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purified human fxii  (Haematologic Technologies)

 
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    Haematologic Technologies purified human fxii
    Purified Human Fxii, supplied by Haematologic Technologies, 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/human+fxii/purified+fxii/pmc11448313-141-2-4
    Average 90 stars, based on 1 article reviews
    purified human fxii - by Bioz Stars, 2026-10
    90/100 stars

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    Related Articles

    Activation Assay:

    Article Title: Ayadualin, a novel RGD peptide with dual antihemostatic activities from the sand fly Lutzomyia ayacuchensis, a vector of Andean-type cutaneous leishmaniasis.
    Article Snippet: Data were analyzed and the IC50 values were determined by non-linear regression (curve-fitting) using GraphPad Prism version 6.05 (GraphPad Software, Inc., CA). .. The effect of ayadualin on FXII activation was assessed as follows: human FXII (final concentration, 0.2 mM) (Haematologic Technologies Inc., Essex Junction, VT, USA) was pre-incubated with serially diluted ayadualin for 5 min at 37 C in the presence of ZnCl2 (0.5 mM), and activated by addition of 5 ml of APTT reagent Please cite this article in press as: H. Kato, et al., Ayadualin, a novel RGD pe ayacuchensis, a vector of Andean-type cutaneous leishmaniasis, Biochimi (Sysmex) for 5 min at 37 C. The effect of ayadualin on the enzymatic activity of FXIIa was assessed as follows: human FXII (0.2 mM) (Haematologic Technologies Inc.) was activated with 5 ml of APTT reagent (Sysmex) for 5 min at 37 C in the presence of ZnCl2 (0.5 mM), and then incubated with serially diluted ayadualin for 5 min at 37 C. The activity of FXIIa was measured using the chromogenic substrate SPECTROZYME FXIIa (American Diagnostica). ..

    Article Title: Antibody inhibition of contact factor XII reduces platelet deposition in a model of extracorporeal membrane oxygenator perfusion in nonhuman primates
    Article Snippet: .. For FXII activation experiments, human FXII (40 nM; Haematologic Technologies, Inc, Essex Junction, VT, USA) was incubated with 0 to 80 nM 5C12 (10 min) followed by 1 μg/mL dextran sulfate (20 min). .. Spectrozyme FXIIa (0.5 mM; Sekisui Diagnostics GmbH, Lexington, MA, USA) was then added to measure hydrolysis by activated FXII (FXIIa).

    Article Title: Ayaconin, a novel inhibitor of the plasma contact system from the sand fly Lutzomyia ayacuchensis, a vector of Andean-type cutaneous leishmaniasis.
    Article Snippet: Transcriptome analysis of the salivary gland cDNA library from a phlebotomine sand fly, Lutzomyia ayacuchensis, identified a transcript coding for the PpSP15/SL1 family protein as the second most abundant salivary component.. In the present study, a recombinant protein of the PpSP15/SL1 family protein, designated ayaconin, was expressed in Escherichia coli, and its biological activity was characterized.. The recombinant ayaconin purified from the soluble fraction of E. coli lysate efficiently inhibited the intrinsic but not extrinsic blood coagulation pathway.

    Concentration Assay:

    Article Title: Ayadualin, a novel RGD peptide with dual antihemostatic activities from the sand fly Lutzomyia ayacuchensis, a vector of Andean-type cutaneous leishmaniasis.
    Article Snippet: Data were analyzed and the IC50 values were determined by non-linear regression (curve-fitting) using GraphPad Prism version 6.05 (GraphPad Software, Inc., CA). .. The effect of ayadualin on FXII activation was assessed as follows: human FXII (final concentration, 0.2 mM) (Haematologic Technologies Inc., Essex Junction, VT, USA) was pre-incubated with serially diluted ayadualin for 5 min at 37 C in the presence of ZnCl2 (0.5 mM), and activated by addition of 5 ml of APTT reagent Please cite this article in press as: H. Kato, et al., Ayadualin, a novel RGD pe ayacuchensis, a vector of Andean-type cutaneous leishmaniasis, Biochimi (Sysmex) for 5 min at 37 C. The effect of ayadualin on the enzymatic activity of FXIIa was assessed as follows: human FXII (0.2 mM) (Haematologic Technologies Inc.) was activated with 5 ml of APTT reagent (Sysmex) for 5 min at 37 C in the presence of ZnCl2 (0.5 mM), and then incubated with serially diluted ayadualin for 5 min at 37 C. The activity of FXIIa was measured using the chromogenic substrate SPECTROZYME FXIIa (American Diagnostica). ..

