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α2ap  (Athens Research)


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    Structured Review

    Athens Research α2ap
    α2ap, supplied by Athens Research, used in various techniques. Bioz Stars score: 92/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/alpha+2+antiplasmin/Alpha+2+Antiplasmin/pm39504559-29-2-8
    Average 92 stars, based on 7 article reviews
    α2ap - by Bioz Stars, 2026-09
    92/100 stars

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    Related Articles

    Clinical Proteomics:

    Article Title: The role of SERPIN citrullination in thrombosis.
    Article Snippet: se IgG Licor IRDye 800RD Licor cat # 926–32,212; RRID: AB_621847 Biological samples Human pooled plasma Affinity Biologicals Cat # FRNCP0125 Chemicals, peptides, and recombinant proteins Human plasmin Athens Research & Technology, Inc. Cat # 16-16-161213-L Human a-2 antiplasmin Athens Research & Technology, Inc. Cat # 16-16-012901 Human a-thrombin Haematologic Technologies Cat # HCT-0020 Human anti

    Article Title: Activation of the epidermal growth factor signalling pathway by tissue plasminogen activator in pancreas cancer cells
    Article Snippet: Galardin (GM 6001), mutant [Glu52]diphtheria toxin CRM197, and active human recombinant MMP‐9 were from Calbiochem (Darmstadt, Germany); PD098059, {"type":"entrez-nucleotide","attrs":{"text":"LY294002","term_id":"1257998346","term_text":"LY294002"}} LY294002 , and tyrphostin AG1478 from Biomol (Butler Pike, PA, USA); recombinant human epidermal growth factor (EGF) from Invitrogen (Carlsbad, CA, USA); p‐aminobenzoyl‐gly‐pro‐ d ‐ala‐hydroxamic acid (AHA) from MP Biomedicals (Aurora, OH, USA); plasmin and bisindolylmaleimide (GF109203X) from Roche Diagnostics (Mannheim, Germany); recombinant tPA (Actilyse) from Boehringer Mannheim (Barcelona, Spain); Pefabloc/tPA [2,7‐bis‐(4‐amidinobenzylidene)‐cycloheptanone‐(1) dihydrochloride salt] from Pentapharm (Basel, Switzerland).(Darmstadt, Germany); PD098059, {"type":"entrez-nucleotide","attrs":{"text":"LY294002","term_id":"1257998346","term_text":"LY294002"}} LY294002 , and tyrphostin AG1478 from Biomol (Butler Pike, PA, USA); recombinant human epidermal growth factor (EGF) from Invitrogen (Carlsbad, CA, USA); p‐aminobenzoyl‐gly‐pro‐ d ‐ala‐hydroxamic acid (AHA) from MP Biomedicals (Aurora, OH, USA); plasmin and bisindolylmaleimide (GF109203X) from Roche Diagnostics (Mannheim, Germany); recombinant tPA (Actilyse) from Boehringer Mannheim (Barcelona, Spain); Pefabloc/tPA [2,7‐bis‐(4‐amidinobenzylidene)‐cycloheptanone‐(1) dihydrochloride salt] from Pentapharm (Basel, Switzerland). ... Alpha 2 antiplasmin was from Athens Research and Technology (Athens, GA, USA).. Catalytically inactive mutant tPA (S478A) was obtained from Molecular Innovations Inc (Southfield, MI, USA).Catalytically inactive mutant tPA (S478A) was obtained from Molecular Innovations Inc (Southfield, MI, USA).

    Recombinant:

    Article Title: The role of SERPIN citrullination in thrombosis.
    Article Snippet: se IgG Licor IRDye 800RD Licor cat # 926–32,212; RRID: AB_621847 Biological samples Human pooled plasma Affinity Biologicals Cat # FRNCP0125 Chemicals, peptides, and recombinant proteins Human plasmin Athens Research & Technology, Inc. Cat # 16-16-161213-L Human a-2 antiplasmin Athens Research & Technology, Inc. Cat # 16-16-012901 Human a-thrombin Haematologic Technologies Cat # HCT-0020 Human anti

