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rat anti wnt3a antibody (R&D Systems)

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R&D Systems rat anti wnt3a antibody
Rat Anti Wnt3a Antibody, supplied by R&D Systems, used in various techniques. Bioz Stars score: 92/100, based on 51 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/rat+anti+wnt3a/Wnt-3a+Antibody+(217804%2E2R)+%5BAllophycocyanin%5D/pmc05831263-212-10-13
Average 92 stars, based on 51 article reviews

rat anti wnt3a antibody - by Bioz Stars, 2026-09

92/100 stars

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Article Title: Enhanced Tumorigenic Potential of Colorectal Cancer Cells by Extracellular Sulfatases
Article Snippet: The lysate proteins were separated according to molecular mass by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDSPAGE) using a 7,5 to 10% polyacrylamide gel (Merck, Darmstadt, Germany) and transferred to polyvinylidene difluoride membranes (Merck, Darmstadt, Germany). .. The membranes were quenched for 1h with 5% non-fat dry milk in TBST buffer and then incubated overnight at 4°C with primary antibodies: goat anti-SULF1 (Santa Cruz, TX, USA), rabbit anti-SULF2 (Santa Cruz, TX, USA), rat anti-Wnt3A (R&D Systems, MA, USA), mouse anti-beta-catenin (R&D Systems, MA, USA), rabbit phospho-beta-catenin (R&D Systems, MA, USA), mouse anti-beta-actin (Santa Cruz, TX, USA), diluted in 1% bovine serum albumin (BSA) in TBST. .. Thereafter, the membranes were further incubated for 1h at room temperature with the appropriate secondary antibodies conjugated with Horseradish peroxidase (Cell Signaling, MA, USA).

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Figure 2 Expressions of miR-195-5p and Wnt3a during osteogenic differentiation of rat BMSCs. Rat BMSCs in the CORM-3 or osteogenic group were cultured in the osteogenic medium with or without 200 μΜ CORM-3, respectively. Rat BMSCs in the control group were cultured in the control medium. (A) RT-qPCR analysis of miR-195- 5p on 24 hours, normalized to U6. (B) Representative Western blot images of three independent experiments for Wnt3a protein expression at 24, 48 and 72 hours and quantitative results of Western blot images, using ImageJ software, normalized to Tubulin. The experiment was repeated for three times. Data were presented as the mean ±standard deviation (n=3). ^ P<0.05 vs control; * P<0.05 as indicated.

Journal: Drug Design, Development and Therapy

Article Title: Carbon Monoxide-Releasing Molecule-3 Enhances Osteogenic Differentiation of Rat Bone Marrow Mesenchymal Stem Cells via miR-195-5p/Wnt3a Pathway

doi: 10.2147/dddt.s367277

Figure Lengend Snippet: Figure 2 Expressions of miR-195-5p and Wnt3a during osteogenic differentiation of rat BMSCs. Rat BMSCs in the CORM-3 or osteogenic group were cultured in the osteogenic medium with or without 200 μΜ CORM-3, respectively. Rat BMSCs in the control group were cultured in the control medium. (A) RT-qPCR analysis of miR-195- 5p on 24 hours, normalized to U6. (B) Representative Western blot images of three independent experiments for Wnt3a protein expression at 24, 48 and 72 hours and quantitative results of Western blot images, using ImageJ software, normalized to Tubulin. The experiment was repeated for three times. Data were presented as the mean ±standard deviation (n=3). ^ P<0.05 vs control; * P<0.05 as indicated.

Article Snippet: After blocking with 5% non-fat milk, membranes were incubated overnight at 4°C with primary antibodies: rabbit anti-rat Runx2 monoclonal antibody (cat no., 12556s, 1:1000 dilution; Cell Signaling Technology, Inc., Danvers, MA, USA), rabbit anti-rat OPN polyclonal antibody (cat no., ab8448, 1:1000 dilution; Abcam, Cambridge, Britain), and rabbit anti-rat Wnt3a polyclonal antibody (cat no., WL0199a, 1:400 dilution; Wanleibio, Shenyang, China), respectively.

