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antibody against vdbp rabbit  (Proteintech)


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    Structured Review

    Proteintech antibody against vdbp rabbit
    Antibody Against Vdbp Rabbit, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/anti+vdbp/Vitamin+D+binding+protein+Antibody/pm39332774-99-2-9
    Average 93 stars, based on 16 article reviews
    antibody against vdbp rabbit - by Bioz Stars, 2026-10
    93/100 stars

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    Related Articles

    Membrane:

    Article Title: Vitamin D-binding protein in plasma microglia-derived extracellular vesicles as a potential biomarker for major depressive disorder
    Article Snippet: The proteins in the lysate were separated by SDS-PAGE gels (GenScript, Nanjing, China), and transferred into a PVDF membrane (ISEQ00010, Millipore, Darmstadt, Germany). .. The membrane was blocked with 5% skimmed milk at room temperature for 1 h, and then incubated with the following primary antibody overnight at 4 °C: Anti-Alix (1:1000, ab275377, Abcam, Cambridge, UK), anti-L1CAM (1:1000, ab208155, Abcam, Cambridge, UK), anti-TMEM119 (1:1000, A20287, ABclonal, Wuhan, China), anti-GLAST (1:1000, ab181036, Abcam, Cambridge, UK), anti-VDBP (16922-1-AP, Proteintech, Rosemont, IL). .. Next, the membrane was incubated with goat anti-rabbit secondary antibody or goat anti-mouse secondary antibody (Abcam, Cambridge, UK), depending on the source of the primary antibody, at room temperature for 1 h. The blots were visualized using the chemiluminescent reagent (E412, Vazyme, Nanjing, China) under a chemiluminescence image analysis system (Tanon4600, China).

    Article Title: Vitamin D-binding protein in plasma microglia-derived extracellular vesicles as a potential biomarker for major depressive disorder.
    Article Snippet: The proteins in the lysate were separated by SDS-PAGE gels (GenScript, Nanjing, China), and transferred into a PVDF membrane (ISEQ00010, Millipore, Darmstadt, Germany). .. The membrane was blocked with 5% skimmed milk at room temperature for 1 h, and then incubated with the following primary antibody overnight at 4 C: Anti-Alix (1:1000, ab275377, Abcam, Cambridge, UK), anti-L1CAM (1:1000, ab208155, Abcam, Cambridge, UK), anti-TMEM119 (1:1000, A20287, ABclonal, Wuhan, China), anti-GLAST (1:1000, ab181036, Abcam, Cambridge, UK), anti-VDBP (16922-1-AP, Proteintech, Rosemont, IL). .. Next, the membrane was incubated with goat anti-rabbit secondary antibody or goat anti-mouse secondary antibody (Abcam, Cambridge, UK), depending on the source of the primary antibody, at room temperature for 1 h. The blots were visualized using the chemiluminescent reagent (E412, Vazyme, Nanjing, China) under a chemiluminescence image analysis system (Tanon4600, China).

    Incubation:

    Article Title: Vitamin D-binding protein in plasma microglia-derived extracellular vesicles as a potential biomarker for major depressive disorder
    Article Snippet: The proteins in the lysate were separated by SDS-PAGE gels (GenScript, Nanjing, China), and transferred into a PVDF membrane (ISEQ00010, Millipore, Darmstadt, Germany). .. The membrane was blocked with 5% skimmed milk at room temperature for 1 h, and then incubated with the following primary antibody overnight at 4 °C: Anti-Alix (1:1000, ab275377, Abcam, Cambridge, UK), anti-L1CAM (1:1000, ab208155, Abcam, Cambridge, UK), anti-TMEM119 (1:1000, A20287, ABclonal, Wuhan, China), anti-GLAST (1:1000, ab181036, Abcam, Cambridge, UK), anti-VDBP (16922-1-AP, Proteintech, Rosemont, IL). .. Next, the membrane was incubated with goat anti-rabbit secondary antibody or goat anti-mouse secondary antibody (Abcam, Cambridge, UK), depending on the source of the primary antibody, at room temperature for 1 h. The blots were visualized using the chemiluminescent reagent (E412, Vazyme, Nanjing, China) under a chemiluminescence image analysis system (Tanon4600, China).

