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β catenin d10a8 xp rabbit mab  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc β catenin d10a8 xp rabbit mab
    Panx1 <t>increases</t> <t>β-Catenin</t> activity and promotes its nuclear translocation (A) Western blot shows Panx1 overexpression and knockout efficiency (GAPDH as loading control). (B) Glycosylation patterns of exogenous Panx1. (C and D) Total and non-phosphorylated β-catenin levels in whole cell and nuclear fractions (Lamin B1 as loading control). (E) Immunofluorescence of β-catenin nuclear translocation (red; nuclei, blue). Scale bars, 25 μm. (F) qRT-PCR of Wnt/β-catenin downstream gene expression normalized to PPIA. (G) Western blot of Wnt/β-catenin downstream proteins (GAPDH as loading control). Data are mean ± SD, statistics in (C), (D), (F), and (G): ∗ p < 0.05, ∗∗ p < 0.01, and ∗∗∗ p < 0.001, two-sided Student’s t test.
    β Catenin D10a8 Xp Rabbit Mab, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 2512 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/%CE%B2+catenin+d10a8/beta-Catenin+XP+Rabbit+mAb/pmc12999355-20-0-6
    Average 96 stars, based on 2512 article reviews
    β catenin d10a8 xp rabbit mab - by Bioz Stars, 2026-10
    96/100 stars

    Images

    1) Product Images from "Panx1 deficiency exacerbates GAN diet-induced obesity by destabilizing β-catenin via GSK3β"

    Article Title: Panx1 deficiency exacerbates GAN diet-induced obesity by destabilizing β-catenin via GSK3β

    Journal: iScience

    doi: 10.1016/j.isci.2026.115098

    Panx1 increases β-Catenin activity and promotes its nuclear translocation (A) Western blot shows Panx1 overexpression and knockout efficiency (GAPDH as loading control). (B) Glycosylation patterns of exogenous Panx1. (C and D) Total and non-phosphorylated β-catenin levels in whole cell and nuclear fractions (Lamin B1 as loading control). (E) Immunofluorescence of β-catenin nuclear translocation (red; nuclei, blue). Scale bars, 25 μm. (F) qRT-PCR of Wnt/β-catenin downstream gene expression normalized to PPIA. (G) Western blot of Wnt/β-catenin downstream proteins (GAPDH as loading control). Data are mean ± SD, statistics in (C), (D), (F), and (G): ∗ p < 0.05, ∗∗ p < 0.01, and ∗∗∗ p < 0.001, two-sided Student’s t test.
    Figure Legend Snippet: Panx1 increases β-Catenin activity and promotes its nuclear translocation (A) Western blot shows Panx1 overexpression and knockout efficiency (GAPDH as loading control). (B) Glycosylation patterns of exogenous Panx1. (C and D) Total and non-phosphorylated β-catenin levels in whole cell and nuclear fractions (Lamin B1 as loading control). (E) Immunofluorescence of β-catenin nuclear translocation (red; nuclei, blue). Scale bars, 25 μm. (F) qRT-PCR of Wnt/β-catenin downstream gene expression normalized to PPIA. (G) Western blot of Wnt/β-catenin downstream proteins (GAPDH as loading control). Data are mean ± SD, statistics in (C), (D), (F), and (G): ∗ p < 0.05, ∗∗ p < 0.01, and ∗∗∗ p < 0.001, two-sided Student’s t test.

    Techniques Used: Activity Assay, Translocation Assay, Western Blot, Over Expression, Knock-Out, Control, Glycoproteomics, Immunofluorescence, Quantitative RT-PCR, Gene Expression