Techniques: Cell Culture, Control, Quantitative RT-PCR, Western Blot, Expressing, Software, Standard Deviation

Figure 4 miR-195-5p directly targeted Wnt3a. (A) The design of luciferase reporters with Wnt3a 3′UTR-wt or Wnt3a 3′UTR-mut, the position also showed. (B and C) Western blot images and analysis for Wnt3a protein expression in rat BMSCs after 48 hours transfection with miR-195-5p mimics or mimics NC (B), miR-195-5p inhibitor or inhibitor NC (C), using ImageJ software, normalized to Tubulin. (D) Effect of miR-195-5p mimics on luciferase activity in 293T cells transfected with either the 3′UTR-wt reporter or the 3′UTR-mut reporter for Wnt3a. The experiment was repeated for three times. Data were presented as the mean±standard deviation (n=3). ^ P<0.05 vs control; * P<0.05 as indicated.

Journal: Drug Design, Development and Therapy

Article Title: Carbon Monoxide-Releasing Molecule-3 Enhances Osteogenic Differentiation of Rat Bone Marrow Mesenchymal Stem Cells via miR-195-5p/Wnt3a Pathway

doi: 10.2147/dddt.s367277

Figure Lengend Snippet: Figure 4 miR-195-5p directly targeted Wnt3a. (A) The design of luciferase reporters with Wnt3a 3′UTR-wt or Wnt3a 3′UTR-mut, the position also showed. (B and C) Western blot images and analysis for Wnt3a protein expression in rat BMSCs after 48 hours transfection with miR-195-5p mimics or mimics NC (B), miR-195-5p inhibitor or inhibitor NC (C), using ImageJ software, normalized to Tubulin. (D) Effect of miR-195-5p mimics on luciferase activity in 293T cells transfected with either the 3′UTR-wt reporter or the 3′UTR-mut reporter for Wnt3a. The experiment was repeated for three times. Data were presented as the mean±standard deviation (n=3). ^ P<0.05 vs control; * P<0.05 as indicated.

Techniques: Luciferase, Western Blot, Expressing, Transfection, Software, Activity Assay, Standard Deviation, Control

Figure 5 CORM-3-stimulated osteogenic differentiation of rat BMSCs was modified by up- or down-regulation of Wnt3a. (A) The rat BMSCs were transfected with pcDNA3.1-Wnt3a and Wnt3a siRNA. 24 hours after transfection, the cell viabilities were measured. After 48 hours, the protein expressions of Wnt3a were determined by Western blot and image analysis. (B and C) The rat BMSCs were transfected with pcDNA3.1-Wnt3a or NC (B), Wnt3a siRNA or NC (C) for 24 hours and then cultured in the osteogenic medium containing 200 μΜ CORM-3. Meanwhile, cells in the CORM-3 or control group were cultured in the osteogenic medium containing 200 μΜ CORM- 3 or control medium respectively. After 3 and 7 days, the mRNA expressions of Runx2 and OPN were determined by RT-qPCR, normalized to β-actin. (D and E) The rat BMSCs were cultured as B and C described above. After 3 and 7 days, the protein expressions of Runx2 and OPN were determined by Western blot, then analysed using ImageJ software, normalized to GAPDH. (F) The rat BMSCs were cultured in different mediums as described above. After 14 days, the mineralization was determined by alizarin red staining and semi quantitative analysis. The experiment was repeated for three times. Data were presented as the mean±standard deviation (n=3). ^ P<0.05 vs control; * P<0.05 as indicated.

Journal: Drug Design, Development and Therapy

Article Title: Carbon Monoxide-Releasing Molecule-3 Enhances Osteogenic Differentiation of Rat Bone Marrow Mesenchymal Stem Cells via miR-195-5p/Wnt3a Pathway

