human ppm1f tissue expression data Search Results


mppm1f  (Thermo Fisher)
99
Thermo Fisher mppm1f
<t>PPM1F</t> knock-out embryos show severe defects, resulting in early abortion of development. A PPM1F ± mice were mated and embryos were isolated and genotyped at 12.5, 13.5 and 14.5 days post coitus. B WCLs of MEFs isolated at day E10.5 from regularly developed (putative PPM1F +/+ and PPM1F ±) or malformed (putative PPM1F-/-) embryos were probed with polyclonal <t>α-mPPM1F</t> antiserum (upper panel) or monoclonal α-tubulin (lower panel). C Genomic DNA was extracted from E10.5 fibroblasts as in ( B ). Genotyping PCR identified WT, heterozygous and homozygous ppm1f KO embryos. D Isolated ppm1f −/− embryo at E10.5 (right picture) is smaller in size compared to a wildtype embryo and shows a stunted forebrain and hemorhages (left picture); malformation of the telencephalon (arrow) and branchial archs (arrowhead) in the ppm1f −/− embryo is indicated; scale bar: 1 mm. D Whole-mount X-gal staining and sagittal sections of representative ppm1f +/+ (left picture) and ppm1f ± embryo (right picture) at E10.5 showing strong β-galactosidase expression in the rostral region of the telencephalon, the neural tube, the liver and lung. Tc: telencephalon; FV: forebrain vesicle; NT: neural tube; NL: neural lumen; BA: branchial arch; H: heart; Li: liver; scale bar: 500 μm. Areas marked with numbered boxes are shown enlarged on the right hand side; scale bar enlargement: 150 µm
Mppm1f, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/mppm1f/product/Thermo Fisher
Average 99 stars, based on 1 article reviews
mppm1f - by Bioz Stars, 2026-06
99/100 stars
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hppm1f  (Proteintech)
93
Proteintech hppm1f
PPM1F contributes to the invasive phenotype of tumor cells. A WCLs from indicated cancer cell lines were analyzed by Western blotting with α-human PPM1F or α-integrin β1 antibodies. α-Tubulin antibody was used as loading control. B , C Indicated serum-starved cancer cells were seeded on top of a Matrigel basement membrane (30 µg/100 µl) in Boyden chamber cell invasion assays using 20% FCS as stimulus or 2% BSA to evaluate random invasion activity. NIH3 T3 cells served as non-invasive control cells. Representative pictures of the lower porous membrane surface (20x) are shown in (B); scale bar: 50 µm. Crystal violet-stained cells can be distinguished from the 8 µm membrane pores. Cells were evaluated for invasion after 24 h by dye elution with 10% acetic acid and absorbance measurement at 590 nm. Graph in ( C ) shows quantified means ± SEM from three independent experiments. Statistics was performed using one-way ANOVA and Bonferroni post-hoc test ( p *** < 0.001, p ** < 0.01, ns = not significant). D MCF-7 cells were stably transduced with lentiviral particles harboring a bicistronic GFP and <t>hPPM1F</t> wildtype or hPPM1F D360 A expression cassette and single-cell sorted via flow cytometry for GFP positive cells to obtain a mixed population of PPM1F-overexpressing MCF-7 cells (PPM1F + + and PPM1F D360 A + +). WCL of the wildtype and modified cell lines were analyzed by Western blotting with indicated antibodies. α-tubulin antibody (lowest panel) served as loading control. E Serum-starved cells from ( D ) were seeded on top of a Matrigel base (30 µg/100 µl) in Boyden chambers. Cell invasion was stimulated by addition of 20% FCS or 2% BSA to the lower chamber. Representative pictures of the lower porous membrane surface (20x) are shown; scale bar: 50 µm. Crystal violet-stained cells can be distinguished from the 8 µm membrane pores. Invasion was quantified by dye elution. Graph (right) shows means ± SEM from four independent experiments performed in triplicate. Statistics as in ( C )
Hppm1f, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/hppm1f/product/Proteintech
Average 93 stars, based on 1 article reviews
hppm1f - by Bioz Stars, 2026-06
93/100 stars
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protein phosphatase 1f antibody  (Novus Biologicals)
N/A
The Protein phosphatase 1F Antibody from Novus Biologicals is a rabbit polyclonal antibody to Protein phosphatase 1F This antibody reacts with human The Protein phosphatase 1F Antibody has been validated for the following applications Western
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ppm1f antibody (fitc)  (biorbyt)
N/A
Rabbit Polyclonal to PPM1F conjugated to FITC. Isotype Note: IgG Host Note: Rabbit Conjugation Note: FITC Reactivity Note: Human Application Note: IF/ICC
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ppm1f nm 014634 human tagged orf clone lentiviral particle  (OriGene)
N/A
Lenti ORF particles PPM1F Myc DDK tagged Human protein phosphatase Mg2 Mn2 dependent 1F PPM1F 200ul 10 7 TU mL
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anti-ppm1f (full length) polyclonal antibody  (Creative BioMart)
N/A
Dephosphorylates and concomitantly deactivates CaM-kinase II activated upon autophosphorylation, and CaM-kinases IV and I activated upon phosphorylation by CaM-kinase kinase. Promotes apoptosis.Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term.
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recombinant human ppm1f,gst-tagged  (Creative BioMart)
N/A
Recombinant full-length human CaMKPase was expressed inE. colicells using an N-terminal GST tag. MW = 74kDa.CaMKPase is a member of the PP2C family of Ser/Thr protein phosphatases that dephosphorylate and regulate the multifunctional Ca2+/calmodulin-dependent protein
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anti-ppm1f antibody  (St Johns Laboratory)
N/A
The protein encoded by this gene is a member of the PP2C family of Ser/Thr protein phosphatases. PP2C family members are known to be negative regulators of cell stress response pathways. This phosphatase can interact
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ppm1f antibody  (Abbexa)
N/A
The protein encoded by this gene is a member of the PP2C family of Ser Thr protein phosphatases PP2C family members are known to be negative regulators of cell stress response pathways This phosphatase can
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mirna 3´utr target expression clone for human ppm1f  (Genecopoeia)
N/A
GeneCopoeia offers genome-wide human, mouse and rat microRNA (miRNA) 3′ UTR target clones in mammalian expression vectors. miRNA 3′ UTR target clones can be used for miRNA target identification and functional validation of predicted targets,
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rabbit anti- ppm1f polyclonal antibody  (Cusabio)
N/A
Rabbit anti-Human PPM1F Polyclonal Antibody
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Image Search Results