    Panx1 forms complexes with β-Catenin and GSK-3β (A) Western blot of destruction complex proteins in Panx1-OE and Panx1 −/− 3T3-L1 cells (GAPDH as loading control). (B) Co-IP of Panx1 with β-catenin or destruction complex proteins in HEK293T cells expressing Panx1-HA. (C) Co-IP of β-catenin (total or phosphorylated) with GSK-3β in Panx1-OE and Panx1 −/− cells (GAPDH as loading control for input). (D) Western blot showing β-catenin knockdown efficiency in Panx1-OE cells (GAPDH as loading control). (E) Co-IP of Panx1 with GSK-3β after β-catenin knockdown (GAPDH as loading control for input). (F) Predicted 3D structures of Panx1, β-catenin, and GSK-3β complexes showing conformational changes. (G) Ranking scores of binding affinities among Panx1, β-catenin, and GSK-3β. Data are mean ± SD, statistics in (A): ∗ p < 0.05 and ∗∗ p < 0.01, two-sided Student’s t test.
    Figure Legend Snippet: Panx1 forms complexes with β-Catenin and GSK-3β (A) Western blot of destruction complex proteins in Panx1-OE and Panx1 −/− 3T3-L1 cells (GAPDH as loading control). (B) Co-IP of Panx1 with β-catenin or destruction complex proteins in HEK293T cells expressing Panx1-HA. (C) Co-IP of β-catenin (total or phosphorylated) with GSK-3β in Panx1-OE and Panx1 −/− cells (GAPDH as loading control for input). (D) Western blot showing β-catenin knockdown efficiency in Panx1-OE cells (GAPDH as loading control). (E) Co-IP of Panx1 with GSK-3β after β-catenin knockdown (GAPDH as loading control for input). (F) Predicted 3D structures of Panx1, β-catenin, and GSK-3β complexes showing conformational changes. (G) Ranking scores of binding affinities among Panx1, β-catenin, and GSK-3β. Data are mean ± SD, statistics in (A): ∗ p < 0.05 and ∗∗ p < 0.01, two-sided Student’s t test.

    Techniques Used: Western Blot, Control, Co-Immunoprecipitation Assay, Expressing, Knockdown, Binding Assay

    Effect of Panx1 on cell proliferation (A) Cell viability of Panx1-OE and Panx1 −/− cells. (B–D) Flow cytometry analysis of cell cycle distribution (PI staining) with the quantification of G1, S, and G2/M phases. (E) Western blot confirms β-catenin knockdown and effects on downstream proteins in Panx1-OE cells. (F and G) Flow cytometry and quantification of cell cycle distribution after β-catenin knockdown. Each panel represents an independently generated pair of stable lines, and statistical analyses are performed within each matched pair. Data are mean ± SD, statistics in (A), (D), and (G): ∗∗ p < 0.01 and ∗∗∗ p < 0.001, two-sided Student’s t test.
    Figure Legend Snippet: Effect of Panx1 on cell proliferation (A) Cell viability of Panx1-OE and Panx1 −/− cells. (B–D) Flow cytometry analysis of cell cycle distribution (PI staining) with the quantification of G1, S, and G2/M phases. (E) Western blot confirms β-catenin knockdown and effects on downstream proteins in Panx1-OE cells. (F and G) Flow cytometry and quantification of cell cycle distribution after β-catenin knockdown. Each panel represents an independently generated pair of stable lines, and statistical analyses are performed within each matched pair. Data are mean ± SD, statistics in (A), (D), and (G): ∗∗ p < 0.01 and ∗∗∗ p < 0.001, two-sided Student’s t test.

    Techniques Used: Flow Cytometry, Staining, Western Blot, Knockdown, Generated

    Related Articles

    Incubation:

    Article Title: Asiatic Acid Inhibits Nasopharyngeal Carcinoma Cell Viability and Migration via Suppressing STAT3 and Claudin-1
    Article Snippet: .. The membranes were blocked with 5% BSA in TBS-N for 1 h with these following primary antibodies: pY-STAT3 (Y705) (#9131S), caspase-3 (#9662S), vimentin (D21H3) (#5741T), E-cadherin (24E10) (#3195T), N-cadherin (D4R1H) (#13116T), claudin-1 (D5H1D) (#13255T), β-catenin (D10A8) (#8480T), β-actin (#4967) (Cell Signaling Technology, Inc. (Danvers, MA, USA)), and STAT3 (#610190) (BD Biosciences, San Jose, CA, USA) at 1:1000 dilution; then the membranes were incubated overnight at 4 °C. .. Membranes were washed three times with TBS-N and then incubated with secondary antibody (mouse: #ab6789, rabbit: #ab6721) (both from Abcam, Cambridge, UK) for 30 min. After washing, the immunoblots were visualized using a chemiluminescence (ECL) HRP substrate (Bio-Rad, California, USA).

