integrin α v β 3 antibody  (Merck & Co)

Journal: Molecular Imaging and Biology

Article Title: Quantifying Molecular Changes in the Preeclamptic Rat Placenta with Targeted Contrast-Enhanced Ultrasound Imaging

doi: 10.1007/s11307-025-01988-4

Figure Lengend Snippet: Quantification methods for binding contrast agent.​ a LE method: Acoustic intensity at t = t Burst – 40 s represents attached contrast agent value. b dTE method: Schematic showing changes before (t ≈ 2 min) and after Burst (t = t Burst + 30 s). The schematic illustrates the dTE method to quantify the attached contrast agent within the placenta. After tail vein injection, MBs adhere to the α ν β 3 integrin on the endothelial cells. Ten minutes later, a destructive ultrasound pulse is applied to destroy the adherent MBs, and 1 min later, the free-circulating MBs are replenished. c BCM method: data from t = 0 ~ 2 min are fitted into the complete equation for each pixel to calculate the binding constant of the attached MBs

Article Snippet: Placental sections were incubated with mouse polyclonal α ν β 3 integrin (1:200 dilution, Bioss antibodies, bs‐1310R) and secondary HRP-polymer (Rabbit-On-Rodent HRP-polymer, Biocare Medical, Pacheco, CA).

Techniques: Binding Assay, Injection

Journal: Molecular Imaging and Biology

Article Title: Quantifying Molecular Changes in the Preeclamptic Rat Placenta with Targeted Contrast-Enhanced Ultrasound Imaging

doi: 10.1007/s11307-025-01988-4

Figure Lengend Snippet: α ν β 3 integrin expression in NP vs RUPP placentas. a IHC staining in NP placenta. b IHC staining in RUPP placenta, showing decreased intensity. c Quantification of α ν β 3 integrin protein expression. Each data point represents the mean of 3–4 slices from a single placenta from each rat subject. ( n = 4 rats; mean ± SEM; * p < 0.05). d Relative α ν β 3 mRNA levels ( n = 6 each; normalized to β-Actin; mean ± SEM; ** p < 0.01)

Article Snippet: Placental sections were incubated with mouse polyclonal α ν β 3 integrin (1:200 dilution, Bioss antibodies, bs‐1310R) and secondary HRP-polymer (Rabbit-On-Rodent HRP-polymer, Biocare Medical, Pacheco, CA).

Techniques: Expressing, Immunohistochemistry

Journal: Journal of Nanobiotechnology

Article Title: Aminolysis-mediated single-step surface functionalization of poly (butyl cyanoacrylate) microbubbles for ultrasound molecular imaging

doi: 10.1186/s12951-024-02806-9

Figure Lengend Snippet: In vitro binding of cRGD-MB to HUVEC under flow conditions. A Fluorescence images of non-stimulated (control) or TNF-α stimulated HUVEC. The nuclei, cell membrane and α v β 3 integrins were stained with DAPI (blue), wheat germ agglutinin-488 (WGA, green) and CD51/61 antibody (red), respectively. Scale bar = 50 μm. B Quantitative analysis indicating significantly higher area fraction of α v β 3 integrin in HUVEC stimulated with TNF-α. Data are represented as mean ± SD. C Schematic showing the in vitro setup of the flow chamber. Petri dishes with cultured HUVEC were connected to a flow chamber, in turn perfused with an MB solution (standard-MB, cRAD-MB, or cRGD-MB) at 0.25 mL/min. D Representative fluorescent images of the three different, rhodamine-labeled MB types binding to TNF-α stimulated HUVEC. The nuclei, cell membrane and MB were labeled with DAPI (blue), WGA (green) and rhodamine (red), respectively. Scale bar: 100 μm. E Number of bound MB per cell. cRGD-MB displayed significantly higher binding to TNF-α stimulated HUVEC compared to both controls. Data represent mean ± SD of three independent MB batches. Statistical comparisons were performed using unpaired t-tests in panel B, while for panel E comparisons were performed using one-way ANOVA. **p < 0.01 and ***p < 0.001

Article Snippet: The tumor sections were fixed with 80% methanol for 5 min at 4 °C followed by the addition of acetone at − 20 °C for 2 min. After fixation, sections were washed 3 times with PBS and incubated overnight with a rabbit anti-α v β 3 integrin antibody (1 μg/ μL; eBioscience, San Diego, California, USA) at a dilution of 1:100 at 4 °C.