PPM1F knock-out embryos show severe defects, resulting in early abortion of development. A PPM1F ± mice were mated and embryos were isolated and genotyped at 12.5, 13.5 and 14.5 days post coitus. B WCLs of MEFs isolated at day E10.5 from regularly developed (putative PPM1F +/+ and PPM1F ±) or malformed (putative PPM1F-/-) embryos were probed with polyclonal α-mPPM1F antiserum (upper panel) or monoclonal α-tubulin (lower panel). C Genomic DNA was extracted from E10.5 fibroblasts as in ( B ). Genotyping PCR identified WT, heterozygous and homozygous ppm1f KO embryos. D Isolated ppm1f −/− embryo at E10.5 (right picture) is smaller in size compared to a wildtype embryo and shows a stunted forebrain and hemorhages (left picture); malformation of the telencephalon (arrow) and branchial archs (arrowhead) in the ppm1f −/− embryo is indicated; scale bar: 1 mm. D Whole-mount X-gal staining and sagittal sections of representative ppm1f +/+ (left picture) and ppm1f ± embryo (right picture) at E10.5 showing strong β-galactosidase expression in the rostral region of the telencephalon, the neural tube, the liver and lung. Tc: telencephalon; FV: forebrain vesicle; NT: neural tube; NL: neural lumen; BA: branchial arch; H: heart; Li: liver; scale bar: 500 μm. Areas marked with numbered boxes are shown enlarged on the right hand side; scale bar enlargement: 150 µm

Journal: BMC Biology

Article Title: The phosphatase PPM1F, a negative regulator of integrin activity, is essential for embryonic development and controls tumor cell invasion

