< 0.0001 by two-way ANOVA test.

Journal: bioRxiv

Article Title: Targeting of PTP4A3 overexpression sensitises HGSOC cells towards chemotherapeutic drugs

doi: 10.1101/2024.10.28.620719

Figure Lengend Snippet: OVCAR 3 cells were transiently transfected with either pEGFP (empty vector), pEGFP-PTP4A1 or pEGFP-PTP4A3. ( A ) Cells were incubated with or without 100 nM BafA1 for 1 h. The phosphorylation of S6K1 (pThr389) was used to confirm the inhibition of mTORC1 signalling and β- actin was used as a loading control, while GFP was probed as a transfection efficiency control. ( B ) Basal autophagy activity was quantified by densitometry of LC3B-II and normalised to β-actin. ( C ) Alternatively, cells were incubated with or without EBSS for 2 h in the presence or absence of BafA1 (100 nM) for the last hour. ( D ) Activatable autophagy was quantified by densitometry of LC3B-II normalised to β-actin expression. Data was pooled from three independent experiments and error bars = ±S.E.M. * p< 0.05, *** p< 0.001, **** p< 0.0001 by two-way ANOVA test.

Techniques: Transfection, Plasmid Preparation, Incubation, Phospho-proteomics, Inhibition, Control, Activity Assay, Expressing

Kuramochi ( A ) and OVCAR 4 ( B ) cells were infected with lentiviral particles harbouring either scrambled control shRNA (Scr) or PTP4A3-targeting shRNA (shPTP4A3). The silencing of PTP4A3 expression was quantified by Western immunoblotting. ( C, D ) Kuramochi-Scr (K- Scr), ( E, F ) Kuramochi-shPTP4A3 (K-shPTP4A3), ( G, H ) OVCAR 4-Scr (4-Scr) and ( I, J ) OVCAR 4-shPTP4A3 (4-shPTP4A3) cells were incubated with EBSS for 0, 1, 2 or 4 h and BafA1 (100 nM) was added for the final hour. ( C, E, G, I ) The phosphorylation of S6K1 (pThr389) was assessed by western blot to confirm inhibition of mTORC1 signalling. β-actin was used as a loading control. ( D, F, H, J ) Activation of autophagy was quantified by densitometry of LC3B-II normalised to β-actin. Data was pooled from at least three independent experiments and error bars = ±S.E.M. * p< 0.05, ** p< 0.01 by two-way ANOVA test.

Journal: bioRxiv

Article Title: Targeting of PTP4A3 overexpression sensitises HGSOC cells towards chemotherapeutic drugs

doi: 10.1101/2024.10.28.620719

Figure Lengend Snippet: Kuramochi ( A ) and OVCAR 4 ( B ) cells were infected with lentiviral particles harbouring either scrambled control shRNA (Scr) or PTP4A3-targeting shRNA (shPTP4A3). The silencing of PTP4A3 expression was quantified by Western immunoblotting. ( C, D ) Kuramochi-Scr (K- Scr), ( E, F ) Kuramochi-shPTP4A3 (K-shPTP4A3), ( G, H ) OVCAR 4-Scr (4-Scr) and ( I, J ) OVCAR 4-shPTP4A3 (4-shPTP4A3) cells were incubated with EBSS for 0, 1, 2 or 4 h and BafA1 (100 nM) was added for the final hour. ( C, E, G, I ) The phosphorylation of S6K1 (pThr389) was assessed by western blot to confirm inhibition of mTORC1 signalling. β-actin was used as a loading control. ( D, F, H, J ) Activation of autophagy was quantified by densitometry of LC3B-II normalised to β-actin. Data was pooled from at least three independent experiments and error bars = ±S.E.M. * p< 0.05, ** p< 0.01 by two-way ANOVA test.

Techniques: Infection, Control, shRNA, Expressing, Western Blot, Incubation, Phospho-proteomics, Inhibition, Activation Assay

( A ) Kuramochi-WT, Scr and shPTP4A3 and ( B ) OVCAR 4-WT, Scr and shPTP4A3 cells were treated with increasing concentrations of JMS-053 (iPRL; 0 - 25 µM) for 2 h. Cell extracts were analysed for phosphorylation of ULK1 (pSer757), S6K1 (pThr389), AKT/PKB (pSer473) and ERK1-2 (pThr202-Tyr204). LC3B was used as a marker of autophagy activity, β-actin was used as a loading control, and PTP4A3 knockdown was also confirmed. ( C-F ) The basal phosphorylation of AKT and ERK in WT, Scr and shPTP4A3 cells (no JMS-053 treatment) in ( C, D ) Kuramochi and ( E, F ) OVCAR 4 cells was determined. Data was pooled from three independent experiments and error bars = ±S.E.M.