    Article Title: Asiatic Acid Inhibits Nasopharyngeal Carcinoma Cell Viability and Migration via Suppressing STAT3 and Claudin-1.
    Article Snippet: .. The membranes were blocked with 5% BSA in TBS-N for 1 h with these following primary antibodies: pY-STAT3 (Y705) (#9131S), caspase-3 (#9662S), vimentin (D21H3) (#5741T), E-cadherin (24E10) (#3195T), N-cadherin (D4R1H) (#13116T), claudin-1 (D5H1D) (#13255T), β-catenin (D10A8) (#8480T), β-actin (#4967) (Cell Signaling Technology, Inc. (Danvers, MA, USA)), and STAT3 (#610190) (BD Biosciences, San Jose, CA, USA) at 1:1000 dilution; then the membranes were incubated overnight at 4 ◦C. .. Membranes were washed three times with TBS-N and then incubated with secondary antibody (mouse: #ab6789, rabbit: #ab6721) (both from Abcam, Cambridge, UK) for 30 min. After washing, the immunoblots were visualized using a chemiluminescence (ECL) HRP substrate (Bio-Rad, California, USA).

    other:


    Western Blot:

    Article Title: Engineered human iPS cell models reveal altered podocytogenesis and glomerular capillary wall in CHD-associated SMAD2 mutations
    Article Snippet: .. Primary antibodies used for Western blot were rabbit Anti-Phospho-SMAD1 (Ser206) (Cell Signaling; mAb #5753, 1:1000), rabbit Anti-SMAD2 (D43B4) (Cell Signaling; mAb #5339, 1:1000) rabbit Anti-SMAD3 (C67H9) (Cell Signaling; mAb #9523, 1:1000), rabbit Anti-Phospho-SMAD3 (C25A9) (Cell Signaling; mAb #9520, 1:1000), rabbit Anti-SMAD4 (D3R4N) (Cell Signaling; mAb #46535, 1:1000), rabbit Anti-SMAD6 (AbClonal; pAb #9520, 1:250), rabbit Anti-SMAD7 (AbClonal; pAb #16396, 1:250), rabbit Anti-Brachyury (Abcam; ab20680, 1:1000), rabbit Anti-CDX2 antibody (Abcam; ab76541, 1:1000), goat Anti-Goosecoid (R&D Systems, AF4086, 1:500), rabbit Anti-PAX2 (Cell Signaling; mAb #9666S, 1:1000), rabbit Anti β-Catenin (D10A8) (Cell Signaling; mAb #8480, 1:1000), mouse Anti-Twist antibody (Abcam; ab175430, 1:1000), rabbit Anti-Snail (C15D3) (Cell Signaling; mAb #3879, 1:1000), rabbit Anti-alpha smooth muscle Actin antibody (Abcam; mAb #ab7817, 1:500), rabbit Anti-MLKL antibody (Abcam; mAb #ab184718, 1:500), guinea pig Anti-Nephrin antibody (ARP; #GPN02, 1:500), rabbit Anti-Podocin (Abcam, mAb #ab50339, 1:1000), mouse Anti-Synaptopodin (D-9) (SantaCruz, mAb #sc-515842, 1:1000), mouse Anti-CD2AP (B-4) (SantaCruz, mAb #sc-25273, 1:1000), mouse Anti-GLEPP1 (B-6) (SantaCruz, mAb #sc-365354, 1:1000), mouse Anti-YAP (63.7) (SantaCruz; mAb #sc-101199, 1:1000), rabbit Anti-phospho-YAP (D9W2I) (Cell Signaling; mAb #13008, 1:1000), rabbit Anti-TEAD1 (D9X2L) (Cell Signaling; mAb #12292, 1:1000), rabbit Anti-CTGF (D8Z8U) (Cell Signaling; mAb #86641, 1:1000), rabbit Anti-Naked2 (C67C4) (Cell Signaling; mAb #2073, 1:1000), mouse Anti-VE-Cadherin (BV-9) (SantaCruz, mAb #sc-52751, 1:1000); rabbit Anti-transgelin (AbClonal, pAb, #A6760, 1: 1000), rabbit Anti-ICAM1/CD54 (AbClonal, pAb, #A5597, 1:1000), rabbit Anti-vimentin (AbClonal, pAb, #A2584, 1:1000), sheep Anti-PECAM1 (Bio-Rad, mAb, #CO.3E1D4, 1:1000), and rabbit Anti-GAPDH (Millipore Sigma; #ABS16, 1:10000). .. Secondary antibodies --HRP-conjugated goat anti-mouse (Cell Signaling; #7076, 1:5000),HRP-conjugated goat anti-rabbit (Cell Signaling; #7074, 1:10000), HRP-conjugated goat anti-guinea pig polyclonal (ARP; #90001, 1:1000), and HRP-conjugated donkey anti-goat polyclonal (R&D Systems, #HAF109, 1:1000) -- were diluted in TBST supplemented with 5% Blotto and incubated for 1 h at room temperature on a platform angle rocker.

