antithrombin iii Search Results


92
Novus Biologicals anti serpin c1 antithrombin iii
Anti Serpin C1 Antithrombin Iii, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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R&D Systems anti thrombin iii
Anti Thrombin Iii, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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OriGene human antithrombin iii at3 gene
Human Antithrombin Iii At3 Gene, supplied by OriGene, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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R&D Systems detection antibody
Detection Antibody, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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R&D Systems serpinc1
Serpinc1, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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R&D Systems human serpin c1 at iii ab
Human Serpin C1 At Iii Ab, supplied by R&D Systems, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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OriGene antithrombin antibody
Fig. 5. Markers of coagulation and fibrinolysis system. Markers of coagulation and fibrinolysis systems were measured in bronchoalveolar lavage fluid using commercial enzyme immunoassay kits in wild-type mice treated with saline (WT/SAL, n ¼ 15) or monocrotaline (WT/MCT, n ¼ 13) and in protein C inhibitor transgenic mice treated with saline (TG/SAL, n ¼ 8) or monocrotaline (TG/MCT, n ¼ 11). (A) The level of thrombin– <t>antithrombin</t> complex was significantly different between WT/SAL and WT/MCT, between TG/SAL and TG/MCT, and between WT/MCT and TG/MCT mice. (B) The level of plasminogen activator inhibitor-1 was significantly different between WT/SAL and WT/MCT mice, and between TG/SAL and TG/MCT mice, but not between WT/MCT and TG/MCT mice or between WT/SAL and TG/SAL mice. (C) The level of tissue-type plasminogen activator was significantly different between WT/MCT and TG/MCT mice but not between WT/SAL and WT/MCT, TG/SAL and TG/MCT or WT/SAL and TG/SAL mice. Samples were tested in dupli- cate. Bars represent the means ± SEM. Statistical analysis was performed by ANOVA with Fisher’s predicted least significant difference test.
Antithrombin Antibody, supplied by OriGene, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/antithrombin+iii/pm17059470-70-10-12?v=OriGene
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R&D Systems serpin c1 cat 1267 pi 010 were purchased
Fig. 5. Markers of coagulation and fibrinolysis system. Markers of coagulation and fibrinolysis systems were measured in bronchoalveolar lavage fluid using commercial enzyme immunoassay kits in wild-type mice treated with saline (WT/SAL, n ¼ 15) or monocrotaline (WT/MCT, n ¼ 13) and in protein C inhibitor transgenic mice treated with saline (TG/SAL, n ¼ 8) or monocrotaline (TG/MCT, n ¼ 11). (A) The level of thrombin– <t>antithrombin</t> complex was significantly different between WT/SAL and WT/MCT, between TG/SAL and TG/MCT, and between WT/MCT and TG/MCT mice. (B) The level of plasminogen activator inhibitor-1 was significantly different between WT/SAL and WT/MCT mice, and between TG/SAL and TG/MCT mice, but not between WT/MCT and TG/MCT mice or between WT/SAL and TG/SAL mice. (C) The level of tissue-type plasminogen activator was significantly different between WT/MCT and TG/MCT mice but not between WT/SAL and WT/MCT, TG/SAL and TG/MCT or WT/SAL and TG/SAL mice. Samples were tested in dupli- cate. Bars represent the means ± SEM. Statistical analysis was performed by ANOVA with Fisher’s predicted least significant difference test.
Serpin C1 Cat 1267 Pi 010 Were Purchased, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Rockland Immunochemicals dog fab
