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human enteropeptidase  (R&D Systems)


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    Structured Review

    R&D Systems human enteropeptidase
    Human Enteropeptidase, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/recombinant+human+enteropeptidase/Recombinant+Human+Enteropeptidase%2FEnterokinase+Protein%2C+CF/pm40341748-175-16-21
    Average 93 stars, based on 6 article reviews
    human enteropeptidase - by Bioz Stars, 2026-10
    93/100 stars

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    Related Articles

    Fluorescence:

    Article Title: Heteroarylcarboxylic acid ester derivative
    Article Snippet: .. Using a 96 well plate (#3915, Costar), a test compound (25 μL), 400 mM Tris-HCl buffer (pH 8.0, 25 μL) and 0.5 mg/mL fluorescence enzyme substrate (Gly-Asp-Asp-Asp-Asp-Lys-β-Naphtylamide, 25 μL) were mixed, and recombinant human enteropeptidase (R&D Systems, Inc., 25 μL) was added. .. Using a fluorescence plate reader fmax (Molecular Devices, Inc.), the reaction rate was measured from the time-course changes at excitation wavelength 320 nm and fluorescence wavelength 405 nm.

    Article Title: Heteroarylcarboxylic acid ester derivative
    Article Snippet: .. Using a 96 well plate (#3915, Costar), a test compound (25 μL), 400 mM Tris-HCl buffer (pH 8.0, 25 μL) and 0.5 mg/mL fluorescence enzyme substrate (Gly-Asp-Asp-Asp-Asp-Lys-β-Naphtylamide, 25 μL) were mixed, and recombinant human enteropeptidase (R&D Systems, Inc., 25 μL) was added. .. Using a fluorescence plate reader fmax (Molecular Devices, Inc.), the reaction rate was measured from the time-course changes at excitation wavelength 320 nm and fluorescence wavelength 405 nm.

    Article Title: Heteroarylcarboxylic acid ester derivative
    Article Snippet: .. Using a 96 well plate (#3915, Costar), a test compound (25 μL), 400 mM Tris-HCl buffer (pH 8.0, 25 μL) and 0.5 mg/mL fluorescence enzyme substrate (Gly-Asp-Asp-Asp-Asp-Lys-β-Naphtylamide, 25 μL) were mixed, and recombinant human enteropeptidase (R&D Systems, Inc., 25 μL) was added. .. Using a fluorescence plate reader fmax (Molecular Devices, Inc.), the reaction rate was measured from the time-course changes at excitation wavelength 320 nm and fluorescence wavelength 405 nm.

    Article Title: Heteroarylcarboxylic acid ester derivative
    Article Snippet: .. Using a 96 well plate (#3915, Costar), a test compound (25 μL), 400 mM Tris-HCl buffer (pH 8.0, 25 μL) and 0.5 mg/mL fluorescence enzyme substrate (Gly-Asp-Asp-Asp-Asp-Lys-β-Naphtylamide, 25 μL) were mixed, and recombinant human enteropeptidase (R&D Systems, Inc., 25 μL) was added. .. Using a fluorescence plate reader fmax (Molecular Devices, Inc.), the reaction rate was measured from the time-course changes at excitation wavelength 320 nm and fluorescence wavelength 405 nm.

    Article Title: Heteroarylcarboxylic acid ester derivative
    Article Snippet: .. Using a 96 well plate (#3915, Costar), a test compound (25 μL), 400 mM Tris-HCl buffer (pH 8.0, 25 μL) and 0.5 mg/mL, fluorescence enzyme substrate (Gly-Asp-Asp-Asp-Asp-Lys-β-Naphtylamide, 25 μL) were mixed, and recombinant human enteropeptidase (R&D Systems, Inc., 25 μL) was added. .. Using a fluorescence plate reader fmax (Molecular Devices, Inc.), the reaction rate was measured from the time-course changes at excitation wavelength 320 nm and fluorescence wavelength 405 nm.

    Article Title: Heteroarylcarboxylic acid ester derivative
    Article Snippet: .. Using a 96 well plate (#3915, Costar), a test compound (25 μL), 400 mM Tris-HCl buffer (pH 8.0, 25 μL) and 0.5 mg/mL fluorescence enzyme substrate (Gly-Asp-Asp-Asp-Asp-Lys-β-Naphtylamide, 25 μL) were mixed, and recombinant human enteropeptidase (R&D Systems, Inc., 25 μL) was added. .. Using a fluorescence plate reader fmax (Molecular Devices, Inc.), the reaction rate was measured from the time-course changes at excitation wavelength 320 nm and fluorescence wavelength 405 nm.