    Article Title: Ayaconin, a novel inhibitor of the plasma contact system from the sand fly Lutzomyia ayacuchensis, a vector of Andean-type cutaneous leishmaniasis.
    Article Snippet: Transcriptome analysis of the salivary gland cDNA library from a phlebotomine sand fly, Lutzomyia ayacuchensis, identified a transcript coding for the PpSP15/SL1 family protein as the second most abundant salivary component.. In the present study, a recombinant protein of the PpSP15/SL1 family protein, designated ayaconin, was expressed in Escherichia coli, and its biological activity was characterized.. The recombinant ayaconin purified from the soluble fraction of E. coli lysate efficiently inhibited the intrinsic but not extrinsic blood coagulation pathway.

    Plasmid Preparation:

    Article Title: Ayadualin, a novel RGD peptide with dual antihemostatic activities from the sand fly Lutzomyia ayacuchensis, a vector of Andean-type cutaneous leishmaniasis.
    Article Snippet: Data were analyzed and the IC50 values were determined by non-linear regression (curve-fitting) using GraphPad Prism version 6.05 (GraphPad Software, Inc., CA). .. The effect of ayadualin on FXII activation was assessed as follows: human FXII (final concentration, 0.2 mM) (Haematologic Technologies Inc., Essex Junction, VT, USA) was pre-incubated with serially diluted ayadualin for 5 min at 37 C in the presence of ZnCl2 (0.5 mM), and activated by addition of 5 ml of APTT reagent Please cite this article in press as: H. Kato, et al., Ayadualin, a novel RGD pe ayacuchensis, a vector of Andean-type cutaneous leishmaniasis, Biochimi (Sysmex) for 5 min at 37 C. The effect of ayadualin on the enzymatic activity of FXIIa was assessed as follows: human FXII (0.2 mM) (Haematologic Technologies Inc.) was activated with 5 ml of APTT reagent (Sysmex) for 5 min at 37 C in the presence of ZnCl2 (0.5 mM), and then incubated with serially diluted ayadualin for 5 min at 37 C. The activity of FXIIa was measured using the chromogenic substrate SPECTROZYME FXIIa (American Diagnostica). ..

    Activity Assay:

    Article Title: Ayadualin, a novel RGD peptide with dual antihemostatic activities from the sand fly Lutzomyia ayacuchensis, a vector of Andean-type cutaneous leishmaniasis.
    Article Snippet: Data were analyzed and the IC50 values were determined by non-linear regression (curve-fitting) using GraphPad Prism version 6.05 (GraphPad Software, Inc., CA). .. The effect of ayadualin on FXII activation was assessed as follows: human FXII (final concentration, 0.2 mM) (Haematologic Technologies Inc., Essex Junction, VT, USA) was pre-incubated with serially diluted ayadualin for 5 min at 37 C in the presence of ZnCl2 (0.5 mM), and activated by addition of 5 ml of APTT reagent Please cite this article in press as: H. Kato, et al., Ayadualin, a novel RGD pe ayacuchensis, a vector of Andean-type cutaneous leishmaniasis, Biochimi (Sysmex) for 5 min at 37 C. The effect of ayadualin on the enzymatic activity of FXIIa was assessed as follows: human FXII (0.2 mM) (Haematologic Technologies Inc.) was activated with 5 ml of APTT reagent (Sysmex) for 5 min at 37 C in the presence of ZnCl2 (0.5 mM), and then incubated with serially diluted ayadualin for 5 min at 37 C. The activity of FXIIa was measured using the chromogenic substrate SPECTROZYME FXIIa (American Diagnostica). ..

