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human bpi (Hycult Biotech)

Name: human bpi
Brand: Hycult Biotech
Rating: 90 (3 reviews)

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Hycult Biotech human bpi
Human Bpi, supplied by Hycult Biotech, 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/result/human bpi/product/Hycult Biotech
Average 90 stars, based on 1 article reviews

human bpi - by Bioz Stars, 2025-06

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Human PBMCs were isolated by dense gradient centrifugation from buffy coats. Thereafter, the cells were seeded and stimulated with purified Influenza A virus (MOI 2) (H1N1) in the presence (black bars) of increasing concentrations and absence (white bar) of human and mouse BPI-peptides (50 μg/mL, (grey bar)), and left unstimulated (control). In addition, the cells were incubated in the presence of either human BPI-peptide (50 μg/mL, huBPI) or mouse BPI-peptide (50 μg/mL, mBPI), respectively. After 20 h the supernatant was collected and the release of IFNα (A) as well as IL-6 (B) was determined by a specific ELISA. One representative experiment out of three is displayed. Statistically significant differences are given as p values (* <0.05 and ** <0.01); n = 3 ± SEM.

Journal: PLoS ONE

Article Title: The Human Antimicrobial Protein Bactericidal/Permeability-Increasing Protein (BPI) Inhibits the Infectivity of Influenza A Virus

doi: 10.1371/journal.pone.0156929

Figure Lengend Snippet: Human PBMCs were isolated by dense gradient centrifugation from buffy coats. Thereafter, the cells were seeded and stimulated with purified Influenza A virus (MOI 2) (H1N1) in the presence (black bars) of increasing concentrations and absence (white bar) of human and mouse BPI-peptides (50 μg/mL, (grey bar)), and left unstimulated (control). In addition, the cells were incubated in the presence of either human BPI-peptide (50 μg/mL, huBPI) or mouse BPI-peptide (50 μg/mL, mBPI), respectively. After 20 h the supernatant was collected and the release of IFNα (A) as well as IL-6 (B) was determined by a specific ELISA. One representative experiment out of three is displayed. Statistically significant differences are given as p values (* <0.05 and ** <0.01); n = 3 ± SEM.

Article Snippet: Finally, the detection of the binding was determined by the incubation of a rabbit anti-human BPI antiserum (Hycult Biotechnology, pAB HP9022) followed by a donkey anti-rabbit peroxidase coupled antiserum (dianova, Hamburg, Germany).

Techniques: Isolation, Gradient Centrifugation, Purification, Incubation, Enzyme-linked Immunosorbent Assay

Protease-deficient MDCK(H) cells were infected with 500 PFU/well of Influenza A virus strain A/PR/8/34 (H1N1) (A) and strain A/Aichi/2/68 (H3N2) (B) for 1 h. After the infection the virus containing supernatant was removed and the cells were grown for additional 13 h. Thereafter, the fixed and permeabilized cells were incubated with the mouse anti–nucleoprotein IAV monoclonal antibody. The binding of the antibody was detected by a donkey anti-mouse IgG-HRP antiserum and adding the reagent TMB Super Sensitive One Component HRP Microwell Substrate. Substrate conversion was detected by 450 nm. For the control sample is n = 8 ± SEM, all other samples n = 5 ± SEM. C) Calu-3 cells were infected with 300 PFU/well of Influenza A virus strain A/Aichi/2/68 (H3N2). Prior to the infection the virus was incubated in the presence or absences of the indicated amount of human or mouse BPI-peptide for 1 h. Thereafter, the virus solution was removed and the cells were incubated for 24 h. The virus amount in the supernatant was analysed by adding an aliquot of the supernatant to MDCK (H) cells for 1 h. After the infection the virus containing supernatant was removed and the cells were grown for additional 13 h. Thereafter, the fixed and permeabilized cells were incubated with the mouse anti–nucleoprotein IAV monoclonal antibody and detected as outlined above. (D) Furthermore, also the release of CCL5 into the supernatant of the infected Calu-3 cells was determined via a specific ELISA. One representative experiment out of 5 performed is displayed. Statistically significant differences are given as p values (** <0.01 and *** <0.001); n.s. is not significant; n = 3 ± SEM.

Journal: PLoS ONE

Article Title: The Human Antimicrobial Protein Bactericidal/Permeability-Increasing Protein (BPI) Inhibits the Infectivity of Influenza A Virus

doi: 10.1371/journal.pone.0156929

Figure Lengend Snippet: Protease-deficient MDCK(H) cells were infected with 500 PFU/well of Influenza A virus strain A/PR/8/34 (H1N1) (A) and strain A/Aichi/2/68 (H3N2) (B) for 1 h. After the infection the virus containing supernatant was removed and the cells were grown for additional 13 h. Thereafter, the fixed and permeabilized cells were incubated with the mouse anti–nucleoprotein IAV monoclonal antibody. The binding of the antibody was detected by a donkey anti-mouse IgG-HRP antiserum and adding the reagent TMB Super Sensitive One Component HRP Microwell Substrate. Substrate conversion was detected by 450 nm. For the control sample is n = 8 ± SEM, all other samples n = 5 ± SEM. C) Calu-3 cells were infected with 300 PFU/well of Influenza A virus strain A/Aichi/2/68 (H3N2). Prior to the infection the virus was incubated in the presence or absences of the indicated amount of human or mouse BPI-peptide for 1 h. Thereafter, the virus solution was removed and the cells were incubated for 24 h. The virus amount in the supernatant was analysed by adding an aliquot of the supernatant to MDCK (H) cells for 1 h. After the infection the virus containing supernatant was removed and the cells were grown for additional 13 h. Thereafter, the fixed and permeabilized cells were incubated with the mouse anti–nucleoprotein IAV monoclonal antibody and detected as outlined above. (D) Furthermore, also the release of CCL5 into the supernatant of the infected Calu-3 cells was determined via a specific ELISA. One representative experiment out of 5 performed is displayed. Statistically significant differences are given as p values (** <0.01 and *** <0.001); n.s. is not significant; n = 3 ± SEM.