    Recombinant:

    Article Title: Heteroarylcarboxylic acid ester derivative
    Article Snippet: .. Using a 96 well plate (#3915, Costar), a test compound (25 μL), 400 mM Tris-HCl buffer (pH 8.0, 25 μL) and 0.5 mg/mL fluorescence enzyme substrate (Gly-Asp-Asp-Asp-Asp-Lys-β-Naphtylamide, 25 μL) were mixed, and recombinant human enteropeptidase (R&D Systems, Inc., 25 μL) was added. .. Using a fluorescence plate reader fmax (Molecular Devices, Inc.), the reaction rate was measured from the time-course changes at excitation wavelength 320 nm and fluorescence wavelength 405 nm.

    Article Title: Heteroarylcarboxylic acid ester derivative
    Article Snippet: .. Using a 96 well plate (#3915, Costar), a test compound (25 μL), 400 mM Tris-HCl buffer (pH 8.0, 25 μL) and 0.5 mg/mL fluorescence enzyme substrate (Gly-Asp-Asp-Asp-Asp-Lys-β-Naphtylamide, 25 μL) were mixed, and recombinant human enteropeptidase (R&D Systems, Inc., 25 μL) was added. .. Using a fluorescence plate reader fmax (Molecular Devices, Inc.), the reaction rate was measured from the time-course changes at excitation wavelength 320 nm and fluorescence wavelength 405 nm.

    Article Title: Heteroarylcarboxylic acid ester derivative
    Article Snippet: .. Using a 96 well plate (#3915, Costar), a test compound (25 μL), 400 mM Tris-HCl buffer (pH 8.0, 25 μL) and 0.5 mg/mL fluorescence enzyme substrate (Gly-Asp-Asp-Asp-Asp-Lys-β-Naphtylamide, 25 μL) were mixed, and recombinant human enteropeptidase (R&D Systems, Inc., 25 μL) was added. .. Using a fluorescence plate reader fmax (Molecular Devices, Inc.), the reaction rate was measured from the time-course changes at excitation wavelength 320 nm and fluorescence wavelength 405 nm.

    Article Title: CHYMOTRYPSIN C (CALDECRIN) STIMULATES AUTOACTIVATION OF HUMAN CATONIC TRYPSINOGEN
    Article Snippet: .. After recording the absorbance change at 405 nm for 1 min in a microplate reader, 0.032 nM recombinant human enteropeptidase (R & D Systems, Minneapolis) or 10 nM cationic trypsin was added (final concentrations). ..

    Article Title: Heteroarylcarboxylic acid ester derivative
    Article Snippet: .. Using a 96 well plate (#3915, Costar), a test compound (25 μL), 400 mM Tris-HCl buffer (pH 8.0, 25 μL) and 0.5 mg/mL fluorescence enzyme substrate (Gly-Asp-Asp-Asp-Asp-Lys-β-Naphtylamide, 25 μL) were mixed, and recombinant human enteropeptidase (R&D Systems, Inc., 25 μL) was added. .. Using a fluorescence plate reader fmax (Molecular Devices, Inc.), the reaction rate was measured from the time-course changes at excitation wavelength 320 nm and fluorescence wavelength 405 nm.

    Article Title: Heteroarylcarboxylic acid ester derivative
    Article Snippet: .. Using a 96 well plate (#3915, Costar), a test compound (25 μL), 400 mM Tris-HCl buffer (pH 8.0, 25 μL) and 0.5 mg/mL, fluorescence enzyme substrate (Gly-Asp-Asp-Asp-Asp-Lys-β-Naphtylamide, 25 μL) were mixed, and recombinant human enteropeptidase (R&D Systems, Inc., 25 μL) was added. .. Using a fluorescence plate reader fmax (Molecular Devices, Inc.), the reaction rate was measured from the time-course changes at excitation wavelength 320 nm and fluorescence wavelength 405 nm.