    Article Title: Ayaconin, a novel inhibitor of the plasma contact system from the sand fly Lutzomyia ayacuchensis, a vector of Andean-type cutaneous leishmaniasis.
    Article Snippet: Transcriptome analysis of the salivary gland cDNA library from a phlebotomine sand fly, Lutzomyia ayacuchensis, identified a transcript coding for the PpSP15/SL1 family protein as the second most abundant salivary component.. In the present study, a recombinant protein of the PpSP15/SL1 family protein, designated ayaconin, was expressed in Escherichia coli, and its biological activity was characterized.. The recombinant ayaconin purified from the soluble fraction of E. coli lysate efficiently inhibited the intrinsic but not extrinsic blood coagulation pathway.

    Incubation:

    Article Title: Ayadualin, a novel RGD peptide with dual antihemostatic activities from the sand fly Lutzomyia ayacuchensis, a vector of Andean-type cutaneous leishmaniasis.
    Article Snippet: Data were analyzed and the IC50 values were determined by non-linear regression (curve-fitting) using GraphPad Prism version 6.05 (GraphPad Software, Inc., CA). .. The effect of ayadualin on FXII activation was assessed as follows: human FXII (final concentration, 0.2 mM) (Haematologic Technologies Inc., Essex Junction, VT, USA) was pre-incubated with serially diluted ayadualin for 5 min at 37 C in the presence of ZnCl2 (0.5 mM), and activated by addition of 5 ml of APTT reagent Please cite this article in press as: H. Kato, et al., Ayadualin, a novel RGD pe ayacuchensis, a vector of Andean-type cutaneous leishmaniasis, Biochimi (Sysmex) for 5 min at 37 C. The effect of ayadualin on the enzymatic activity of FXIIa was assessed as follows: human FXII (0.2 mM) (Haematologic Technologies Inc.) was activated with 5 ml of APTT reagent (Sysmex) for 5 min at 37 C in the presence of ZnCl2 (0.5 mM), and then incubated with serially diluted ayadualin for 5 min at 37 C. The activity of FXIIa was measured using the chromogenic substrate SPECTROZYME FXIIa (American Diagnostica). ..

    Article Title: Antibody inhibition of contact factor XII reduces platelet deposition in a model of extracorporeal membrane oxygenator perfusion in nonhuman primates
    Article Snippet: .. For FXII activation experiments, human FXII (40 nM; Haematologic Technologies, Inc, Essex Junction, VT, USA) was incubated with 0 to 80 nM 5C12 (10 min) followed by 1 μg/mL dextran sulfate (20 min). .. Spectrozyme FXIIa (0.5 mM; Sekisui Diagnostics GmbH, Lexington, MA, USA) was then added to measure hydrolysis by activated FXII (FXIIa).

    Article Title: Ayaconin, a novel inhibitor of the plasma contact system from the sand fly Lutzomyia ayacuchensis, a vector of Andean-type cutaneous leishmaniasis.
    Article Snippet: Transcriptome analysis of the salivary gland cDNA library from a phlebotomine sand fly, Lutzomyia ayacuchensis, identified a transcript coding for the PpSP15/SL1 family protein as the second most abundant salivary component.. In the present study, a recombinant protein of the PpSP15/SL1 family protein, designated ayaconin, was expressed in Escherichia coli, and its biological activity was characterized.. The recombinant ayaconin purified from the soluble fraction of E. coli lysate efficiently inhibited the intrinsic but not extrinsic blood coagulation pathway.

    Coagulation:

    Article Title: A Comparison of Blood Factor XII Autoactivation in Buffer, Protein Cocktail, Serum, and Plasma Solutions
    Article Snippet: .. 2.2.4 Coagulation Proteins Human FXII (4 lots designated Lots A, B, C, D) and αFXIIa (2 lots designated Lots 1, 2) were used as received from Haematologic Technologies (Essex Junction, VT) and Enzyme Research Laboratories (South Bend, IN) respectively. ..