doi: 10.1186/s12915-025-02254-3

Figure Lengend Snippet: PPM1F knock-out embryos show severe defects, resulting in early abortion of development. A PPM1F ± mice were mated and embryos were isolated and genotyped at 12.5, 13.5 and 14.5 days post coitus. B WCLs of MEFs isolated at day E10.5 from regularly developed (putative PPM1F +/+ and PPM1F ±) or malformed (putative PPM1F-/-) embryos were probed with polyclonal α-mPPM1F antiserum (upper panel) or monoclonal α-tubulin (lower panel). C Genomic DNA was extracted from E10.5 fibroblasts as in ( B ). Genotyping PCR identified WT, heterozygous and homozygous ppm1f KO embryos. D Isolated ppm1f −/− embryo at E10.5 (right picture) is smaller in size compared to a wildtype embryo and shows a stunted forebrain and hemorhages (left picture); malformation of the telencephalon (arrow) and branchial archs (arrowhead) in the ppm1f −/− embryo is indicated; scale bar: 1 mm. D Whole-mount X-gal staining and sagittal sections of representative ppm1f +/+ (left picture) and ppm1f ± embryo (right picture) at E10.5 showing strong β-galactosidase expression in the rostral region of the telencephalon, the neural tube, the liver and lung. Tc: telencephalon; FV: forebrain vesicle; NT: neural tube; NL: neural lumen; BA: branchial arch; H: heart; Li: liver; scale bar: 500 μm. Areas marked with numbered boxes are shown enlarged on the right hand side; scale bar enlargement: 150 µm

Article Snippet: The following antibodies were used with the corresponding dilutions for western blot analysis (WB), immunofluorescence (IF), immunohistochemistry (IHC), immunoprecipitation (IP), or integrin activity assay (IA): α-Actinin (BM75.2, mouse anti-human, Abcam; 1:1000 WB), α 1 -integrin (TS2/7, mouse anti-human/anti-mouse, Abcam; 1:50 IF), α 2 -integrin (6 F1, mouse anti-human/anti-mouse, DSHB; 1:60 IF), α 3 -integrin (P1B5, mouse anti-human/anti-mouse, DSHB; 1:60 IF), α 5 -integrin (BIIG2, rat anti-human/anti-mouse, DSHB; 1:10 IF), α v -integrin (PE-P2 W7 mouse anti-human/anti-mouse, sc-9969; IF 1:300), β 1 -integrin (HMβ1-1, armenian hamster anti-mouse, Bio Legend; 1:300 IF; AIIB2, rat anti-human/anti-mouse, DSHB; 1:600 IF, IA; M-106, rabbit anti-mouse/anti-human, Santa Cruz; 1:500 WB; D2E5, rabbit anti-human, Cell Signaling; 1:1000 WB), human β 1 -integrin (P5D2, mouse anti-human, DSHB, 2.5 μg IP; 9EG7, rat anti- human, DSHB 2.5 μg IP; AIIB2, rat anti-human, DSHB; 2.5 μg IP), β 3 -integrin (2 C9.G3, arm. hamster anti-mouse, eBioscience; 1:300 IF; PM6/13, mouse anti-human, Abcam; 1:100 IF), β 5 -integrin (KN-52, mouse anti-mouse/human, eBioscience; IF 1:300), Focal adhesion kinase (FAK) (77, mouse anti-human, BD; 1:250 WB), integrin-linked kinase (ILK) (EP1593Y, rabbit anti-human, Epitomics; 1:800 WB), Kindlin-2 (3 A3, mouse anti-human, Millipore; 1:200 WB, 1:250 IF), Laminin (ab11575, rabbit anti-mouse, Abcam; 1:300 IHC), Nestin (rat-401, anti-mouse, Millipore; IHC 1:200), Paxillin (5H11, mouse monoclonal, Thermo Scientific; 1:1000 WB), hPPM1F (17,020–1-AP, rabbit anti-human, Protein-Tech; 1:1000 WB), mPPM1F (#1147, rabbit anti-mouse PPM1F; generated at the central animal care facility; University of Konstanz; 1:200 WB; see Additional File2: Fig. S2), FilaminA (EP2405Y, IgG, rabbit anti-human, Epitomics; 1:125.000 WB), Tubulin (E7, IgG1, mouse anti-human, DSHB; 1:1000), Talin (8 d4, mouse anti-human, Thermo Scientific; 1:800 WB, 1:40 IF), Vinculin (hVIN-1, mouse anti-human, Sigma; 1:2000 WB, 1:200 IF), Zyxin (Zol301, mouse anti-human, Abcam; 1:1000 WB), Dylight488-conjugated goat anti-mouse IgG (Jackson; 1:200), Cy3-conjugated goat anti-rabbit IgG (Jackson; 1:200), Cy3-conjugated goat anti-mouse IgG (Jackson; 1:200), Cy5-conjugated goat anti-mouse IgG (Jackson; 1:200), RhodamineRed-conjugated goat anti-rat IgG (Jackson; 1:200), RhodamineRed-conjugated goat anti-Armenian Hamster IgG (Jackson; 1:200), HRP-conjugated goat anti-mouse IgG (Jackson; WB 1:10 000), HRP-conjugated goat anti-rat IgG (Santa Cruz; 1:250), HRP-conjugated goat anti-rabbit IgG (Jackson; WB 1:3000), unspecific control IgG (anti-mouse, 96/1, generated at the Tierforschungsanlage; University of Konstanz; anti-rat, MJ7/18 Endoglin, DSHB).