Techniques: In Vitro, Binding Assay, Fluorescence, Control, Membrane, Staining, Cell Culture, Labeling

Journal: Molecular Therapy Oncology

Article Title: Conditionally replicative adenovirus as a therapy for malignant peripheral nerve sheath tumors

doi: 10.1016/j.omton.2024.200783

Figure Lengend Snippet: Adenovirus binding affinity to MPNST cell lines and viral receptor expression (A) Schematic of viral genome for Ad vectors used in binding assay. (B) Each cell line was infected with Ad vectors equipped with either WT (Ad5), RGD fiber-modified (RGD), or chimeric Ad5/Ad3 fiber (Ad5/3) at 100 VP/cell. Binding was allowed to proceed for 2 h at 4°C, then was assessed by qPCR. (C) Flow cytometry analysis of CAR and integrin expression. MPNST cell lines were incubated with fluorescent antibodies against α V β 3 and α V β 5 integrins and coxsackie adenovirus receptor (CAR). The data are shown as a relative percentage of positive cells scored among at least 10,000 cells assessed. (D) Flow cytometry plots by cell line with respective isotype control for viral entry receptors in MPNST cell lines and iHSC1 λ controls. Error bars represents ± standard deviation. ∗p < 0.05; ∗∗ p < 0.01; ∗∗∗p < 0.001; ∗∗∗∗p < 0.0001, Student's t test.

Article Snippet: Cells were plated and cultured for 24 h, non-enzymatically lifted off the plate (Sigma C5789), washed with PBS, and stained with antibodies for integrins α ν β 3 (BS-1310R-Cy3, Bioss) or immunoglobulin (Ig)G isotype control (BS-025P); α ν β 5 (565836-AF647, BD) or κ isotype control (565378-AF647, BD); and CAR (BS-2389R-A488, Bioss) or IgG Isotype control (BS-0295P-A488).

Techniques: Binding Assay, Expressing, Infection, Modification, Flow Cytometry, Incubation, Control, Standard Deviation

Journal: Frontiers in Pharmacology

Article Title: Optimizing the enzymatic release of MMAE from iso DGR-based small molecule drug conjugate by incorporation of a GPLG-PABC enzymatically cleavable linker

doi: 10.3389/fphar.2023.1215694

Figure Lengend Snippet: Flow cytometry analysis of integrin α V β 3 receptor level of expression in the four cancer cell lines used in this work.

Article Snippet: Afterwards, integrin α V β 3 antibody (Anti-Integrin α V β 3 antibody, clone LM609, mouse; MAB 1976, Merck) was used in a concentration of 3 µg/million cells, diluted in PBS and 3% BSA solution and incubated for 2 h at rt.

Techniques: Flow Cytometry, Expressing

Journal: Frontiers in Pharmacology

Article Title: Optimizing the enzymatic release of MMAE from iso DGR-based small molecule drug conjugate by incorporation of a GPLG-PABC enzymatically cleavable linker

doi: 10.3389/fphar.2023.1215694

Figure Lengend Snippet: Cell viability curves and calculated IC 50 values of cancer cell lines with different integrin α V β 3 receptor level of expression after 72 h of continuous treatment with the conjugate 2 , free drug MMAE, and free ligand. (A) U87MG. (B) SK-MEL-28. (C) SK-OV-3. (D) A549.

Article Snippet: Afterwards, integrin α V β 3 antibody (Anti-Integrin α V β 3 antibody, clone LM609, mouse; MAB 1976, Merck) was used in a concentration of 3 µg/million cells, diluted in PBS and 3% BSA solution and incubated for 2 h at rt.

Techniques: Expressing

Journal: Frontiers in Pharmacology

Article Title: Optimizing the enzymatic release of MMAE from iso DGR-based small molecule drug conjugate by incorporation of a GPLG-PABC enzymatically cleavable linker

doi: 10.3389/fphar.2023.1215694

Figure Lengend Snippet: Cell viability curves and calculated IC 50 values obtained after 30 min treatment of cancer cell lines with different integrin α V β 3 receptor level of expression with the conjugate 2 , free drug MMAE, and free ligand, followed by washout and further incubation of the cells up to 72 h (A) U87MG. (B) SK-MEL-28. (C) SK-OV-3. (D) A549.

Article Snippet: Afterwards, integrin α V β 3 antibody (Anti-Integrin α V β 3 antibody, clone LM609, mouse; MAB 1976, Merck) was used in a concentration of 3 µg/million cells, diluted in PBS and 3% BSA solution and incubated for 2 h at rt.

Techniques: Expressing, Incubation