    Article Title: Vitamin D-binding protein in plasma microglia-derived extracellular vesicles as a potential biomarker for major depressive disorder.
    Article Snippet: The proteins in the lysate were separated by SDS-PAGE gels (GenScript, Nanjing, China), and transferred into a PVDF membrane (ISEQ00010, Millipore, Darmstadt, Germany). .. The membrane was blocked with 5% skimmed milk at room temperature for 1 h, and then incubated with the following primary antibody overnight at 4 C: Anti-Alix (1:1000, ab275377, Abcam, Cambridge, UK), anti-L1CAM (1:1000, ab208155, Abcam, Cambridge, UK), anti-TMEM119 (1:1000, A20287, ABclonal, Wuhan, China), anti-GLAST (1:1000, ab181036, Abcam, Cambridge, UK), anti-VDBP (16922-1-AP, Proteintech, Rosemont, IL). .. Next, the membrane was incubated with goat anti-rabbit secondary antibody or goat anti-mouse secondary antibody (Abcam, Cambridge, UK), depending on the source of the primary antibody, at room temperature for 1 h. The blots were visualized using the chemiluminescent reagent (E412, Vazyme, Nanjing, China) under a chemiluminescence image analysis system (Tanon4600, China).



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    ZSO inhibits high glucose-induced vascular endothelial cell senescence and calcification through downregulating <t>VDBP</t> protein levels. (A) Endothelial cells were treated with high glucose (30 mM) and various concentrations of ZSO (1, 5, 10 μM) for 24 h. RT-qPCR was then performed to quantify VDBP mRNA level, and the results were statistically analyzed. (B) Endothelial cells were treated with DOM and various concentrations of ZSO (1, 5, 10 μM) for 4 days. RT-qPCR was then performed to quantify VDBP mRNA level, and the results were statistically analyzed. (C) Endothelial cells were treated with high glucose (30 mM) and ZSO (5 μM) for 24 h, followed by Western blot analysis of VDBP protein level. (D) Statistical analysis of VDBP protein level under senescence conditions. (E) Endothelial cells were treated with 5 μM ZSO under calcification-inducing conditions for 4 days, followed by Western blot analysis of VDBP protein level. (F) Quantitative analysis of VDBP protein level under calcification conditions. (G) Immunohistochemical staining of VDBP in mouse thoracic aorta sections, with brown coloration indicating positive immunoreactivity. (H) Quantitative analysis of VDBP-positive staining intensity in vascular tissues, with corresponding statistical graphs. (I) Measurement of VDBP protein level in mouse serum using an ELISA kit, followed by statistical analysis. (J) Endothelial cells were treated with high glucose (30 mM) and 5 μM ZSO for 24 h, and <t>the</t> <t>ubiquitination</t> level of VDBP was assessed. (K) Quantification of VDBP ubiquitination level. ns p > 0.05, *p < 0.05, **p < 0.01, n = 3.
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    ZSO inhibits high glucose-induced vascular endothelial cell senescence and calcification through downregulating <t>VDBP</t> protein levels. (A) Endothelial cells were treated with high glucose (30 mM) and various concentrations of ZSO (1, 5, 10 μM) for 24 h. RT-qPCR was then performed to quantify VDBP mRNA level, and the results were statistically analyzed. (B) Endothelial cells were treated with DOM and various concentrations of ZSO (1, 5, 10 μM) for 4 days. RT-qPCR was then performed to quantify VDBP mRNA level, and the results were statistically analyzed. (C) Endothelial cells were treated with high glucose (30 mM) and ZSO (5 μM) for 24 h, followed by Western blot analysis of VDBP protein level. (D) Statistical analysis of VDBP protein level under senescence conditions. (E) Endothelial cells were treated with 5 μM ZSO under calcification-inducing conditions for 4 days, followed by Western blot analysis of VDBP protein level. (F) Quantitative analysis of VDBP protein level under calcification conditions. (G) Immunohistochemical staining of VDBP in mouse thoracic aorta sections, with brown coloration indicating positive immunoreactivity. (H) Quantitative analysis of VDBP-positive staining intensity in vascular tissues, with corresponding statistical graphs. (I) Measurement of VDBP protein level in mouse serum using an ELISA kit, followed by statistical analysis. (J) Endothelial cells were treated with high glucose (30 mM) and 5 μM ZSO for 24 h, and <t>the</t> <t>ubiquitination</t> level of VDBP was assessed. (K) Quantification of VDBP ubiquitination level. ns p > 0.05, *p < 0.05, **p < 0.01, n = 3.
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    ZSO inhibits high glucose-induced vascular endothelial cell senescence and calcification through downregulating <t>VDBP</t> protein levels. (A) Endothelial cells were treated with high glucose (30 mM) and various concentrations of ZSO (1, 5, 10 μM) for 24 h. RT-qPCR was then performed to quantify VDBP mRNA level, and the results were statistically analyzed. (B) Endothelial cells were treated with DOM and various concentrations of ZSO (1, 5, 10 μM) for 4 days. RT-qPCR was then performed to quantify VDBP mRNA level, and the results were statistically analyzed. (C) Endothelial cells were treated with high glucose (30 mM) and ZSO (5 μM) for 24 h, followed by Western blot analysis of VDBP protein level. (D) Statistical analysis of VDBP protein level under senescence conditions. (E) Endothelial cells were treated with 5 μM ZSO under calcification-inducing conditions for 4 days, followed by Western blot analysis of VDBP protein level. (F) Quantitative analysis of VDBP protein level under calcification conditions. (G) Immunohistochemical staining of VDBP in mouse thoracic aorta sections, with brown coloration indicating positive immunoreactivity. (H) Quantitative analysis of VDBP-positive staining intensity in vascular tissues, with corresponding statistical graphs. (I) Measurement of VDBP protein level in mouse serum using an ELISA kit, followed by statistical analysis. (J) Endothelial cells were treated with high glucose (30 mM) and 5 μM ZSO for 24 h, and <t>the</t> <t>ubiquitination</t> level of VDBP was assessed. (K) Quantification of VDBP ubiquitination level. ns p > 0.05, *p < 0.05, **p < 0.01, n = 3.
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    Proteintech antibody against vdbp rabbit
    ZSO inhibits high glucose-induced vascular endothelial cell senescence and calcification through downregulating <t>VDBP</t> protein levels. (A) Endothelial cells were treated with high glucose (30 mM) and various concentrations of ZSO (1, 5, 10 μM) for 24 h. RT-qPCR was then performed to quantify VDBP mRNA level, and the results were statistically analyzed. (B) Endothelial cells were treated with DOM and various concentrations of ZSO (1, 5, 10 μM) for 4 days. RT-qPCR was then performed to quantify VDBP mRNA level, and the results were statistically analyzed. (C) Endothelial cells were treated with high glucose (30 mM) and ZSO (5 μM) for 24 h, followed by Western blot analysis of VDBP protein level. (D) Statistical analysis of VDBP protein level under senescence conditions. (E) Endothelial cells were treated with 5 μM ZSO under calcification-inducing conditions for 4 days, followed by Western blot analysis of VDBP protein level. (F) Quantitative analysis of VDBP protein level under calcification conditions. (G) Immunohistochemical staining of VDBP in mouse thoracic aorta sections, with brown coloration indicating positive immunoreactivity. (H) Quantitative analysis of VDBP-positive staining intensity in vascular tissues, with corresponding statistical graphs. (I) Measurement of VDBP protein level in mouse serum using an ELISA kit, followed by statistical analysis. (J) Endothelial cells were treated with high glucose (30 mM) and 5 μM ZSO for 24 h, and <t>the</t> <t>ubiquitination</t> level of VDBP was assessed. (K) Quantification of VDBP ubiquitination level. ns p > 0.05, *p < 0.05, **p < 0.01, n = 3.
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    Proteintech antibodies against vdbp
    The <t>VDBP</t> expression in injured alveolar epithelial cells. ( A ) The VDBP protein level in LPS-induced injury of alveolar epithelial cells at different time points. The representative Western blot results and the relative expression of VDBP from the Western blot were shown. ( B ) The VDBP gene expression in the LPS-induced injury of alveolar epithelial cells. The q-PCR was used to analyze the relative expression of genes. Columns and error bars represented mean ± SEM. ** P < 0.01, *** P < 0.001. VDBP: Vitamin D-binding protein, LPS: Lipopolysaccharide, NC: negative <t>control,</t> <t>GAPDH:</t> glyceraldehyde-3-phosphate dehydrogenase.
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    Proteintech anti vdbp
    The <t>VDBP</t> expression in injured alveolar epithelial cells. ( A ) The VDBP protein level in LPS-induced injury of alveolar epithelial cells at different time points. The representative Western blot results and the relative expression of VDBP from the Western blot were shown. ( B ) The VDBP gene expression in the LPS-induced injury of alveolar epithelial cells. The q-PCR was used to analyze the relative expression of genes. Columns and error bars represented mean ± SEM. ** P < 0.01, *** P < 0.001. VDBP: Vitamin D-binding protein, LPS: Lipopolysaccharide, NC: negative <t>control,</t> <t>GAPDH:</t> glyceraldehyde-3-phosphate dehydrogenase.
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    Image Search Results