    Article Title: Heteroarylcarboxylic acid ester derivative
    Article Snippet: .. Using a 96 well plate (#3915, Costar), a test compound (25 μL), 400 mM Tris-HCl buffer (pH 8.0, 25 μL) and 0.5 mg/mL fluorescence enzyme substrate (Gly-Asp-Asp-Asp-Asp-Lys-β-Naphtylamide, 25 μL) were mixed, and recombinant human enteropeptidase (R&D Systems, Inc., 25 μL) was added. .. Using a fluorescence plate reader fmax (Molecular Devices, Inc.), the reaction rate was measured from the time-course changes at excitation wavelength 320 nm and fluorescence wavelength 405 nm.

    other:

    Article Title: Heterocyclic carboxylic acid ester derivative
    Article Snippet: Using a fluorescence plate reader fmax (Molecular Devices, Inc.), the reaction rate was measured from the time-course changes at excitation wavelength 320 nm and fluorescence wavelength 405 nm.



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    Image Search Results


    Small-molecule enteropeptidase inhibitors that exert pharmacological effects in DIO mice.

    Journal: Journal of Medicinal Chemistry

    Article Title: Design, Synthesis, and Biological Evaluation of a Novel Series of 4-Guanidinobenzoate Derivatives as Enteropeptidase Inhibitors with Low Systemic Exposure for the Treatment of Obesity

    doi: 10.1021/acs.jmedchem.2c00463

    Figure Lengend Snippet: Small-molecule enteropeptidase inhibitors that exert pharmacological effects in DIO mice.

    Article Snippet: 10 μL of compound solution was added in 96-well plate (corning), and then, 10 μL of 100 mU/mL human recombinant enteropeptidase (ITSI-Biosciences) solution was added into the plate and incubated at room temperature for 2 h. The concentration of the compound was equal to 10-fold the IC 50 value at 120 min incubation.

    Techniques:

    Structures of 1a–1c . Human enteropeptidase IC 50(initial) refers to the inhibitory activity of human enteropeptidase after 6 min of incubation with the enzyme, substrate, and compound. Human enteropeptidase IC 50(app) refers to the apparent IC 50 value after 120 min of incubation with the enzyme, substrate, and compound.

    Journal: Journal of Medicinal Chemistry

    Article Title: Design, Synthesis, and Biological Evaluation of a Novel Series of 4-Guanidinobenzoate Derivatives as Enteropeptidase Inhibitors with Low Systemic Exposure for the Treatment of Obesity

    doi: 10.1021/acs.jmedchem.2c00463

    Figure Lengend Snippet: Structures of 1a–1c . Human enteropeptidase IC 50(initial) refers to the inhibitory activity of human enteropeptidase after 6 min of incubation with the enzyme, substrate, and compound. Human enteropeptidase IC 50(app) refers to the apparent IC 50 value after 120 min of incubation with the enzyme, substrate, and compound.

    Article Snippet: 10 μL of compound solution was added in 96-well plate (corning), and then, 10 μL of 100 mU/mL human recombinant enteropeptidase (ITSI-Biosciences) solution was added into the plate and incubated at room temperature for 2 h. The concentration of the compound was equal to 10-fold the IC 50 value at 120 min incubation.

    Techniques: Activity Assay, Incubation

    Docking model of 1c with enteropeptidase. The apo form of human enteropeptidase (PDB ID: 4DGJ ) was used as a template. The surface of the catalytic triad (His825, Asp876, and Ser971) is illustrated in cyan.

    Journal: Journal of Medicinal Chemistry

    Article Title: Design, Synthesis, and Biological Evaluation of a Novel Series of 4-Guanidinobenzoate Derivatives as Enteropeptidase Inhibitors with Low Systemic Exposure for the Treatment of Obesity

    doi: 10.1021/acs.jmedchem.2c00463

    Figure Lengend Snippet: Docking model of 1c with enteropeptidase. The apo form of human enteropeptidase (PDB ID: 4DGJ ) was used as a template. The surface of the catalytic triad (His825, Asp876, and Ser971) is illustrated in cyan.

    Article Snippet: 10 μL of compound solution was added in 96-well plate (corning), and then, 10 μL of 100 mU/mL human recombinant enteropeptidase (ITSI-Biosciences) solution was added into the plate and incubated at room temperature for 2 h. The concentration of the compound was equal to 10-fold the IC 50 value at 120 min incubation.

    Techniques:

    Proposed mechanism for enteropeptidase inhibition by 1c .

    Journal: Journal of Medicinal Chemistry

    Article Title: Design, Synthesis, and Biological Evaluation of a Novel Series of 4-Guanidinobenzoate Derivatives as Enteropeptidase Inhibitors with Low Systemic Exposure for the Treatment of Obesity

    doi: 10.1021/acs.jmedchem.2c00463

    Figure Lengend Snippet: Proposed mechanism for enteropeptidase inhibition by 1c .