    Article Title: Broad-spectrum kinome profiling identifies CDK6 upregulation as a driver of lenvatinib resistance in hepatocellular carcinoma
    Article Snippet: The protein lysate was immunoprecipitated overnight with anti-β-catenin (D10A8) antibody (#8480 S, Cell Signaling Technology) antibody at 4 °C with gentle rotation overnight, followed by Protein A agarose incubation (Cell Signaling Technology) for 8 hours at 4 °C with gentle agitation. .. Immunoprecipitates were washed thrice with 1% TritonX-100-PBS, eluted by boiling in 2× SDS loading buffer for 10 minutes, and subjected to immunoblotting analyses using primary antibodies against HA (1F5C6) (1:1000, 66006-1-Ig, Proteintech) and β-catenin (D10A8) (1:1000, #8480 S, Cell Signaling Technology). ..

    Article Title: Alpinetin Suppresses Effects of TGF-β1 on Stimulating the Production and Organization of Fibrotic Markers in Human Primary Dermal Fibroblasts
    Article Snippet: .. After blocking with 5% BSA/TBST at RT for 1 h, the immunoblots were probed with appropriate primary antibodies (all from Cell Signaling Technology (Boston, MA, USA)) against N-cadherin (D4R1H) (catalog number 13,116), β-catenin (D10A8) (catalog number 8480), vimentin (D21H3) (catalog number 5741), α-SMA (1A4) (catalog number 48,938), Col1A1 (catalog number 84,336), and β-actin (8H10D10) (catalog number 3700) followed by appropriate secondary antibodies which included an anti-mouse IgG conjugated with IRDye ® 800CW (catalog number 926-32210) and an anti-rabbit IgG conjugated with IRDye ® 680RT (catalog number 926-68071). .. Fluorescent signal was detected with the Odyssey ® CLx Imaging System (LI−COR Biosciences, Lincoln, NE, USA), and densitometric analysis was performed by the ImageJ software (version 1.51j8) (NIH, Bethesda, MD, USA).

    Blocking Assay:

    Article Title: Alpinetin Suppresses Effects of TGF-β1 on Stimulating the Production and Organization of Fibrotic Markers in Human Primary Dermal Fibroblasts
    Article Snippet: .. After blocking with 5% BSA/TBST at RT for 1 h, the immunoblots were probed with appropriate primary antibodies (all from Cell Signaling Technology (Boston, MA, USA)) against N-cadherin (D4R1H) (catalog number 13,116), β-catenin (D10A8) (catalog number 8480), vimentin (D21H3) (catalog number 5741), α-SMA (1A4) (catalog number 48,938), Col1A1 (catalog number 84,336), and β-actin (8H10D10) (catalog number 3700) followed by appropriate secondary antibodies which included an anti-mouse IgG conjugated with IRDye ® 800CW (catalog number 926-32210) and an anti-rabbit IgG conjugated with IRDye ® 680RT (catalog number 926-68071). .. Fluorescent signal was detected with the Odyssey ® CLx Imaging System (LI−COR Biosciences, Lincoln, NE, USA), and densitometric analysis was performed by the ImageJ software (version 1.51j8) (NIH, Bethesda, MD, USA).