    Article Title: Activation of the epidermal growth factor signalling pathway by tissue plasminogen activator in pancreas cancer cells
    Article Snippet: Galardin (GM 6001), mutant [Glu52]diphtheria toxin CRM197, and active human recombinant MMP‐9 were from Calbiochem (Darmstadt, Germany); PD098059, {"type":"entrez-nucleotide","attrs":{"text":"LY294002","term_id":"1257998346","term_text":"LY294002"}} LY294002 , and tyrphostin AG1478 from Biomol (Butler Pike, PA, USA); recombinant human epidermal growth factor (EGF) from Invitrogen (Carlsbad, CA, USA); p‐aminobenzoyl‐gly‐pro‐ d ‐ala‐hydroxamic acid (AHA) from MP Biomedicals (Aurora, OH, USA); plasmin and bisindolylmaleimide (GF109203X) from Roche Diagnostics (Mannheim, Germany); recombinant tPA (Actilyse) from Boehringer Mannheim (Barcelona, Spain); Pefabloc/tPA [2,7‐bis‐(4‐amidinobenzylidene)‐cycloheptanone‐(1) dihydrochloride salt] from Pentapharm (Basel, Switzerland).(Darmstadt, Germany); PD098059, {"type":"entrez-nucleotide","attrs":{"text":"LY294002","term_id":"1257998346","term_text":"LY294002"}} LY294002 , and tyrphostin AG1478 from Biomol (Butler Pike, PA, USA); recombinant human epidermal growth factor (EGF) from Invitrogen (Carlsbad, CA, USA); p‐aminobenzoyl‐gly‐pro‐ d ‐ala‐hydroxamic acid (AHA) from MP Biomedicals (Aurora, OH, USA); plasmin and bisindolylmaleimide (GF109203X) from Roche Diagnostics (Mannheim, Germany); recombinant tPA (Actilyse) from Boehringer Mannheim (Barcelona, Spain); Pefabloc/tPA [2,7‐bis‐(4‐amidinobenzylidene)‐cycloheptanone‐(1) dihydrochloride salt] from Pentapharm (Basel, Switzerland). ... Alpha 2 antiplasmin was from Athens Research and Technology (Athens, GA, USA).. Catalytically inactive mutant tPA (S478A) was obtained from Molecular Innovations Inc (Southfield, MI, USA).Catalytically inactive mutant tPA (S478A) was obtained from Molecular Innovations Inc (Southfield, MI, USA).



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    A. Representative images of plasminogen activator inhibitor 1 (PAI-1, green) in ischemic stroke thrombi showing its association with strings of NETs (cyan, arrows, highlighted at higher magnification shown in the squared area) in a neutrophil-rich area at the thrombus periphery. Neutrophils were identified by the polynucleated aspect of their nuclei and positive staining for myeloperoxidase (red). B. Representative images <t>of</t> <t>α2-antiplasmin</t> (red) localization relative to fibrin (green, arrows) and NETs (cyan, asterisks). Higher magnification views of the squared areas are shown in the insets. C-F. Quantification of PAI-1, protease nexin-1, neutrophil elastase, and α2-antiplasmin, in ischemic stroke thrombus supernatants collected after 2 hours of incubation in HBSS-calcium-magnesium supplemented with either recombinant DNase 1 (pulmozyme, 100 µg/mL) or calcium saline (vehicle). Each dot represents the individual value of a different thrombus fragment. Each patient thrombus was split in 2 fragments, both fragments being randomly allocated to different treatment with either DNase 1 or vehicle. G. Western blot analysis (reducing conditions) of α2-antiplasmin integrity in supernatants from 4 different stroke thrombi cut in half and treated with either recombinant DNase 1 or calcium saline (vehicle). In addition to the expected 70 kDa α2-antiplasmin band (a), 3 additional lower molecular weight forms were detected (labeled b to d). Note that DNase 1 treatment was associated with a decrease in the 39 kDa form (c), which was mirrored by an increase in that of the lowest 30 kDa molecular weight band (d).
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    α2ap  (Athens Research)
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    Athens Research α2ap
    A. Representative images of plasminogen activator inhibitor 1 (PAI-1, green) in ischemic stroke thrombi showing its association with strings of NETs (cyan, arrows, highlighted at higher magnification shown in the squared area) in a neutrophil-rich area at the thrombus periphery. Neutrophils were identified by the polynucleated aspect of their nuclei and positive staining for myeloperoxidase (red). B. Representative images <t>of</t> <t>α2-antiplasmin</t> (red) localization relative to fibrin (green, arrows) and NETs (cyan, asterisks). Higher magnification views of the squared areas are shown in the insets. C-F. Quantification of PAI-1, protease nexin-1, neutrophil elastase, and α2-antiplasmin, in ischemic stroke thrombus supernatants collected after 2 hours of incubation in HBSS-calcium-magnesium supplemented with either recombinant DNase 1 (pulmozyme, 100 µg/mL) or calcium saline (vehicle). Each dot represents the individual value of a different thrombus fragment. Each patient thrombus was split in 2 fragments, both fragments being randomly allocated to different treatment with either DNase 1 or vehicle. G. Western blot analysis (reducing conditions) of α2-antiplasmin integrity in supernatants from 4 different stroke thrombi cut in half and treated with either recombinant DNase 1 or calcium saline (vehicle). In addition to the expected 70 kDa α2-antiplasmin band (a), 3 additional lower molecular weight forms were detected (labeled b to d). Note that DNase 1 treatment was associated with a decrease in the 39 kDa form (c), which was mirrored by an increase in that of the lowest 30 kDa molecular weight band (d).
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    affimer highly purified human α2ap  (Athens Research)
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    Athens Research affimer highly purified human α2ap
    A. Representative images of plasminogen activator inhibitor 1 (PAI-1, green) in ischemic stroke thrombi showing its association with strings of NETs (cyan, arrows, highlighted at higher magnification shown in the squared area) in a neutrophil-rich area at the thrombus periphery. Neutrophils were identified by the polynucleated aspect of their nuclei and positive staining for myeloperoxidase (red). B. Representative images <t>of</t> <t>α2-antiplasmin</t> (red) localization relative to fibrin (green, arrows) and NETs (cyan, asterisks). Higher magnification views of the squared areas are shown in the insets. C-F. Quantification of PAI-1, protease nexin-1, neutrophil elastase, and α2-antiplasmin, in ischemic stroke thrombus supernatants collected after 2 hours of incubation in HBSS-calcium-magnesium supplemented with either recombinant DNase 1 (pulmozyme, 100 µg/mL) or calcium saline (vehicle). Each dot represents the individual value of a different thrombus fragment. Each patient thrombus was split in 2 fragments, both fragments being randomly allocated to different treatment with either DNase 1 or vehicle. G. Western blot analysis (reducing conditions) of α2-antiplasmin integrity in supernatants from 4 different stroke thrombi cut in half and treated with either recombinant DNase 1 or calcium saline (vehicle). In addition to the expected 70 kDa α2-antiplasmin band (a), 3 additional lower molecular weight forms were detected (labeled b to d). Note that DNase 1 treatment was associated with a decrease in the 39 kDa form (c), which was mirrored by an increase in that of the lowest 30 kDa molecular weight band (d).
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    Image Search Results