Fig. 5. Markers of coagulation and fibrinolysis system. Markers of coagulation and fibrinolysis systems were measured in bronchoalveolar lavage fluid using commercial enzyme immunoassay kits in wild-type mice treated with saline (WT/SAL, n ¼ 15) or monocrotaline (WT/MCT, n ¼ 13) and in protein C inhibitor transgenic mice treated with saline (TG/SAL, n ¼ 8) or monocrotaline (TG/MCT, n ¼ 11). (A) The level of thrombin– <t>antithrombin</t> complex was significantly different between WT/SAL and WT/MCT, between TG/SAL and TG/MCT, and between WT/MCT and TG/MCT mice. (B) The level of plasminogen activator inhibitor-1 was significantly different between WT/SAL and WT/MCT mice, and between TG/SAL and TG/MCT mice, but not between WT/MCT and TG/MCT mice or between WT/SAL and TG/SAL mice. (C) The level of tissue-type plasminogen activator was significantly different between WT/MCT and TG/MCT mice but not between WT/SAL and WT/MCT, TG/SAL and TG/MCT or WT/SAL and TG/SAL mice. Samples were tested in dupli- cate. Bars represent the means ± SEM. Statistical analysis was performed by ANOVA with Fisher’s predicted least significant difference test.
Dog Fab, supplied by Rockland Immunochemicals, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Novus Biologicals nbp2
Fig. 5. Markers of coagulation and fibrinolysis system. Markers of coagulation and fibrinolysis systems were measured in bronchoalveolar lavage fluid using commercial enzyme immunoassay kits in wild-type mice treated with saline (WT/SAL, n ¼ 15) or monocrotaline (WT/MCT, n ¼ 13) and in protein C inhibitor transgenic mice treated with saline (TG/SAL, n ¼ 8) or monocrotaline (TG/MCT, n ¼ 11). (A) The level of thrombin– <t>antithrombin</t> complex was significantly different between WT/SAL and WT/MCT, between TG/SAL and TG/MCT, and between WT/MCT and TG/MCT mice. (B) The level of plasminogen activator inhibitor-1 was significantly different between WT/SAL and WT/MCT mice, and between TG/SAL and TG/MCT mice, but not between WT/MCT and TG/MCT mice or between WT/SAL and TG/SAL mice. (C) The level of tissue-type plasminogen activator was significantly different between WT/MCT and TG/MCT mice but not between WT/SAL and WT/MCT, TG/SAL and TG/MCT or WT/SAL and TG/SAL mice. Samples were tested in dupli- cate. Bars represent the means ± SEM. Statistical analysis was performed by ANOVA with Fisher’s predicted least significant difference test.
Nbp2, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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R&D Systems recombinant human serpinc1
Temporal changes in LDL-EV hemostatic protein composition in post-AMI patients with adverse and reverse LV remodeling. Coagulation proteins (VWF, <t>SerpinC1)</t> and fibrinolytic protein (plasminogen) levels and their ratios (VWF:Plasminogen, SerpinC1:Plasmingen) in LDL-EVs of 198 post-AMI patients at baseline and after 1 and 6 month follow-up. ( A ) A diagram illustrating the studied hemostatic proteins in LDL-EVs. ( B – F ) Differences between baseline and follow-up measurements were established by Wilcoxon signed-ranked test (horizontal statistical bar). Differences in the three protein levels and the protein ratios between patients with adverse LV remodeling and reverse LV remodeling were established by Mann–Whitney U test (vertical statistical bar). Data are presented as mean ± SEM.
Recombinant Human Serpinc1, supplied by R&D Systems, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/antithrombin+iii/pmc09820565-133-77-80?v=R%26D+Systems
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R&D Systems anti serpin c1
Temporal changes in LDL-EV hemostatic protein composition in post-AMI patients with adverse and reverse LV remodeling. Coagulation proteins (VWF, <t>SerpinC1)</t> and fibrinolytic protein (plasminogen) levels and their ratios (VWF:Plasminogen, SerpinC1:Plasmingen) in LDL-EVs of 198 post-AMI patients at baseline and after 1 and 6 month follow-up. ( A ) A diagram illustrating the studied hemostatic proteins in LDL-EVs. ( B – F ) Differences between baseline and follow-up measurements were established by Wilcoxon signed-ranked test (horizontal statistical bar). Differences in the three protein levels and the protein ratios between patients with adverse LV remodeling and reverse LV remodeling were established by Mann–Whitney U test (vertical statistical bar). Data are presented as mean ± SEM.
Anti Serpin C1, supplied by R&D Systems, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