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    Image Search Results


    Panx1 increases β-Catenin activity and promotes its nuclear translocation (A) Western blot shows Panx1 overexpression and knockout efficiency (GAPDH as loading control). (B) Glycosylation patterns of exogenous Panx1. (C and D) Total and non-phosphorylated β-catenin levels in whole cell and nuclear fractions (Lamin B1 as loading control). (E) Immunofluorescence of β-catenin nuclear translocation (red; nuclei, blue). Scale bars, 25 μm. (F) qRT-PCR of Wnt/β-catenin downstream gene expression normalized to PPIA. (G) Western blot of Wnt/β-catenin downstream proteins (GAPDH as loading control). Data are mean ± SD, statistics in (C), (D), (F), and (G): ∗ p < 0.05, ∗∗ p < 0.01, and ∗∗∗ p < 0.001, two-sided Student’s t test.

    Journal: iScience

    Article Title: Panx1 deficiency exacerbates GAN diet-induced obesity by destabilizing β-catenin via GSK3β

    doi: 10.1016/j.isci.2026.115098

    Figure Lengend Snippet: Panx1 increases β-Catenin activity and promotes its nuclear translocation (A) Western blot shows Panx1 overexpression and knockout efficiency (GAPDH as loading control). (B) Glycosylation patterns of exogenous Panx1. (C and D) Total and non-phosphorylated β-catenin levels in whole cell and nuclear fractions (Lamin B1 as loading control). (E) Immunofluorescence of β-catenin nuclear translocation (red; nuclei, blue). Scale bars, 25 μm. (F) qRT-PCR of Wnt/β-catenin downstream gene expression normalized to PPIA. (G) Western blot of Wnt/β-catenin downstream proteins (GAPDH as loading control). Data are mean ± SD, statistics in (C), (D), (F), and (G): ∗ p < 0.05, ∗∗ p < 0.01, and ∗∗∗ p < 0.001, two-sided Student’s t test.

    Article Snippet: β-Catenin (D10A8) XP Rabbit mAb , Cell Signaling Technology , Cat# 8480S; RRID: AB_11127855.

    Techniques: Activity Assay, Translocation Assay, Western Blot, Over Expression, Knock-Out, Control, Glycoproteomics, Immunofluorescence, Quantitative RT-PCR, Gene Expression

    Panx1 forms complexes with β-Catenin and GSK-3β (A) Western blot of destruction complex proteins in Panx1-OE and Panx1 −/− 3T3-L1 cells (GAPDH as loading control). (B) Co-IP of Panx1 with β-catenin or destruction complex proteins in HEK293T cells expressing Panx1-HA. (C) Co-IP of β-catenin (total or phosphorylated) with GSK-3β in Panx1-OE and Panx1 −/− cells (GAPDH as loading control for input). (D) Western blot showing β-catenin knockdown efficiency in Panx1-OE cells (GAPDH as loading control). (E) Co-IP of Panx1 with GSK-3β after β-catenin knockdown (GAPDH as loading control for input). (F) Predicted 3D structures of Panx1, β-catenin, and GSK-3β complexes showing conformational changes. (G) Ranking scores of binding affinities among Panx1, β-catenin, and GSK-3β. Data are mean ± SD, statistics in (A): ∗ p < 0.05 and ∗∗ p < 0.01, two-sided Student’s t test.