    Article Title: Ayaconin, a novel inhibitor of the plasma contact system from the sand fly Lutzomyia ayacuchensis, a vector of Andean-type cutaneous leishmaniasis.
    Article Snippet: Transcriptome analysis of the salivary gland cDNA library from a phlebotomine sand fly, Lutzomyia ayacuchensis, identified a transcript coding for the PpSP15/SL1 family protein as the second most abundant salivary component.. In the present study, a recombinant protein of the PpSP15/SL1 family protein, designated ayaconin, was expressed in Escherichia coli, and its biological activity was characterized.. The recombinant ayaconin purified from the soluble fraction of E. coli lysate efficiently inhibited the intrinsic but not extrinsic blood coagulation pathway.



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    a Schematic representation of the strategy used to identify <t>FXII-specific</t> nanobodies and to design nanobody-Fc fusion after immunizing an alpaca with <t>human</t> <t>FXII.</t> b Characterization of E. coli BL21-expressed Nb and Chinese Hamster Ovary (CHO) cell-expressed Nb-Fc by SDS-PAGE (left panel) and Western blot (right panel). c Binding affinity of Nb or Nb-Fc to human FXII determined by kinetic assays using the Fortebio Octet System. d Dot blot assay to analyze the interaction of native or heat-treated FXII and Nb as indicated. BSA was used as control. e , f FXII epitope mapping. e FXII domains were individually expressed using E. coli BL21, separated by SDS-PAGE under reducing conditions and visualized by Brilliant Coomassie Blue (upper panel), and probed for Nb binding by Western blot (lower panel). f Full-length FXII (FXII_fl) and FXII mutants with indicated deleted domains (FXII_ΔFnII: deletion of FnII; FXII_ΔKringle: deletion of the Kringle domain; FXII_ΔPRR: deletion of the C-terminal part of PRR) were expressed in HEK 293 cells. Binding capacity of a polyclonal anti-FXII antibody as control (upper panel) and Nb (lower panel) to the mutants was evaluated by Western blot under both reducing and non-reducing conditions. g Effects of increasing concentrations of Nb-Fc on ellagic acid (EA, 4 µg/ml)-induced FXII activation using the FXIIa-specific substrate S-2302 (final concentration: 0.8 mM). Isotype control antibody (Iso-Fc) was used as control. h Effects of Nb-Fc on plasma prekallikrein (PK) activation. FXII was pretreated with Nb-Fc, followed by the addition of EA (final concentration: 4 μg/mL) and PK (6.25 μg/mL), then the chromogenic substrate CS-31(02) was used to evaluate the enzymatic activity of activated PK. i Effects of Nb-Fc on activated partial thromboplastin time (aPTT). Citrated human plasma was incubated with increasing concentrations of Nb-Fc (0–31.5 µg/ml) for 5 min prior to aPTT measurements. Experiments in b , d – f were independently performed twice with consistent results. See the Methods for details. Source data are provided as a Source Data file.
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    Image Search Results