    Article Snippet: 10 μL of compound solution was added in 96-well plate (corning), and then, 10 μL of 100 mU/mL human recombinant enteropeptidase (ITSI-Biosciences) solution was added into the plate and incubated at room temperature for 2 h. The concentration of the compound was equal to 10-fold the IC 50 value at 120 min incubation.

    Techniques: Inhibition

    (A) Docking model of 2a with enteropeptidase. The apo form of human enteropeptidase (PDB ID: 4DGJ ) was used as a template. The surface of the catalytic triad is highlighted in cyan. (B) Properties of 2a . (C) Increase in fecal protein output. (D) Plasma exposure of 2a by oral (60 mg/kg) and subcutaneous (10 mg/kg) administration in mice. ###; P ≤ 0.01, vs vehicle using the Aspin–Welch test vs the vehicle.

    Journal: Journal of Medicinal Chemistry

    Article Title: Design, Synthesis, and Biological Evaluation of a Novel Series of 4-Guanidinobenzoate Derivatives as Enteropeptidase Inhibitors with Low Systemic Exposure for the Treatment of Obesity

    doi: 10.1021/acs.jmedchem.2c00463

    Figure Lengend Snippet: (A) Docking model of 2a with enteropeptidase. The apo form of human enteropeptidase (PDB ID: 4DGJ ) was used as a template. The surface of the catalytic triad is highlighted in cyan. (B) Properties of 2a . (C) Increase in fecal protein output. (D) Plasma exposure of 2a by oral (60 mg/kg) and subcutaneous (10 mg/kg) administration in mice. ###; P ≤ 0.01, vs vehicle using the Aspin–Welch test vs the vehicle.

    Article Snippet: 10 μL of compound solution was added in 96-well plate (corning), and then, 10 μL of 100 mU/mL human recombinant enteropeptidase (ITSI-Biosciences) solution was added into the plate and incubated at room temperature for 2 h. The concentration of the compound was equal to 10-fold the IC 50 value at 120 min incubation.

    Techniques:

    Docking model of 4b with enteropeptidase. The apo form of human enteropeptidase (PDB ID: 4DGJ ) was used as a template. (A) Overall structure. The surface of the catalytic triad is highlighted in cyan. (B) Top view of the S2 site. (C) Replacement of the amide group of 4b with bioisosteres. (D) Superposition of 6a (green) and 6b (magenta) to enteropeptidase-docked 4b (gray) by MOE. (E) Calculation of the charge distribution.

    Journal: Journal of Medicinal Chemistry

    Article Title: Design, Synthesis, and Biological Evaluation of a Novel Series of 4-Guanidinobenzoate Derivatives as Enteropeptidase Inhibitors with Low Systemic Exposure for the Treatment of Obesity

    doi: 10.1021/acs.jmedchem.2c00463

    Figure Lengend Snippet: Docking model of 4b with enteropeptidase. The apo form of human enteropeptidase (PDB ID: 4DGJ ) was used as a template. (A) Overall structure. The surface of the catalytic triad is highlighted in cyan. (B) Top view of the S2 site. (C) Replacement of the amide group of 4b with bioisosteres. (D) Superposition of 6a (green) and 6b (magenta) to enteropeptidase-docked 4b (gray) by MOE. (E) Calculation of the charge distribution.

    Article Snippet: 10 μL of compound solution was added in 96-well plate (corning), and then, 10 μL of 100 mU/mL human recombinant enteropeptidase (ITSI-Biosciences) solution was added into the plate and incubated at room temperature for 2 h. The concentration of the compound was equal to 10-fold the IC 50 value at 120 min incubation.

    Techniques:

    Properties of ( S )-5b and 6b . Rat enteropeptidase IC 50(app) refers to the inhibitory activity of rat enteropeptidase after 120 min of incubation of the enzyme, substrate, and compound.

    Journal: Journal of Medicinal Chemistry

    Article Title: Design, Synthesis, and Biological Evaluation of a Novel Series of 4-Guanidinobenzoate Derivatives as Enteropeptidase Inhibitors with Low Systemic Exposure for the Treatment of Obesity

    doi: 10.1021/acs.jmedchem.2c00463

    Figure Lengend Snippet: Properties of ( S )-5b and 6b . Rat enteropeptidase IC 50(app) refers to the inhibitory activity of rat enteropeptidase after 120 min of incubation of the enzyme, substrate, and compound.