Techniques: Knock-Out, Isolation, Staining, Expressing

PPM1F contributes to the invasive phenotype of tumor cells. A WCLs from indicated cancer cell lines were analyzed by Western blotting with α-human PPM1F or α-integrin β1 antibodies. α-Tubulin antibody was used as loading control. B , C Indicated serum-starved cancer cells were seeded on top of a Matrigel basement membrane (30 µg/100 µl) in Boyden chamber cell invasion assays using 20% FCS as stimulus or 2% BSA to evaluate random invasion activity. NIH3 T3 cells served as non-invasive control cells. Representative pictures of the lower porous membrane surface (20x) are shown in (B); scale bar: 50 µm. Crystal violet-stained cells can be distinguished from the 8 µm membrane pores. Cells were evaluated for invasion after 24 h by dye elution with 10% acetic acid and absorbance measurement at 590 nm. Graph in ( C ) shows quantified means ± SEM from three independent experiments. Statistics was performed using one-way ANOVA and Bonferroni post-hoc test ( p *** < 0.001, p ** < 0.01, ns = not significant). D MCF-7 cells were stably transduced with lentiviral particles harboring a bicistronic GFP and hPPM1F wildtype or hPPM1F D360 A expression cassette and single-cell sorted via flow cytometry for GFP positive cells to obtain a mixed population of PPM1F-overexpressing MCF-7 cells (PPM1F + + and PPM1F D360 A + +). WCL of the wildtype and modified cell lines were analyzed by Western blotting with indicated antibodies. α-tubulin antibody (lowest panel) served as loading control. E Serum-starved cells from ( D ) were seeded on top of a Matrigel base (30 µg/100 µl) in Boyden chambers. Cell invasion was stimulated by addition of 20% FCS or 2% BSA to the lower chamber. Representative pictures of the lower porous membrane surface (20x) are shown; scale bar: 50 µm. Crystal violet-stained cells can be distinguished from the 8 µm membrane pores. Invasion was quantified by dye elution. Graph (right) shows means ± SEM from four independent experiments performed in triplicate. Statistics as in ( C )

Journal: BMC Biology

Article Title: The phosphatase PPM1F, a negative regulator of integrin activity, is essential for embryonic development and controls tumor cell invasion

doi: 10.1186/s12915-025-02254-3

Figure Lengend Snippet: PPM1F contributes to the invasive phenotype of tumor cells. A WCLs from indicated cancer cell lines were analyzed by Western blotting with α-human PPM1F or α-integrin β1 antibodies. α-Tubulin antibody was used as loading control. B , C Indicated serum-starved cancer cells were seeded on top of a Matrigel basement membrane (30 µg/100 µl) in Boyden chamber cell invasion assays using 20% FCS as stimulus or 2% BSA to evaluate random invasion activity. NIH3 T3 cells served as non-invasive control cells. Representative pictures of the lower porous membrane surface (20x) are shown in (B); scale bar: 50 µm. Crystal violet-stained cells can be distinguished from the 8 µm membrane pores. Cells were evaluated for invasion after 24 h by dye elution with 10% acetic acid and absorbance measurement at 590 nm. Graph in ( C ) shows quantified means ± SEM from three independent experiments. Statistics was performed using one-way ANOVA and Bonferroni post-hoc test ( p *** < 0.001, p ** < 0.01, ns = not significant). D MCF-7 cells were stably transduced with lentiviral particles harboring a bicistronic GFP and hPPM1F wildtype or hPPM1F D360 A expression cassette and single-cell sorted via flow cytometry for GFP positive cells to obtain a mixed population of PPM1F-overexpressing MCF-7 cells (PPM1F + + and PPM1F D360 A + +). WCL of the wildtype and modified cell lines were analyzed by Western blotting with indicated antibodies. α-tubulin antibody (lowest panel) served as loading control. E Serum-starved cells from ( D ) were seeded on top of a Matrigel base (30 µg/100 µl) in Boyden chambers. Cell invasion was stimulated by addition of 20% FCS or 2% BSA to the lower chamber. Representative pictures of the lower porous membrane surface (20x) are shown; scale bar: 50 µm. Crystal violet-stained cells can be distinguished from the 8 µm membrane pores. Invasion was quantified by dye elution. Graph (right) shows means ± SEM from four independent experiments performed in triplicate. Statistics as in ( C )