doi: 10.2147/dddt.s367277

Figure Lengend Snippet: Figure 5 CORM-3-stimulated osteogenic differentiation of rat BMSCs was modified by up- or down-regulation of Wnt3a. (A) The rat BMSCs were transfected with pcDNA3.1-Wnt3a and Wnt3a siRNA. 24 hours after transfection, the cell viabilities were measured. After 48 hours, the protein expressions of Wnt3a were determined by Western blot and image analysis. (B and C) The rat BMSCs were transfected with pcDNA3.1-Wnt3a or NC (B), Wnt3a siRNA or NC (C) for 24 hours and then cultured in the osteogenic medium containing 200 μΜ CORM-3. Meanwhile, cells in the CORM-3 or control group were cultured in the osteogenic medium containing 200 μΜ CORM- 3 or control medium respectively. After 3 and 7 days, the mRNA expressions of Runx2 and OPN were determined by RT-qPCR, normalized to β-actin. (D and E) The rat BMSCs were cultured as B and C described above. After 3 and 7 days, the protein expressions of Runx2 and OPN were determined by Western blot, then analysed using ImageJ software, normalized to GAPDH. (F) The rat BMSCs were cultured in different mediums as described above. After 14 days, the mineralization was determined by alizarin red staining and semi quantitative analysis. The experiment was repeated for three times. Data were presented as the mean±standard deviation (n=3). ^ P<0.05 vs control; * P<0.05 as indicated.

Techniques: Modification, Transfection, Western Blot, Cell Culture, Control, Quantitative RT-PCR, Software, Staining, Standard Deviation

Figure 6 Decreased osteogenic differentiation capacity by miR-195-5p up-regulation was rescued with Wnt3a overexpression. (A) The rat BMSCs were co-transfected with miR-195-5p mimics and pcDNA3.1-Wnt3a, miR-195-5p mimics and NC for 24 hours and then cultured in the osteogenic medium containing 200 μΜ CORM-3. Meanwhile, cells in the CORM-3 or control group were cultured in the osteogenic medium containing 200 μΜ CORM-3 or control medium respectively. After 3 and 7 days, the mRNA expressions of Runx2 and OPN were determined by RT-qPCR, normalized to β-actin. (B) The rat BMSCs were cultured in different mediums as described above. After 3 and 7 days, the protein expressions of Runx2 and OPN were determined by Western blot, then analysed using ImageJ software, normalized to GAPDH. (C) The rat BMSCs were cultured in different mediums as described above. After 14 days, the mineralization was determined by alizarin red staining and semi quantitative analysis. The experiment was repeated for three times. Data were presented as the mean±standard deviation (n=3). ^ P<0.05 vs control; * P<0.05 as indicated.

Journal: Drug Design, Development and Therapy

Article Title: Carbon Monoxide-Releasing Molecule-3 Enhances Osteogenic Differentiation of Rat Bone Marrow Mesenchymal Stem Cells via miR-195-5p/Wnt3a Pathway

doi: 10.2147/dddt.s367277

Figure Lengend Snippet: Figure 6 Decreased osteogenic differentiation capacity by miR-195-5p up-regulation was rescued with Wnt3a overexpression. (A) The rat BMSCs were co-transfected with miR-195-5p mimics and pcDNA3.1-Wnt3a, miR-195-5p mimics and NC for 24 hours and then cultured in the osteogenic medium containing 200 μΜ CORM-3. Meanwhile, cells in the CORM-3 or control group were cultured in the osteogenic medium containing 200 μΜ CORM-3 or control medium respectively. After 3 and 7 days, the mRNA expressions of Runx2 and OPN were determined by RT-qPCR, normalized to β-actin. (B) The rat BMSCs were cultured in different mediums as described above. After 3 and 7 days, the protein expressions of Runx2 and OPN were determined by Western blot, then analysed using ImageJ software, normalized to GAPDH. (C) The rat BMSCs were cultured in different mediums as described above. After 14 days, the mineralization was determined by alizarin red staining and semi quantitative analysis. The experiment was repeated for three times. Data were presented as the mean±standard deviation (n=3). ^ P<0.05 vs control; * P<0.05 as indicated.

Techniques: Over Expression, Transfection, Cell Culture, Control, Quantitative RT-PCR, Western Blot, Software, Staining, Standard Deviation

( A ) ELISA measurements of Wnt3a and DKK4 secretory proteins in culture media collected after 16 hr from HepG2 cells in NG, HG and HG + CytoB. ( B ) HepG2 and SK-HEP-1 cells were cultured in NG, HG and HG + CytoB for 16 hr. Whole cell lysates were subjected to western blotting and levels of Wnt3a and DKK4 proteins were detected. ( C ) HepG2 cells were cultured in NG, HG and HG + CytoB for 16 hr. Total RNA was isolated and cDNA was prepared to determine relative mRNA fold expression of DKK4 by quantitative real-time RT-PCR. ( D ) HepG2 cells were cultured in HG for 16 hr and then allowed to grow in medium without glucose for indicated time course. Whole cell lysates were prepared for detection of DKK4 protein by western blotting. All the bar graphs represent the mean ± SD of an experiment done in triplicate (*P < 0.05, **P < 0.001, ***P < 0.0001). Cropped blots are used in the main figure and full length blots are included in .