    a Schematic representation of the strategy used to identify FXII-specific nanobodies and to design nanobody-Fc fusion after immunizing an alpaca with human FXII. b Characterization of E. coli BL21-expressed Nb and Chinese Hamster Ovary (CHO) cell-expressed Nb-Fc by SDS-PAGE (left panel) and Western blot (right panel). c Binding affinity of Nb or Nb-Fc to human FXII determined by kinetic assays using the Fortebio Octet System. d Dot blot assay to analyze the interaction of native or heat-treated FXII and Nb as indicated. BSA was used as control. e , f FXII epitope mapping. e FXII domains were individually expressed using E. coli BL21, separated by SDS-PAGE under reducing conditions and visualized by Brilliant Coomassie Blue (upper panel), and probed for Nb binding by Western blot (lower panel). f Full-length FXII (FXII_fl) and FXII mutants with indicated deleted domains (FXII_ΔFnII: deletion of FnII; FXII_ΔKringle: deletion of the Kringle domain; FXII_ΔPRR: deletion of the C-terminal part of PRR) were expressed in HEK 293 cells. Binding capacity of a polyclonal anti-FXII antibody as control (upper panel) and Nb (lower panel) to the mutants was evaluated by Western blot under both reducing and non-reducing conditions. g Effects of increasing concentrations of Nb-Fc on ellagic acid (EA, 4 µg/ml)-induced FXII activation using the FXIIa-specific substrate S-2302 (final concentration: 0.8 mM). Isotype control antibody (Iso-Fc) was used as control. h Effects of Nb-Fc on plasma prekallikrein (PK) activation. FXII was pretreated with Nb-Fc, followed by the addition of EA (final concentration: 4 μg/mL) and PK (6.25 μg/mL), then the chromogenic substrate CS-31(02) was used to evaluate the enzymatic activity of activated PK. i Effects of Nb-Fc on activated partial thromboplastin time (aPTT). Citrated human plasma was incubated with increasing concentrations of Nb-Fc (0–31.5 µg/ml) for 5 min prior to aPTT measurements. Experiments in b , d – f were independently performed twice with consistent results. See the Methods for details. Source data are provided as a Source Data file.

    Journal: Nature Communications

    Article Title: A single-domain antibody targeting factor XII inhibits both thrombosis and inflammation

    doi: 10.1038/s41467-024-51745-4

    Figure Lengend Snippet: a Schematic representation of the strategy used to identify FXII-specific nanobodies and to design nanobody-Fc fusion after immunizing an alpaca with human FXII. b Characterization of E. coli BL21-expressed Nb and Chinese Hamster Ovary (CHO) cell-expressed Nb-Fc by SDS-PAGE (left panel) and Western blot (right panel). c Binding affinity of Nb or Nb-Fc to human FXII determined by kinetic assays using the Fortebio Octet System. d Dot blot assay to analyze the interaction of native or heat-treated FXII and Nb as indicated. BSA was used as control. e , f FXII epitope mapping. e FXII domains were individually expressed using E. coli BL21, separated by SDS-PAGE under reducing conditions and visualized by Brilliant Coomassie Blue (upper panel), and probed for Nb binding by Western blot (lower panel). f Full-length FXII (FXII_fl) and FXII mutants with indicated deleted domains (FXII_ΔFnII: deletion of FnII; FXII_ΔKringle: deletion of the Kringle domain; FXII_ΔPRR: deletion of the C-terminal part of PRR) were expressed in HEK 293 cells. Binding capacity of a polyclonal anti-FXII antibody as control (upper panel) and Nb (lower panel) to the mutants was evaluated by Western blot under both reducing and non-reducing conditions. g Effects of increasing concentrations of Nb-Fc on ellagic acid (EA, 4 µg/ml)-induced FXII activation using the FXIIa-specific substrate S-2302 (final concentration: 0.8 mM). Isotype control antibody (Iso-Fc) was used as control. h Effects of Nb-Fc on plasma prekallikrein (PK) activation. FXII was pretreated with Nb-Fc, followed by the addition of EA (final concentration: 4 μg/mL) and PK (6.25 μg/mL), then the chromogenic substrate CS-31(02) was used to evaluate the enzymatic activity of activated PK. i Effects of Nb-Fc on activated partial thromboplastin time (aPTT). Citrated human plasma was incubated with increasing concentrations of Nb-Fc (0–31.5 µg/ml) for 5 min prior to aPTT measurements. Experiments in b , d – f were independently performed twice with consistent results. See the Methods for details. Source data are provided as a Source Data file.

    Article Snippet: 800 μg of human FXII zymogen (Enzyme Research Laboratories) isolated from human plasma was emulsified with Freund’s complete adjuvant (Millipore Sigma) and used for subcutaneous immunization of an alpaca.

    Techniques: SDS Page, Western Blot, Binding Assay, Dot Blot, Control, Activation Assay, Concentration Assay, Clinical Proteomics, Activity Assay, Incubation