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Absolute Biotech Inc anti integrin β 3 antibody
Anti Integrin β 3 Antibody, supplied by Absolute Biotech Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/anti integrin β 3 antibody/product/Absolute Biotech Inc
Average 86 stars, based on 1 article reviews
anti integrin β 3 antibody - by Bioz Stars, 2026-06
86/100 stars

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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 <t>α</t> <t>ν</t> β 3 <t>integrin</t> 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
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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 <t>α</t> <t>ν</t> β 3 <t>integrin</t> 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
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Image Search Results


Platelet aggregation is impaired in S 485 A kindlin-3 platelets. (A) Comparison of kindlin-3 phosphorylation in wild-type (WT) and S 485 A mouse platelets. Platelet suspensions were treated with protease-activated receptor 4 (PAR4) agonist peptide for the times indicated, and incubations were terminated by the addition of 2× Laemmli sample buffer. Phosphorylated kindlin-3, total kindlin-3, β 3 integrin, talin, and actin loading control were detected on Western blots. (B) Representative traces showing the aggregation kinetics of WT and S 485 A K3 mouse platelets stimulated with 0.1 U/mL or 0.2 U/mL of thrombin. (C) Quantification of the thrombin-induced aggregation. Results are representative of 3 independent experiments, ∗ P < .001. (D) Representative trace showing the aggregation kinetics of WT and S 485 A K3 mouse platelets stimulated with a high dose of thrombin (0.5 U/mL). (E) Representative trace showing the aggregation kinetics of WT and S 485 A K3 mouse platelets stimulated with 1 mM PAR4 agonist peptide. (F) Quantification of the 1 mM PAR4 agonist-induced aggregation. Results are representative of 2 independent experiments, ∗ P < .001. (G and H) Representative traces showing the aggregation kinetics of WT and S 485 A K3 mouse platelets stimulated with U46619 and collagen. (I) Quantification of 4 μg/mL collagen-induced aggregation. Results are representative of 2 independent experiments, ∗ P < .001.

Journal: Research and Practice in Thrombosis and Haemostasis

Article Title: Kindlin-3 phosphorylation is crucial for thrombosis and hemostasis in vivo

doi: 10.1016/j.rpth.2025.102863

Figure Lengend Snippet: Platelet aggregation is impaired in S 485 A kindlin-3 platelets. (A) Comparison of kindlin-3 phosphorylation in wild-type (WT) and S 485 A mouse platelets. Platelet suspensions were treated with protease-activated receptor 4 (PAR4) agonist peptide for the times indicated, and incubations were terminated by the addition of 2× Laemmli sample buffer. Phosphorylated kindlin-3, total kindlin-3, β 3 integrin, talin, and actin loading control were detected on Western blots. (B) Representative traces showing the aggregation kinetics of WT and S 485 A K3 mouse platelets stimulated with 0.1 U/mL or 0.2 U/mL of thrombin. (C) Quantification of the thrombin-induced aggregation. Results are representative of 3 independent experiments, ∗ P < .001. (D) Representative trace showing the aggregation kinetics of WT and S 485 A K3 mouse platelets stimulated with a high dose of thrombin (0.5 U/mL). (E) Representative trace showing the aggregation kinetics of WT and S 485 A K3 mouse platelets stimulated with 1 mM PAR4 agonist peptide. (F) Quantification of the 1 mM PAR4 agonist-induced aggregation. Results are representative of 2 independent experiments, ∗ P < .001. (G and H) Representative traces showing the aggregation kinetics of WT and S 485 A K3 mouse platelets stimulated with U46619 and collagen. (I) Quantification of 4 μg/mL collagen-induced aggregation. Results are representative of 2 independent experiments, ∗ P < .001.

Article Snippet: Rabbit polyclonal antibodies (Abs) against mouse kindlin-3 were from Invitrogen (PA5-116402), rabbit polyclonal Abs against β 3 integrin were from Cell Signaling Technology (#4702), mouse mAb against talin was from Sigma Aldrich (T3287, clone 8d4), rabbit mAb against actin was from Cell Signaling Technology (#8456), rat mAb against mouse active α IIb β 3 integrin was from Emfret Analytics (M023-2, clone JON/A), and rat mAb against total α II β 3 integrin was from Emfret Analytics (M021-1, Leo.H4).

Techniques: Comparison, Phospho-proteomics, Control, Western Blot

Kindlin-3 S 485 phosphorylation is required for α IIb β 3 integrin activation in platelets. (A–D) Overlays of representative histograms of wild-type (WT; cyan) and S 485 A kindlin-3 (pink) platelets (A) unstained and (B) stained with JON/A monoclonal antibody at resting state or upon stimulation with (C) thrombin (Thr; 0.1 U/mL), (D) protease-activated receptor 4 (PAR4) agonist peptide (2.4 mM), or (E) U46619 (0.2 μg/mL). (F) Statistical comparison of data is shown in B–E. ∗ P < .001; S 485 A kindlin-3 vs WT, n = 4. (G) For total surface expression of α II β 3 integrin, platelets were stained with monoclonal antibody Leo.H4. (H) Alexa Fluor 647-labeled fibrinogen fragment D binding to S 485 A kindlin-3 platelets is reduced compared with WT platelets in response to Thr (0.1 U/mL), U46619 (0.2 μg/mL), PAR4 agonist peptide (2.4 mM), and resting platelets. (∗ P < .05; n = 6). (I) Platelet degranulation measured by the surface expression of P-selectin is the same in WT and S 485 A kindlin-3 platelets ( n = 2).

Journal: Research and Practice in Thrombosis and Haemostasis

Article Title: Kindlin-3 phosphorylation is crucial for thrombosis and hemostasis in vivo

doi: 10.1016/j.rpth.2025.102863

Figure Lengend Snippet: Kindlin-3 S 485 phosphorylation is required for α IIb β 3 integrin activation in platelets. (A–D) Overlays of representative histograms of wild-type (WT; cyan) and S 485 A kindlin-3 (pink) platelets (A) unstained and (B) stained with JON/A monoclonal antibody at resting state or upon stimulation with (C) thrombin (Thr; 0.1 U/mL), (D) protease-activated receptor 4 (PAR4) agonist peptide (2.4 mM), or (E) U46619 (0.2 μg/mL). (F) Statistical comparison of data is shown in B–E. ∗ P < .001; S 485 A kindlin-3 vs WT, n = 4. (G) For total surface expression of α II β 3 integrin, platelets were stained with monoclonal antibody Leo.H4. (H) Alexa Fluor 647-labeled fibrinogen fragment D binding to S 485 A kindlin-3 platelets is reduced compared with WT platelets in response to Thr (0.1 U/mL), U46619 (0.2 μg/mL), PAR4 agonist peptide (2.4 mM), and resting platelets. (∗ P < .05; n = 6). (I) Platelet degranulation measured by the surface expression of P-selectin is the same in WT and S 485 A kindlin-3 platelets ( n = 2).

Article Snippet: Rabbit polyclonal antibodies (Abs) against mouse kindlin-3 were from Invitrogen (PA5-116402), rabbit polyclonal Abs against β 3 integrin were from Cell Signaling Technology (#4702), mouse mAb against talin was from Sigma Aldrich (T3287, clone 8d4), rabbit mAb against actin was from Cell Signaling Technology (#8456), rat mAb against mouse active α IIb β 3 integrin was from Emfret Analytics (M023-2, clone JON/A), and rat mAb against total α II β 3 integrin was from Emfret Analytics (M021-1, Leo.H4).

Techniques: Phospho-proteomics, Activation Assay, Staining, Comparison, Expressing, Labeling, Binding Assay

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

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

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)

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