Fig. 5. Markers of coagulation and fibrinolysis system. Markers of coagulation and fibrinolysis systems were measured in bronchoalveolar lavage fluid using commercial enzyme immunoassay kits in wild-type mice treated with saline (WT/SAL, n ¼ 15) or monocrotaline (WT/MCT, n ¼ 13) and in protein C inhibitor transgenic mice treated with saline (TG/SAL, n ¼ 8) or monocrotaline (TG/MCT, n ¼ 11). (A) The level of thrombin– antithrombin complex was significantly different between WT/SAL and WT/MCT, between TG/SAL and TG/MCT, and between WT/MCT and TG/MCT mice. (B) The level of plasminogen activator inhibitor-1 was significantly different between WT/SAL and WT/MCT mice, and between TG/SAL and TG/MCT mice, but not between WT/MCT and TG/MCT mice or between WT/SAL and TG/SAL mice. (C) The level of tissue-type plasminogen activator was significantly different between WT/MCT and TG/MCT mice but not between WT/SAL and WT/MCT, TG/SAL and TG/MCT or WT/SAL and TG/SAL mice. Samples were tested in dupli- cate. Bars represent the means ± SEM. Statistical analysis was performed by ANOVA with Fisher’s predicted least significant difference test.

Journal: Journal of thrombosis and haemostasis : JTH

Article Title: Protective role of protein C inhibitor in monocrotaline-induced pulmonary hypertension.

doi: 10.1111/j.1538-7836.2006.02174.x

Figure Lengend Snippet: Fig. 5. Markers of coagulation and fibrinolysis system. Markers of coagulation and fibrinolysis systems were measured in bronchoalveolar lavage fluid using commercial enzyme immunoassay kits in wild-type mice treated with saline (WT/SAL, n ¼ 15) or monocrotaline (WT/MCT, n ¼ 13) and in protein C inhibitor transgenic mice treated with saline (TG/SAL, n ¼ 8) or monocrotaline (TG/MCT, n ¼ 11). (A) The level of thrombin– antithrombin complex was significantly different between WT/SAL and WT/MCT, between TG/SAL and TG/MCT, and between WT/MCT and TG/MCT mice. (B) The level of plasminogen activator inhibitor-1 was significantly different between WT/SAL and WT/MCT mice, and between TG/SAL and TG/MCT mice, but not between WT/MCT and TG/MCT mice or between WT/SAL and TG/SAL mice. (C) The level of tissue-type plasminogen activator was significantly different between WT/MCT and TG/MCT mice but not between WT/SAL and WT/MCT, TG/SAL and TG/MCT or WT/SAL and TG/SAL mice. Samples were tested in dupli- cate. Bars represent the means ± SEM. Statistical analysis was performed by ANOVA with Fisher’s predicted least significant difference test.

Article Snippet: The concentration of PCI-thrombin complex was measured by EIA using antithrombin antibody (Acris antibodies GmbH, Hiddenhausen, Germany) and biotin-labeled anti-PCI antibody.

Techniques: Coagulation, Enzyme-linked Immunosorbent Assay, Saline, Transgenic Assay

Temporal changes in LDL-EV hemostatic protein composition in post-AMI patients with adverse and reverse LV remodeling. Coagulation proteins (VWF, SerpinC1) and fibrinolytic protein (plasminogen) levels and their ratios (VWF:Plasminogen, SerpinC1:Plasmingen) in LDL-EVs of 198 post-AMI patients at baseline and after 1 and 6 month follow-up. ( A ) A diagram illustrating the studied hemostatic proteins in LDL-EVs. ( B – F ) Differences between baseline and follow-up measurements were established by Wilcoxon signed-ranked test (horizontal statistical bar). Differences in the three protein levels and the protein ratios between patients with adverse LV remodeling and reverse LV remodeling were established by Mann–Whitney U test (vertical statistical bar). Data are presented as mean ± SEM.

Journal: International Journal of Molecular Sciences

Article Title: Temporal Changes in Extracellular Vesicle Hemostatic Protein Composition Predict Favourable Left Ventricular Remodeling after Acute Myocardial Infarction

doi: 10.3390/ijms24010327

Figure Lengend Snippet: Temporal changes in LDL-EV hemostatic protein composition in post-AMI patients with adverse and reverse LV remodeling. Coagulation proteins (VWF, SerpinC1) and fibrinolytic protein (plasminogen) levels and their ratios (VWF:Plasminogen, SerpinC1:Plasmingen) in LDL-EVs of 198 post-AMI patients at baseline and after 1 and 6 month follow-up. ( A ) A diagram illustrating the studied hemostatic proteins in LDL-EVs. ( B – F ) Differences between baseline and follow-up measurements were established by Wilcoxon signed-ranked test (horizontal statistical bar). Differences in the three protein levels and the protein ratios between patients with adverse LV remodeling and reverse LV remodeling were established by Mann–Whitney U test (vertical statistical bar). Data are presented as mean ± SEM.

Article Snippet: The antibodies and recombinant proteins were as follows: for detection of VWF we used recombinant human VWF protein (Factor VIII free, Fitzgerald #30C-CP4003U, Fitzgerald Industries International, Acton, MA, USA), anti-human VWF (Fitzgerald #70R-10589, Fitzgerald Industries International, Acton, MA, USA), and biotinylated anti-human VWF (Fitzgerald #60R-1019, Fitzgerald Industries International, Acton, MA, USA); for detection of SerpinC1, anti-thrombin III antibody (NOVUS Biologicals #NBP1-05149, Littleton, CO, USA), human SerpinC1 biotinylated affinity purified antibody (R&D Systems #BAF1267, Minneapolis, MN, USA) and recombinant human SerpinC1 (R&D Systems #1267-PI-010, Minneapolis, MN, USA); for detection of plasminogen, anti-human plasminogen (NOVUS Biologicals NB120-10176, Littleton, CO, USA), biotinylated anti-human plasminogen (NOVUS Biologicals, NB120-10177, Littleton, CO, USA), and recombinant human plasminogen (R&D system,1939-SE-200, Minneapolis, MN, USA); and for detection of SerpinF2, anti-human SerpinF2 (R&D Systems #MAB1470, Minneapolis, MN, USA), biotinylated anti-human SerpinF2 (R&D Systems #BAF1470, Minneapolis, MN, USA) and recombinant human SerpinF2 (R&D Systems #1470-PI-010, Minneapolis, MN, USA).