    Journal: iScience

    Article Title: Panx1 deficiency exacerbates GAN diet-induced obesity by destabilizing β-catenin via GSK3β

    doi: 10.1016/j.isci.2026.115098

    Figure Lengend Snippet: Panx1 forms complexes with β-Catenin and GSK-3β (A) Western blot of destruction complex proteins in Panx1-OE and Panx1 −/− 3T3-L1 cells (GAPDH as loading control). (B) Co-IP of Panx1 with β-catenin or destruction complex proteins in HEK293T cells expressing Panx1-HA. (C) Co-IP of β-catenin (total or phosphorylated) with GSK-3β in Panx1-OE and Panx1 −/− cells (GAPDH as loading control for input). (D) Western blot showing β-catenin knockdown efficiency in Panx1-OE cells (GAPDH as loading control). (E) Co-IP of Panx1 with GSK-3β after β-catenin knockdown (GAPDH as loading control for input). (F) Predicted 3D structures of Panx1, β-catenin, and GSK-3β complexes showing conformational changes. (G) Ranking scores of binding affinities among Panx1, β-catenin, and GSK-3β. Data are mean ± SD, statistics in (A): ∗ p < 0.05 and ∗∗ p < 0.01, two-sided Student’s t test.

    Article Snippet: β-Catenin (D10A8) XP Rabbit mAb , Cell Signaling Technology , Cat# 8480S; RRID: AB_11127855.

    Techniques: Western Blot, Control, Co-Immunoprecipitation Assay, Expressing, Knockdown, Binding Assay

    Effect of Panx1 on cell proliferation (A) Cell viability of Panx1-OE and Panx1 −/− cells. (B–D) Flow cytometry analysis of cell cycle distribution (PI staining) with the quantification of G1, S, and G2/M phases. (E) Western blot confirms β-catenin knockdown and effects on downstream proteins in Panx1-OE cells. (F and G) Flow cytometry and quantification of cell cycle distribution after β-catenin knockdown. Each panel represents an independently generated pair of stable lines, and statistical analyses are performed within each matched pair. Data are mean ± SD, statistics in (A), (D), and (G): ∗∗ p < 0.01 and ∗∗∗ p < 0.001, two-sided Student’s t test.

    Journal: iScience

    Article Title: Panx1 deficiency exacerbates GAN diet-induced obesity by destabilizing β-catenin via GSK3β

    doi: 10.1016/j.isci.2026.115098

    Figure Lengend Snippet: Effect of Panx1 on cell proliferation (A) Cell viability of Panx1-OE and Panx1 −/− cells. (B–D) Flow cytometry analysis of cell cycle distribution (PI staining) with the quantification of G1, S, and G2/M phases. (E) Western blot confirms β-catenin knockdown and effects on downstream proteins in Panx1-OE cells. (F and G) Flow cytometry and quantification of cell cycle distribution after β-catenin knockdown. Each panel represents an independently generated pair of stable lines, and statistical analyses are performed within each matched pair. Data are mean ± SD, statistics in (A), (D), and (G): ∗∗ p < 0.01 and ∗∗∗ p < 0.001, two-sided Student’s t test.

    Article Snippet: β-Catenin (D10A8) XP Rabbit mAb , Cell Signaling Technology , Cat# 8480S; RRID: AB_11127855.

    Techniques: Flow Cytometry, Staining, Western Blot, Knockdown, Generated

    Immunofluorescence staining of phospho-β-catenin (p-β-catenin, Ser 675) in mouse kidneys was performed to determine the state of phosphorus metabolism . Immunofluorescence staining of p-β-catenin at Ser675 in mouse renal tissue sections. p-β-catenin was detected using an Alexa Fluor 555-conjugated antibody ( red ); the proximal tubular marker LTL was labeled with FITC ( green ), and nuclei were counterstained with DAPI ( blue ) (N = 6). This scale bar represents 100 μm. Data were acquired using a confocal laser scanning microscope. LTL, Lotus tetragonolobus lectin.