Journal: bioRxiv

Article Title: Targeting of PTP4A3 overexpression sensitises HGSOC cells towards chemotherapeutic drugs

doi: 10.1101/2024.10.28.620719

Figure Lengend Snippet: ( A ) Kuramochi-WT, Scr and shPTP4A3 and ( B ) OVCAR 4-WT, Scr and shPTP4A3 cells were treated with increasing concentrations of JMS-053 (iPRL; 0 - 25 µM) for 2 h. Cell extracts were analysed for phosphorylation of ULK1 (pSer757), S6K1 (pThr389), AKT/PKB (pSer473) and ERK1-2 (pThr202-Tyr204). LC3B was used as a marker of autophagy activity, β-actin was used as a loading control, and PTP4A3 knockdown was also confirmed. ( C-F ) The basal phosphorylation of AKT and ERK in WT, Scr and shPTP4A3 cells (no JMS-053 treatment) in ( C, D ) Kuramochi and ( E, F ) OVCAR 4 cells was determined. Data was pooled from three independent experiments and error bars = ±S.E.M.

Techniques: Phospho-proteomics, Marker, Activity Assay, Control, Knockdown

Overexpression of PRL1 and PRL3 induces membrane blebbing. ( A ) CHO cells for over-expression of myc-PRL1 and myc-PRL3 were treated with or without 4 µg/ml of doxycycline-HCl for 4h (labeled as Tet). Cell lysate was then subjected to western blot analysis with myc antibodies. ( B ) Cells as described in panel A were observed under the light microscope. Scale bar, 10 µm. ( C ) Cells as described in panel A with the Tet treatment were immunostained with myc (green). Scale bar, 50 µm. ( D-E ) Cells described as in panel A were observed under electron microscopy (EM). Scale bars were as labeled.

Journal: Theranostics

Article Title: PRL1 and PRL3 promote macropinocytosis via its lipid phosphatase activity

doi: 10.7150/thno.93127

Figure Lengend Snippet: Overexpression of PRL1 and PRL3 induces membrane blebbing. ( A ) CHO cells for over-expression of myc-PRL1 and myc-PRL3 were treated with or without 4 µg/ml of doxycycline-HCl for 4h (labeled as Tet). Cell lysate was then subjected to western blot analysis with myc antibodies. ( B ) Cells as described in panel A were observed under the light microscope. Scale bar, 10 µm. ( C ) Cells as described in panel A with the Tet treatment were immunostained with myc (green). Scale bar, 50 µm. ( D-E ) Cells described as in panel A were observed under electron microscopy (EM). Scale bars were as labeled.

Article Snippet: Antibodies against PRL3 (sc-130355), PRL1 (sc-130354), GST (sc-138) and c-myc (sc-40) were purchased from Santa Cruz Biotechnology.

Techniques: Over Expression, Membrane, Labeling, Western Blot, Light Microscopy, Electron Microscopy

PRLs interact with PIPs. ( A-B ) Immunohistochemical (IHC) staining for different PIP lipids in CHO cells with over-expression of myc-PRL1 and myc-PRL3. Scale bar, 50 µm ( A ). Statistical analyses were detailed in panel (B), where the percentage of cells exhibiting positive immunohistochemical (IHC) staining was quantified (mean ± SD). ****p < 0.0001. ( C-D ) PIP lipid strip for interaction with purified GST-PRL1, GST-PRL3 and GST-PRL2. SPD-3 was a positive control with a specific affinity to PI(3)P. ( E ) Molecular docking analysis of PRL3 with 4 interacting PIP lipids detected in panel D.

Journal: Theranostics

Article Title: PRL1 and PRL3 promote macropinocytosis via its lipid phosphatase activity

doi: 10.7150/thno.93127

Figure Lengend Snippet: PRLs interact with PIPs. ( A-B ) Immunohistochemical (IHC) staining for different PIP lipids in CHO cells with over-expression of myc-PRL1 and myc-PRL3. Scale bar, 50 µm ( A ). Statistical analyses were detailed in panel (B), where the percentage of cells exhibiting positive immunohistochemical (IHC) staining was quantified (mean ± SD). ****p < 0.0001. ( C-D ) PIP lipid strip for interaction with purified GST-PRL1, GST-PRL3 and GST-PRL2. SPD-3 was a positive control with a specific affinity to PI(3)P. ( E ) Molecular docking analysis of PRL3 with 4 interacting PIP lipids detected in panel D.