Article Snippet: The following antibodies were used with the corresponding dilutions for western blot analysis (WB), immunofluorescence (IF), immunohistochemistry (IHC), immunoprecipitation (IP), or integrin activity assay (IA): α-Actinin (BM75.2, mouse anti-human, Abcam; 1:1000 WB), α 1 -integrin (TS2/7, mouse anti-human/anti-mouse, Abcam; 1:50 IF), α 2 -integrin (6 F1, mouse anti-human/anti-mouse, DSHB; 1:60 IF), α 3 -integrin (P1B5, mouse anti-human/anti-mouse, DSHB; 1:60 IF), α 5 -integrin (BIIG2, rat anti-human/anti-mouse, DSHB; 1:10 IF), α v -integrin (PE-P2 W7 mouse anti-human/anti-mouse, sc-9969; IF 1:300), β 1 -integrin (HMβ1-1, armenian hamster anti-mouse, Bio Legend; 1:300 IF; AIIB2, rat anti-human/anti-mouse, DSHB; 1:600 IF, IA; M-106, rabbit anti-mouse/anti-human, Santa Cruz; 1:500 WB; D2E5, rabbit anti-human, Cell Signaling; 1:1000 WB), human β 1 -integrin (P5D2, mouse anti-human, DSHB, 2.5 μg IP; 9EG7, rat anti- human, DSHB 2.5 μg IP; AIIB2, rat anti-human, DSHB; 2.5 μg IP), β 3 -integrin (2 C9.G3, arm. hamster anti-mouse, eBioscience; 1:300 IF; PM6/13, mouse anti-human, Abcam; 1:100 IF), β 5 -integrin (KN-52, mouse anti-mouse/human, eBioscience; IF 1:300), Focal adhesion kinase (FAK) (77, mouse anti-human, BD; 1:250 WB), integrin-linked kinase (ILK) (EP1593Y, rabbit anti-human, Epitomics; 1:800 WB), Kindlin-2 (3 A3, mouse anti-human, Millipore; 1:200 WB, 1:250 IF), Laminin (ab11575, rabbit anti-mouse, Abcam; 1:300 IHC), Nestin (rat-401, anti-mouse, Millipore; IHC 1:200), Paxillin (5H11, mouse monoclonal, Thermo Scientific; 1:1000 WB), hPPM1F (17,020–1-AP, rabbit anti-human, Protein-Tech; 1:1000 WB), mPPM1F (#1147, rabbit anti-mouse PPM1F; generated at the central animal care facility; University of Konstanz; 1:200 WB; see Additional File2: Fig. S2), FilaminA (EP2405Y, IgG, rabbit anti-human, Epitomics; 1:125.000 WB), Tubulin (E7, IgG1, mouse anti-human, DSHB; 1:1000), Talin (8 d4, mouse anti-human, Thermo Scientific; 1:800 WB, 1:40 IF), Vinculin (hVIN-1, mouse anti-human, Sigma; 1:2000 WB, 1:200 IF), Zyxin (Zol301, mouse anti-human, Abcam; 1:1000 WB), Dylight488-conjugated goat anti-mouse IgG (Jackson; 1:200), Cy3-conjugated goat anti-rabbit IgG (Jackson; 1:200), Cy3-conjugated goat anti-mouse IgG (Jackson; 1:200), Cy5-conjugated goat anti-mouse IgG (Jackson; 1:200), RhodamineRed-conjugated goat anti-rat IgG (Jackson; 1:200), RhodamineRed-conjugated goat anti-Armenian Hamster IgG (Jackson; 1:200), HRP-conjugated goat anti-mouse IgG (Jackson; WB 1:10 000), HRP-conjugated goat anti-rat IgG (Santa Cruz; 1:250), HRP-conjugated goat anti-rabbit IgG (Jackson; WB 1:3000), unspecific control IgG (anti-mouse, 96/1, generated at the Tierforschungsanlage; University of Konstanz; anti-rat, MJ7/18 Endoglin, DSHB).

Techniques: Western Blot, Control, Membrane, Activity Assay, Staining, Stable Transfection, Transduction, Expressing, Flow Cytometry, Modification