    Journal: The Journal of Biological Chemistry

    Article Title: PKM2 inhibitor suppresses kidney fibrogenesis by disrupting YAP-TEAD-CCN2 transcriptional signaling following ischemia–reperfusion injury

    doi: 10.1016/j.jbc.2025.111029

    Figure Lengend Snippet: Immunofluorescence staining of phospho-β-catenin (p-β-catenin, Ser 675) in mouse kidneys was performed to determine the state of phosphorus metabolism . Immunofluorescence staining of p-β-catenin at Ser675 in mouse renal tissue sections. p-β-catenin was detected using an Alexa Fluor 555-conjugated antibody ( red ); the proximal tubular marker LTL was labeled with FITC ( green ), and nuclei were counterstained with DAPI ( blue ) (N = 6). This scale bar represents 100 μm. Data were acquired using a confocal laser scanning microscope. LTL, Lotus tetragonolobus lectin.

    Article Snippet: Primary antibodies against the following proteins were used: CCN2 (CTGF) (D8Z8U) (#86641; CST), phosphorylated YAP (Tyr357) (#ab62751; Abcam), YAP1 (#13584-1-AP; Proteintech), PKM2 (#15822-1-AP; Proteintech), Pan-TEAD (D3F7L) (#13295; CST), PKM1 (#15821-1-AP; Proteintech), β-catenin (D10A8) (#8480; CST), lamin B1 (#PM064MS; MBL), GAPDH (D16H11) (#5174; CST), Smad2/3 (D7G7) (#8685; CST), Phospho-Smad3 (Ser423/425) (#GT1207; GTX), and TEAD2 (#21159-1-AP; Proteintech).

    Techniques: Immunofluorescence, Staining, Marker, Labeling, Laser-Scanning Microscopy

    Immunofluorescence staining of p-β-catenin (Ser552) in mouse kidneys was performed to determine the state of phosphorus metabolism . Immunofluorescence staining of p-β-catenin at Ser552 in mouse renal tissue sections. p-β-catenin was detected using an Alexa Fluor 555-conjugated antibody ( red ); the proximal tubular marker LTL was labeled with FITC ( green ), and nuclei were counterstained with DAPI ( blue ) (N = 6). This scale bar represents 100 μm. Data were acquired using a confocal laser scanning microscope. LTL, Lotus tetragonolobus lectin.

    Journal: The Journal of Biological Chemistry

    Article Title: PKM2 inhibitor suppresses kidney fibrogenesis by disrupting YAP-TEAD-CCN2 transcriptional signaling following ischemia–reperfusion injury

    doi: 10.1016/j.jbc.2025.111029

    Figure Lengend Snippet: Immunofluorescence staining of p-β-catenin (Ser552) in mouse kidneys was performed to determine the state of phosphorus metabolism . Immunofluorescence staining of p-β-catenin at Ser552 in mouse renal tissue sections. p-β-catenin was detected using an Alexa Fluor 555-conjugated antibody ( red ); the proximal tubular marker LTL was labeled with FITC ( green ), and nuclei were counterstained with DAPI ( blue ) (N = 6). This scale bar represents 100 μm. Data were acquired using a confocal laser scanning microscope. LTL, Lotus tetragonolobus lectin.

    Article Snippet: Primary antibodies against the following proteins were used: CCN2 (CTGF) (D8Z8U) (#86641; CST), phosphorylated YAP (Tyr357) (#ab62751; Abcam), YAP1 (#13584-1-AP; Proteintech), PKM2 (#15822-1-AP; Proteintech), Pan-TEAD (D3F7L) (#13295; CST), PKM1 (#15821-1-AP; Proteintech), β-catenin (D10A8) (#8480; CST), lamin B1 (#PM064MS; MBL), GAPDH (D16H11) (#5174; CST), Smad2/3 (D7G7) (#8685; CST), Phospho-Smad3 (Ser423/425) (#GT1207; GTX), and TEAD2 (#21159-1-AP; Proteintech).

    Techniques: Immunofluorescence, Staining, Marker, Labeling, Laser-Scanning Microscopy

    Western blot analysis of cell fraction protein expression in 3k-treated and siPKM2-transfected HK-2 cells . A and B , Western blot analysis of cytoplasmic and nuclear protein fractions from 3k-treated HK-2 cells to determine β-catenin and YAP1 nuclear translocation. C and D , western blot analysis of cytoplasmic and nuclear protein fractions from siPKM2-transfected HK-2 cells to determine β-catenin and YAP1 nuclear translocation (N = 6).