    ZSO inhibits high glucose-induced vascular endothelial cell senescence and calcification through downregulating VDBP protein levels. (A) Endothelial cells were treated with high glucose (30 mM) and various concentrations of ZSO (1, 5, 10 μM) for 24 h. RT-qPCR was then performed to quantify VDBP mRNA level, and the results were statistically analyzed. (B) Endothelial cells were treated with DOM and various concentrations of ZSO (1, 5, 10 μM) for 4 days. RT-qPCR was then performed to quantify VDBP mRNA level, and the results were statistically analyzed. (C) Endothelial cells were treated with high glucose (30 mM) and ZSO (5 μM) for 24 h, followed by Western blot analysis of VDBP protein level. (D) Statistical analysis of VDBP protein level under senescence conditions. (E) Endothelial cells were treated with 5 μM ZSO under calcification-inducing conditions for 4 days, followed by Western blot analysis of VDBP protein level. (F) Quantitative analysis of VDBP protein level under calcification conditions. (G) Immunohistochemical staining of VDBP in mouse thoracic aorta sections, with brown coloration indicating positive immunoreactivity. (H) Quantitative analysis of VDBP-positive staining intensity in vascular tissues, with corresponding statistical graphs. (I) Measurement of VDBP protein level in mouse serum using an ELISA kit, followed by statistical analysis. (J) Endothelial cells were treated with high glucose (30 mM) and 5 μM ZSO for 24 h, and the ubiquitination level of VDBP was assessed. (K) Quantification of VDBP ubiquitination level. ns p > 0.05, *p < 0.05, **p < 0.01, n = 3.