Article Snippet: Antibodies against PRL3 (sc-130355), PRL1 (sc-130354), GST (sc-138) and c-myc (sc-40) were purchased from Santa Cruz Biotechnology.

Techniques: Immunohistochemical staining, Immunohistochemistry, Over Expression, Stripping Membranes, Purification, Positive Control

PRL1 and PRL3 act as lipid phosphatases. ( A ) A simplified cartoon showing the relationship among different PIP lipids. ( B ) Comparison of the structures of PRL1 (PDB code: 1RXD) or PRL3 (PDB code: 1R6H) and PTEN (PDB code: 1D5R) ( C ) Comparison of the structures of PRL1 or PRL3 and Sac1 (PDB code: 3LWT). ( D ) Alignment of sequences of PRL1, PRL3, PTEN and SAC1 proteins. The size of the single letters in the sequence scales with its conservation at this position. The conserved motif required for PRLs' enzyme activity is highlighted by labeled rectangles. The figure was presented through http://weblogo.threeplusone.com/ . ( E ) Molecular docking analysis showing the 4 interacting PIP lipids docking into PRL3. ( F ) Malachite green assay to confirm the lipid phosphatase activity of PRL1/3. Data are from three replicate experiments (mean ± SD). ( G ) Coomassie blue staining of purified proteins as indicated. ( H ) PI(3)P in cells with overexpression of PRL1/3 WT or CS mutant were measured by a quantitative ELISA. The PI(3)P levels were normalized to those observed in cells expressing empty vector. **p< 0.01. ( I ) A cartoon showing the direct dephosphorylation of PI(3,4)P 2 and PI(3,5)P 2 by PRLs.

Journal: Theranostics

Article Title: PRL1 and PRL3 promote macropinocytosis via its lipid phosphatase activity

doi: 10.7150/thno.93127

Figure Lengend Snippet: PRL1 and PRL3 act as lipid phosphatases. ( A ) A simplified cartoon showing the relationship among different PIP lipids. ( B ) Comparison of the structures of PRL1 (PDB code: 1RXD) or PRL3 (PDB code: 1R6H) and PTEN (PDB code: 1D5R) ( C ) Comparison of the structures of PRL1 or PRL3 and Sac1 (PDB code: 3LWT). ( D ) Alignment of sequences of PRL1, PRL3, PTEN and SAC1 proteins. The size of the single letters in the sequence scales with its conservation at this position. The conserved motif required for PRLs' enzyme activity is highlighted by labeled rectangles. The figure was presented through http://weblogo.threeplusone.com/ . ( E ) Molecular docking analysis showing the 4 interacting PIP lipids docking into PRL3. ( F ) Malachite green assay to confirm the lipid phosphatase activity of PRL1/3. Data are from three replicate experiments (mean ± SD). ( G ) Coomassie blue staining of purified proteins as indicated. ( H ) PI(3)P in cells with overexpression of PRL1/3 WT or CS mutant were measured by a quantitative ELISA. The PI(3)P levels were normalized to those observed in cells expressing empty vector. **p< 0.01. ( I ) A cartoon showing the direct dephosphorylation of PI(3,4)P 2 and PI(3,5)P 2 by PRLs.

Article Snippet: Antibodies against PRL3 (sc-130355), PRL1 (sc-130354), GST (sc-138) and c-myc (sc-40) were purchased from Santa Cruz Biotechnology.

Techniques: Comparison, Sequencing, Activity Assay, Labeling, Malachite Green Assay, Staining, Purification, Over Expression, Mutagenesis, Enzyme-linked Immunosorbent Assay, Expressing, Plasmid Preparation, De-Phosphorylation Assay

PRL3 interactomes identify extracellular proteins. (A) GO analysis (cellular compartment) on the PRL3 interactomes. (B) The interactomes network map of PRL3 interactomes. The red dots show the proteins known to be involved in extracellular region regulation.

Journal: Theranostics

Article Title: PRL1 and PRL3 promote macropinocytosis via its lipid phosphatase activity

doi: 10.7150/thno.93127

Figure Lengend Snippet: PRL3 interactomes identify extracellular proteins. (A) GO analysis (cellular compartment) on the PRL3 interactomes. (B) The interactomes network map of PRL3 interactomes. The red dots show the proteins known to be involved in extracellular region regulation.

Article Snippet: Antibodies against PRL3 (sc-130355), PRL1 (sc-130354), GST (sc-138) and c-myc (sc-40) were purchased from Santa Cruz Biotechnology.