    Article Snippet: 10 μL of compound solution was added in 96-well plate (corning), and then, 10 μL of 100 mU/mL human recombinant enteropeptidase (ITSI-Biosciences) solution was added into the plate and incubated at room temperature for 2 h. The concentration of the compound was equal to 10-fold the IC 50 value at 120 min incubation.

    Techniques: Activity Assay, Incubation

    In Vitro Activities and T 1/2 of 2a and 3a–d

    Journal: Journal of Medicinal Chemistry

    Article Title: Design, Synthesis, and Biological Evaluation of a Novel Series of 4-Guanidinobenzoate Derivatives as Enteropeptidase Inhibitors with Low Systemic Exposure for the Treatment of Obesity

    doi: 10.1021/acs.jmedchem.2c00463

    Figure Lengend Snippet: In Vitro Activities and T 1/2 of 2a and 3a–d

    Article Snippet: 10 μL of compound solution was added in 96-well plate (corning), and then, 10 μL of 100 mU/mL human recombinant enteropeptidase (ITSI-Biosciences) solution was added into the plate and incubated at room temperature for 2 h. The concentration of the compound was equal to 10-fold the IC 50 value at 120 min incubation.

    Techniques: In Vitro

    In Vitro and In Vivo Activities of 4a–c

    Journal: Journal of Medicinal Chemistry

    Article Title: Design, Synthesis, and Biological Evaluation of a Novel Series of 4-Guanidinobenzoate Derivatives as Enteropeptidase Inhibitors with Low Systemic Exposure for the Treatment of Obesity

    doi: 10.1021/acs.jmedchem.2c00463

    Figure Lengend Snippet: In Vitro and In Vivo Activities of 4a–c

    Article Snippet: 10 μL of compound solution was added in 96-well plate (corning), and then, 10 μL of 100 mU/mL human recombinant enteropeptidase (ITSI-Biosciences) solution was added into the plate and incubated at room temperature for 2 h. The concentration of the compound was equal to 10-fold the IC 50 value at 120 min incubation.

    Techniques: In Vitro, In Vivo

    In Vitro and In Vivo Activities of 5a , ( R )-5b , and ( S )-5b

    Journal: Journal of Medicinal Chemistry

    Article Title: Design, Synthesis, and Biological Evaluation of a Novel Series of 4-Guanidinobenzoate Derivatives as Enteropeptidase Inhibitors with Low Systemic Exposure for the Treatment of Obesity

    doi: 10.1021/acs.jmedchem.2c00463

    Figure Lengend Snippet: In Vitro and In Vivo Activities of 5a , ( R )-5b , and ( S )-5b

    Article Snippet: 10 μL of compound solution was added in 96-well plate (corning), and then, 10 μL of 100 mU/mL human recombinant enteropeptidase (ITSI-Biosciences) solution was added into the plate and incubated at room temperature for 2 h. The concentration of the compound was equal to 10-fold the IC 50 value at 120 min incubation.

    Techniques: In Vitro, In Vivo

    In Vitro and In Vivo Activities of 6b and 6c

    Journal: Journal of Medicinal Chemistry

    Article Title: Design, Synthesis, and Biological Evaluation of a Novel Series of 4-Guanidinobenzoate Derivatives as Enteropeptidase Inhibitors with Low Systemic Exposure for the Treatment of Obesity

    doi: 10.1021/acs.jmedchem.2c00463

    Figure Lengend Snippet: In Vitro and In Vivo Activities of 6b and 6c

    Article Snippet: 10 μL of compound solution was added in 96-well plate (corning), and then, 10 μL of 100 mU/mL human recombinant enteropeptidase (ITSI-Biosciences) solution was added into the plate and incubated at room temperature for 2 h. The concentration of the compound was equal to 10-fold the IC 50 value at 120 min incubation.

    Techniques: In Vitro, In Vivo

    Binding of different compounds to  recombinant  OBP14 of H. parallela .

    Journal: Insects

    Article Title: Evidence of the Involvement of a Plus-C Odorant-Binding Protein HparOBP14 in Host Plant Selection and Oviposition of the Scarab Beetle Holotrichia parallela

    doi: 10.3390/insects12050430

    Figure Lengend Snippet: Binding of different compounds to recombinant OBP14 of H. parallela .

    Article Snippet: The His-tag of the purified recombinant protein was removed by using recombinant enterokinase (Shanghai Korain Biotech Co Ltd., Shanghai, China), then a second purification was performed with the Ni affinity chromatography.

    Techniques: Binding Assay, Recombinant