Journal: Scientific Reports

Article Title: Glucose induced activation of canonical Wnt signaling pathway in hepatocellular carcinoma is regulated by DKK4

doi: 10.1038/srep27558

Figure Lengend Snippet: ( A ) ELISA measurements of Wnt3a and DKK4 secretory proteins in culture media collected after 16 hr from HepG2 cells in NG, HG and HG + CytoB. ( B ) HepG2 and SK-HEP-1 cells were cultured in NG, HG and HG + CytoB for 16 hr. Whole cell lysates were subjected to western blotting and levels of Wnt3a and DKK4 proteins were detected. ( C ) HepG2 cells were cultured in NG, HG and HG + CytoB for 16 hr. Total RNA was isolated and cDNA was prepared to determine relative mRNA fold expression of DKK4 by quantitative real-time RT-PCR. ( D ) HepG2 cells were cultured in HG for 16 hr and then allowed to grow in medium without glucose for indicated time course. Whole cell lysates were prepared for detection of DKK4 protein by western blotting. All the bar graphs represent the mean ± SD of an experiment done in triplicate (*P < 0.05, **P < 0.001, ***P < 0.0001). Cropped blots are used in the main figure and full length blots are included in .

Article Snippet: Antibodies against DKK4 (sc-25519), GLUT-1 (sc-7903), GLUT-2 (sc-9117), Cyclin D1(sc-717), CDK4 (sc-260), CDK6 (sc-7181), c-Myc (sc-764), Wnt3a (sc-28824), pJNK (sc-6254), JNK (sc-474), pMEK (sc-7995), MEK (sc-13069), Raf (sc-227), pERK (sc-7383), ERK (sc-154), pAkt (sc-7985), AKT (sc-8312), GSK3β (sc-9166), β-tubulin (sc-9104) and Histone H1 (sc-10806), HRP-conjugated (sc-2004), (sc-2031), (sc-2033), FITC conjugated (sc-3839) and Rhodamine conjugated (sc-358922) antibodies were purchased from Santa Cruz Biotechnology (Santa Cruz Biotechnology, CA, USA).

Techniques: Enzyme-linked Immunosorbent Assay, Cell Culture, Western Blot, Isolation, Expressing, Quantitative RT-PCR

( A ) Normoglycemic glucose promotes sustained expression of DKK4 protein. DKK4 antagonizes activation of canonical Wnt signaling by facilitating degradation of β–catenin in cytosol and thus reducing its transcriptional activation thereby causing decrease c-Myc level. Increased DKK4 expression affects progression of cells at S-phase of cell cycle and therefore limits proliferation of HCC cells. ( B ) High glucose diminishes DKK4 expression allowing activation of canonical Wnt signaling because of inactivation of β–catenin degradation complex, by Wnt3a proteins. Increase in β–catenin level enhances its transcriptional activity and promotes c-Myc expression which causes uncontrolled proliferation of HCC cells.

Journal: Scientific Reports

Article Title: Glucose induced activation of canonical Wnt signaling pathway in hepatocellular carcinoma is regulated by DKK4

doi: 10.1038/srep27558

Figure Lengend Snippet: ( A ) Normoglycemic glucose promotes sustained expression of DKK4 protein. DKK4 antagonizes activation of canonical Wnt signaling by facilitating degradation of β–catenin in cytosol and thus reducing its transcriptional activation thereby causing decrease c-Myc level. Increased DKK4 expression affects progression of cells at S-phase of cell cycle and therefore limits proliferation of HCC cells. ( B ) High glucose diminishes DKK4 expression allowing activation of canonical Wnt signaling because of inactivation of β–catenin degradation complex, by Wnt3a proteins. Increase in β–catenin level enhances its transcriptional activity and promotes c-Myc expression which causes uncontrolled proliferation of HCC cells.

Techniques: Expressing, Activation Assay, Activity Assay

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rat anti wnt3a antibody (R&D Systems)

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