Techniques:

PRLs induce macropinocytosis depending on the phosphatase activity. ( A ) WT and PRL3 KO Huh7 cells were treated with or without EGF (200 ng/mL). The IF signal of F-actin was observed under confocal microscopy. Scale bar, 10 μm. The lane labeled

Journal: Theranostics

Article Title: PRL1 and PRL3 promote macropinocytosis via its lipid phosphatase activity

doi: 10.7150/thno.93127

Figure Lengend Snippet: PRLs induce macropinocytosis depending on the phosphatase activity. ( A ) WT and PRL3 KO Huh7 cells were treated with or without EGF (200 ng/mL). The IF signal of F-actin was observed under confocal microscopy. Scale bar, 10 μm. The lane labeled "Enhanced" was included to display the digitally enhanced signal of F-actin staining, providing a clearer visualization of membrane morphology. ( B ) Dextran 70KD uptake assay was performed on WT and PRL3 KO U251 cells with or without treatment of EGF (200 ng/mL). Scale bar, 10 μm. ( C ) Dextran 70KD uptake assay was performed on U251 cells overexpressing GFP, GFP-PRL3 and GFP-PRL3 CS mutant. Cells were treated with or without macropinocytosis inhibitor EIPA. Scale bar, 10 μm. ( D ) Proliferation of indicated cells incubated in medium with normal (2 mM Q) or subphysiological (0.2 mM Q) glutamine concentration in the absence or presence of 2% BSA. ( E ) Wound healing assay of the Vec, myc-PRL1 and myc-PRL3 overexpressing cells. Cells were treated with or without EIPA. Scale bar, 50 μm. ( F ) Transwell assay of the Vec, myc-PRL1 and myc-PRL3 overexpressing cells. Cells were treated with or without EIPA. Scale bar, 50 μm.

Article Snippet: Antibodies against PRL3 (sc-130355), PRL1 (sc-130354), GST (sc-138) and c-myc (sc-40) were purchased from Santa Cruz Biotechnology.

Techniques: Activity Assay, Confocal Microscopy, Labeling, Staining, Membrane, Mutagenesis, Incubation, Concentration Assay, Wound Healing Assay, Transwell Assay

PRLs are involved in glioma developments. ( A ) The expression data of PRL1 and PRL3 retrieved from TCGA and GTEx database. Red bar, tumor samples. Grey bar, normal samples. Cancer entities acronyms: Glioblastoma multiform (GBM), Brain Lower Grade Glioma (LGG). ( B ) The PRL1 and PRL3 normalized expression levels (log 2 (Norm_Count+1)) in GBM and LGG samples were compared by their histological Grade. ( C ) Kaplan-Meier survival curves for LGG and GBM samples were presented. ( D-E ) Immuno-histochemical staining of PRL1, PRL3 and PI(3)P on brain tumor tissues. ( F ) Overall survival map for PRL3 and macropinocytosis genes was generated based on the TCGA datasets (GBM & LGG). The dark blue boxes denote higher risk and the white boxes represent lower risk, with an increase in the gene expression. The blocks with black frames indicate statistical significance in prognostic analyses. ( G ) TCGA GBM and LGG samples were divided into two groups with RAC1 high expression or low expression. Kaplan-Meier survival curves for indicated PRL genes were presented.

Journal: Theranostics

Article Title: PRL1 and PRL3 promote macropinocytosis via its lipid phosphatase activity

doi: 10.7150/thno.93127

Figure Lengend Snippet: PRLs are involved in glioma developments. ( A ) The expression data of PRL1 and PRL3 retrieved from TCGA and GTEx database. Red bar, tumor samples. Grey bar, normal samples. Cancer entities acronyms: Glioblastoma multiform (GBM), Brain Lower Grade Glioma (LGG). ( B ) The PRL1 and PRL3 normalized expression levels (log 2 (Norm_Count+1)) in GBM and LGG samples were compared by their histological Grade. ( C ) Kaplan-Meier survival curves for LGG and GBM samples were presented. ( D-E ) Immuno-histochemical staining of PRL1, PRL3 and PI(3)P on brain tumor tissues. ( F ) Overall survival map for PRL3 and macropinocytosis genes was generated based on the TCGA datasets (GBM & LGG). The dark blue boxes denote higher risk and the white boxes represent lower risk, with an increase in the gene expression. The blocks with black frames indicate statistical significance in prognostic analyses. ( G ) TCGA GBM and LGG samples were divided into two groups with RAC1 high expression or low expression. Kaplan-Meier survival curves for indicated PRL genes were presented.

Article Snippet: Antibodies against PRL3 (sc-130355), PRL1 (sc-130354), GST (sc-138) and c-myc (sc-40) were purchased from Santa Cruz Biotechnology.

Techniques: Expressing, Staining, Generated, Gene Expression

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