    Journal: Frontiers in Physiology

    Article Title: A new SO 2 probe ZSO targeting VDBP inhibits high glucose induced endothelial cell senescence and calcification

    doi: 10.3389/fphys.2025.1719853

    Figure Lengend Snippet: ZSO inhibits high glucose-induced vascular endothelial cell senescence and calcification through downregulating VDBP protein levels. (A) Endothelial cells were treated with high glucose (30 mM) and various concentrations of ZSO (1, 5, 10 μM) for 24 h. RT-qPCR was then performed to quantify VDBP mRNA level, and the results were statistically analyzed. (B) Endothelial cells were treated with DOM and various concentrations of ZSO (1, 5, 10 μM) for 4 days. RT-qPCR was then performed to quantify VDBP mRNA level, and the results were statistically analyzed. (C) Endothelial cells were treated with high glucose (30 mM) and ZSO (5 μM) for 24 h, followed by Western blot analysis of VDBP protein level. (D) Statistical analysis of VDBP protein level under senescence conditions. (E) Endothelial cells were treated with 5 μM ZSO under calcification-inducing conditions for 4 days, followed by Western blot analysis of VDBP protein level. (F) Quantitative analysis of VDBP protein level under calcification conditions. (G) Immunohistochemical staining of VDBP in mouse thoracic aorta sections, with brown coloration indicating positive immunoreactivity. (H) Quantitative analysis of VDBP-positive staining intensity in vascular tissues, with corresponding statistical graphs. (I) Measurement of VDBP protein level in mouse serum using an ELISA kit, followed by statistical analysis. (J) Endothelial cells were treated with high glucose (30 mM) and 5 μM ZSO for 24 h, and the ubiquitination level of VDBP was assessed. (K) Quantification of VDBP ubiquitination level. ns p > 0.05, *p < 0.05, **p < 0.01, n = 3.

    Article Snippet: Beads were washed, and Western blot was used for detection, first incubated with ubiquitination antibody (Abcam, ab137031), developed, and then incubated with VDBP antibody (Santa Cruz, sc-365441) and developed.

    Techniques: Quantitative RT-PCR, Western Blot, Immunohistochemical staining, Staining, Enzyme-linked Immunosorbent Assay, Ubiquitin Proteomics

    The VDBP expression in injured alveolar epithelial cells. ( A ) The VDBP protein level in LPS-induced injury of alveolar epithelial cells at different time points. The representative Western blot results and the relative expression of VDBP from the Western blot were shown. ( B ) The VDBP gene expression in the LPS-induced injury of alveolar epithelial cells. The q-PCR was used to analyze the relative expression of genes. Columns and error bars represented mean ± SEM. ** P < 0.01, *** P < 0.001. VDBP: Vitamin D-binding protein, LPS: Lipopolysaccharide, NC: negative control, GAPDH: glyceraldehyde-3-phosphate dehydrogenase.

    Journal: Journal of Inflammation Research

    Article Title: Vitamin D Binding Protein: A Potential Factor in Geriatric COVID-19 Acute Lung Injury

    doi: 10.2147/JIR.S470097

    Figure Lengend Snippet: The VDBP expression in injured alveolar epithelial cells. ( A ) The VDBP protein level in LPS-induced injury of alveolar epithelial cells at different time points. The representative Western blot results and the relative expression of VDBP from the Western blot were shown. ( B ) The VDBP gene expression in the LPS-induced injury of alveolar epithelial cells. The q-PCR was used to analyze the relative expression of genes. Columns and error bars represented mean ± SEM. ** P < 0.01, *** P < 0.001. VDBP: Vitamin D-binding protein, LPS: Lipopolysaccharide, NC: negative control, GAPDH: glyceraldehyde-3-phosphate dehydrogenase.

    Article Snippet: Then separate equal amounts of proteins on 12% SDS-PAGE for Western blot using antibodies against VDBP (1:2000 dilution, Proteintech, US) and GAPDH (1:5000 dilution, Proteintech, US), the protein was observed using the ECL chemiluminescence method.

    Techniques: Expressing, Western Blot, Gene Expression, Binding Assay, Negative Control