Techniques: Coagulation, MANN-WHITNEY

ML-SEM modeling for LDL-EV proteins.

Journal: International Journal of Molecular Sciences

Article Title: Temporal Changes in Extracellular Vesicle Hemostatic Protein Composition Predict Favourable Left Ventricular Remodeling after Acute Myocardial Infarction

doi: 10.3390/ijms24010327

Figure Lengend Snippet: ML-SEM modeling for LDL-EV proteins.

Article Snippet: The antibodies and recombinant proteins were as follows: for detection of VWF we used recombinant human VWF protein (Factor VIII free, Fitzgerald #30C-CP4003U, Fitzgerald Industries International, Acton, MA, USA), anti-human VWF (Fitzgerald #70R-10589, Fitzgerald Industries International, Acton, MA, USA), and biotinylated anti-human VWF (Fitzgerald #60R-1019, Fitzgerald Industries International, Acton, MA, USA); for detection of SerpinC1, anti-thrombin III antibody (NOVUS Biologicals #NBP1-05149, Littleton, CO, USA), human SerpinC1 biotinylated affinity purified antibody (R&D Systems #BAF1267, Minneapolis, MN, USA) and recombinant human SerpinC1 (R&D Systems #1267-PI-010, Minneapolis, MN, USA); for detection of plasminogen, anti-human plasminogen (NOVUS Biologicals NB120-10176, Littleton, CO, USA), biotinylated anti-human plasminogen (NOVUS Biologicals, NB120-10177, Littleton, CO, USA), and recombinant human plasminogen (R&D system,1939-SE-200, Minneapolis, MN, USA); and for detection of SerpinF2, anti-human SerpinF2 (R&D Systems #MAB1470, Minneapolis, MN, USA), biotinylated anti-human SerpinF2 (R&D Systems #BAF1470, Minneapolis, MN, USA) and recombinant human SerpinF2 (R&D Systems #1470-PI-010, Minneapolis, MN, USA).

Techniques: Coagulation

Area under the receiver-operating curve (AUC) of different candidate markers predicting reverse LV remodeling.

Journal: International Journal of Molecular Sciences

Article Title: Temporal Changes in Extracellular Vesicle Hemostatic Protein Composition Predict Favourable Left Ventricular Remodeling after Acute Myocardial Infarction

doi: 10.3390/ijms24010327

Figure Lengend Snippet: Area under the receiver-operating curve (AUC) of different candidate markers predicting reverse LV remodeling.

Article Snippet: The antibodies and recombinant proteins were as follows: for detection of VWF we used recombinant human VWF protein (Factor VIII free, Fitzgerald #30C-CP4003U, Fitzgerald Industries International, Acton, MA, USA), anti-human VWF (Fitzgerald #70R-10589, Fitzgerald Industries International, Acton, MA, USA), and biotinylated anti-human VWF (Fitzgerald #60R-1019, Fitzgerald Industries International, Acton, MA, USA); for detection of SerpinC1, anti-thrombin III antibody (NOVUS Biologicals #NBP1-05149, Littleton, CO, USA), human SerpinC1 biotinylated affinity purified antibody (R&D Systems #BAF1267, Minneapolis, MN, USA) and recombinant human SerpinC1 (R&D Systems #1267-PI-010, Minneapolis, MN, USA); for detection of plasminogen, anti-human plasminogen (NOVUS Biologicals NB120-10176, Littleton, CO, USA), biotinylated anti-human plasminogen (NOVUS Biologicals, NB120-10177, Littleton, CO, USA), and recombinant human plasminogen (R&D system,1939-SE-200, Minneapolis, MN, USA); and for detection of SerpinF2, anti-human SerpinF2 (R&D Systems #MAB1470, Minneapolis, MN, USA), biotinylated anti-human SerpinF2 (R&D Systems #BAF1470, Minneapolis, MN, USA) and recombinant human SerpinF2 (R&D Systems #1470-PI-010, Minneapolis, MN, USA).

Techniques: