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rabbit polyclonal abs against β 3 integrin  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc rabbit polyclonal abs against β 3 integrin
    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 <t>integrin,</t> 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.
    Rabbit Polyclonal Abs Against β 3 Integrin, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 285 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rabbit+polyclonal+abs+against+%CE%B2+3+integrin/pmc12175241-35-11-20?v=Cell+Signaling+Technology+Inc
    Average 95 stars, based on 285 article reviews
    rabbit polyclonal abs against β 3 integrin - by Bioz Stars, 2026-08
    95/100 stars

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    1) Product Images from "Kindlin-3 phosphorylation is crucial for thrombosis and hemostasis in vivo"

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

    Journal: Research and Practice in Thrombosis and Haemostasis

    doi: 10.1016/j.rpth.2025.102863

    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.
    Figure Legend 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.

    Techniques Used: 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).
    Figure Legend 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).

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



    Similar Products

    rabbit polyclonal abs against β 3 integrin  (Cell Signaling Technology Inc)
    95
    Cell Signaling Technology Inc rabbit polyclonal abs against β 3 integrin
    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 <t>integrin,</t> 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.
    Rabbit Polyclonal Abs Against β 3 Integrin, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rabbit+polyclonal+abs+against+%CE%B2+3+integrin/pmc12175241-35-11-20?v=Cell+Signaling+Technology+Inc
    Average 95 stars, based on 1 article reviews
    rabbit polyclonal abs against β 3 integrin - by Bioz Stars, 2026-08
    95/100 stars
    		  Buy from Supplier

    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