    Journal: The Journal of Biological Chemistry

    Article Title: PKM2 inhibitor suppresses kidney fibrogenesis by disrupting YAP-TEAD-CCN2 transcriptional signaling following ischemia–reperfusion injury

    doi: 10.1016/j.jbc.2025.111029

    Figure Lengend Snippet: Western blot analysis of cell fraction protein expression in 3k-treated and siPKM2-transfected HK-2 cells . A and B , Western blot analysis of cytoplasmic and nuclear protein fractions from 3k-treated HK-2 cells to determine β-catenin and YAP1 nuclear translocation. C and D , western blot analysis of cytoplasmic and nuclear protein fractions from siPKM2-transfected HK-2 cells to determine β-catenin and YAP1 nuclear translocation (N = 6).

    Article Snippet: Primary antibodies against the following proteins were used: CCN2 (CTGF) (D8Z8U) (#86641; CST), phosphorylated YAP (Tyr357) (#ab62751; Abcam), YAP1 (#13584-1-AP; Proteintech), PKM2 (#15822-1-AP; Proteintech), Pan-TEAD (D3F7L) (#13295; CST), PKM1 (#15821-1-AP; Proteintech), β-catenin (D10A8) (#8480; CST), lamin B1 (#PM064MS; MBL), GAPDH (D16H11) (#5174; CST), Smad2/3 (D7G7) (#8685; CST), Phospho-Smad3 (Ser423/425) (#GT1207; GTX), and TEAD2 (#21159-1-AP; Proteintech).

    Techniques: Western Blot, Expressing, Transfection, Translocation Assay

    Western blot analysis of cross-linked protein expression and Co-IP analysis in HK-2 cells . A , western blot analysis of cross-linked proteins extracted from 3k-treated HK-2 cells. B and C , Co-IP analysis of the interaction between YAP1, β-catenin, and PKM2 in HK-2 cells. IP was performed using protein samples from HK-2 cells overexpressing CCN2. Co-IP with an anti-PKM2 antibody confirmed that both β-catenin and YAP1 co-precipitated with PKM2 (N = 6), ( D ) as illustrated in the schematic diagram. CCN2, cellular communication network factor 2.

    Journal: The Journal of Biological Chemistry

    Article Title: PKM2 inhibitor suppresses kidney fibrogenesis by disrupting YAP-TEAD-CCN2 transcriptional signaling following ischemia–reperfusion injury

    doi: 10.1016/j.jbc.2025.111029

    Figure Lengend Snippet: Western blot analysis of cross-linked protein expression and Co-IP analysis in HK-2 cells . A , western blot analysis of cross-linked proteins extracted from 3k-treated HK-2 cells. B and C , Co-IP analysis of the interaction between YAP1, β-catenin, and PKM2 in HK-2 cells. IP was performed using protein samples from HK-2 cells overexpressing CCN2. Co-IP with an anti-PKM2 antibody confirmed that both β-catenin and YAP1 co-precipitated with PKM2 (N = 6), ( D ) as illustrated in the schematic diagram. CCN2, cellular communication network factor 2.

    Article Snippet: Primary antibodies against the following proteins were used: CCN2 (CTGF) (D8Z8U) (#86641; CST), phosphorylated YAP (Tyr357) (#ab62751; Abcam), YAP1 (#13584-1-AP; Proteintech), PKM2 (#15822-1-AP; Proteintech), Pan-TEAD (D3F7L) (#13295; CST), PKM1 (#15821-1-AP; Proteintech), β-catenin (D10A8) (#8480; CST), lamin B1 (#PM064MS; MBL), GAPDH (D16H11) (#5174; CST), Smad2/3 (D7G7) (#8685; CST), Phospho-Smad3 (Ser423/425) (#GT1207; GTX), and TEAD2 (#21159-1-AP; Proteintech).

    Techniques: Western Blot, Expressing, Co-Immunoprecipitation Assay