    A. Representative images of plasminogen activator inhibitor 1 (PAI-1, green) in ischemic stroke thrombi showing its association with strings of NETs (cyan, arrows, highlighted at higher magnification shown in the squared area) in a neutrophil-rich area at the thrombus periphery. Neutrophils were identified by the polynucleated aspect of their nuclei and positive staining for myeloperoxidase (red). B. Representative images of α2-antiplasmin (red) localization relative to fibrin (green, arrows) and NETs (cyan, asterisks). Higher magnification views of the squared areas are shown in the insets. C-F. Quantification of PAI-1, protease nexin-1, neutrophil elastase, and α2-antiplasmin, in ischemic stroke thrombus supernatants collected after 2 hours of incubation in HBSS-calcium-magnesium supplemented with either recombinant DNase 1 (pulmozyme, 100 µg/mL) or calcium saline (vehicle). Each dot represents the individual value of a different thrombus fragment. Each patient thrombus was split in 2 fragments, both fragments being randomly allocated to different treatment with either DNase 1 or vehicle. G. Western blot analysis (reducing conditions) of α2-antiplasmin integrity in supernatants from 4 different stroke thrombi cut in half and treated with either recombinant DNase 1 or calcium saline (vehicle). In addition to the expected 70 kDa α2-antiplasmin band (a), 3 additional lower molecular weight forms were detected (labeled b to d). Note that DNase 1 treatment was associated with a decrease in the 39 kDa form (c), which was mirrored by an increase in that of the lowest 30 kDa molecular weight band (d).

    Journal: bioRxiv

    Article Title: Neutrophil extracellular traps block endogenous and intravenous thrombolysis-induced fibrinolysis in large vessel occlusion acute ischemic stroke

    doi: 10.1101/2025.03.28.646062

    Figure Lengend Snippet: A. Representative images of plasminogen activator inhibitor 1 (PAI-1, green) in ischemic stroke thrombi showing its association with strings of NETs (cyan, arrows, highlighted at higher magnification shown in the squared area) in a neutrophil-rich area at the thrombus periphery. Neutrophils were identified by the polynucleated aspect of their nuclei and positive staining for myeloperoxidase (red). B. Representative images of α2-antiplasmin (red) localization relative to fibrin (green, arrows) and NETs (cyan, asterisks). Higher magnification views of the squared areas are shown in the insets. C-F. Quantification of PAI-1, protease nexin-1, neutrophil elastase, and α2-antiplasmin, in ischemic stroke thrombus supernatants collected after 2 hours of incubation in HBSS-calcium-magnesium supplemented with either recombinant DNase 1 (pulmozyme, 100 µg/mL) or calcium saline (vehicle). Each dot represents the individual value of a different thrombus fragment. Each patient thrombus was split in 2 fragments, both fragments being randomly allocated to different treatment with either DNase 1 or vehicle. G. Western blot analysis (reducing conditions) of α2-antiplasmin integrity in supernatants from 4 different stroke thrombi cut in half and treated with either recombinant DNase 1 or calcium saline (vehicle). In addition to the expected 70 kDa α2-antiplasmin band (a), 3 additional lower molecular weight forms were detected (labeled b to d). Note that DNase 1 treatment was associated with a decrease in the 39 kDa form (c), which was mirrored by an increase in that of the lowest 30 kDa molecular weight band (d).

    Article Snippet: Alpha-2-antiplasmin (α2AP, DuoSet Human Serpin2/alpha-2-antiplasmin, DY1470, R&D Systems), PAI-1 (Asserachrom 00949, Stago), and neutrophil elastase (Hycult Biotech HK319) were quantified in supernatants from AIS thrombi using commercial kits and following the manufacturers’ instructions.

    Techniques: Staining, Incubation, Recombinant, Saline, Western Blot, Molecular Weight, Labeling