Techniques: Infection, Incubation, Binding Assay, Enzyme-linked Immunosorbent Assay

Protease-deficient MDCK(H) cells were infected with 500 of PFU/well Influenza A virus strain A/PR/8/34 (H1N1) for 1 h. Before the infection the virus was incubated in the presence or absence of the indicated amount of human BPI-peptide or control peptides for 1 h up to 4h (A). After the infection the virus containing supernatant was removed and the cells were grown for additional 13 h. Thereafter, the fixed and permeabilized cells were incubated with the mouse anti–nucleoprotein IAV monoclonal antibody. The binding of the antibody was detected by a donkey anti-mouse IgG-HRP antiserum and adding of the reagent TMB Super Sensitive One Component HRP Microwell Substrate at 450nm. (B) MDCK (H) cells were preincubated with the indicated amount of peptides for 1 h. Thereafter the supernatant of the cells was removed and the cells were infected with 500 PFU/well Influenza A virus strain A/PR/8/34 (H1N1) for 1 h. Subsequently the infection and detection of the virus was performed as described above. One representative experiment out of 3 performed is displayed. One representative experiment out of 3 performed is shown. Statistically significant differences are given as p values (*** <0.001); n = 5 ± SEM.

Journal: PLoS ONE

Article Title: The Human Antimicrobial Protein Bactericidal/Permeability-Increasing Protein (BPI) Inhibits the Infectivity of Influenza A Virus

doi: 10.1371/journal.pone.0156929

Figure Lengend Snippet: Protease-deficient MDCK(H) cells were infected with 500 of PFU/well Influenza A virus strain A/PR/8/34 (H1N1) for 1 h. Before the infection the virus was incubated in the presence or absence of the indicated amount of human BPI-peptide or control peptides for 1 h up to 4h (A). After the infection the virus containing supernatant was removed and the cells were grown for additional 13 h. Thereafter, the fixed and permeabilized cells were incubated with the mouse anti–nucleoprotein IAV monoclonal antibody. The binding of the antibody was detected by a donkey anti-mouse IgG-HRP antiserum and adding of the reagent TMB Super Sensitive One Component HRP Microwell Substrate at 450nm. (B) MDCK (H) cells were preincubated with the indicated amount of peptides for 1 h. Thereafter the supernatant of the cells was removed and the cells were infected with 500 PFU/well Influenza A virus strain A/PR/8/34 (H1N1) for 1 h. Subsequently the infection and detection of the virus was performed as described above. One representative experiment out of 3 performed is displayed. One representative experiment out of 3 performed is shown. Statistically significant differences are given as p values (*** <0.001); n = 5 ± SEM.

Techniques: Infection, Incubation, Binding Assay

BHK-cells were infected with 360 PFU/well of VSV-GFP virus. Prior to infection the VSV was incubated with 20 μg/mL of human BPI (huBPI) and mouse BPI-peptide (mBPI), respectively or remained untreated (control) for 1 h. After 1.5 h of the cells were overlaid with 1.25% Avicel medium and incubated for 42 h. Thereafter, the cells were fixed and stained with crystal violet for 1 h at 4°C. Finally the plaques were counted (A). MDCK(H) cells were infected with 500 PFU/well Influenza A virus strain A/PR/8/34 (H1N1) for 1 h. Before the infection the virus was incubated in the presence or absence of 20 μg/mL of either human BPI-peptide (huBPI), murine BPI-peptide (mBPI), human BPI-peptide N 1 D (mutant 1), human BPI-peptide K 11 M (mutant 2), human BPI-peptide N 1 D and K 11 M (mutant 3) or left untreated (control) for 1 h (B) or incubated in the presence or absence of 20 μg/mL of either human BPI-peptide (huBPI), murine BPI-peptide (mBPI), mouse BPI-peptide D 1 N and M 11 K (mutant 4) or left untreated (control) for 1 h (C). After the infection the virus containing supernatant was removed and the cells were grown for additional 13 h. Thereafter, the fixed and permeabilized cells were incubated with the mouse anti–nucleoprotein IAV monoclonal antibody. The binding of the antibody was detected by a donkey anti-mouse IgG-HRP antiserum and adding of the reagent TMB Super Sensitive One Component HRP Microwell Substrate. Substrate conversion was detected by 450 nm. One representative experiment out of 3 performed is shown. Statistically significant differences are given as p values (*** <0.001); n.s. is not significant; n = 5 ± SEM.

Journal: PLoS ONE

Article Title: The Human Antimicrobial Protein Bactericidal/Permeability-Increasing Protein (BPI) Inhibits the Infectivity of Influenza A Virus

doi: 10.1371/journal.pone.0156929

Figure Lengend Snippet: BHK-cells were infected with 360 PFU/well of VSV-GFP virus. Prior to infection the VSV was incubated with 20 μg/mL of human BPI (huBPI) and mouse BPI-peptide (mBPI), respectively or remained untreated (control) for 1 h. After 1.5 h of the cells were overlaid with 1.25% Avicel medium and incubated for 42 h. Thereafter, the cells were fixed and stained with crystal violet for 1 h at 4°C. Finally the plaques were counted (A). MDCK(H) cells were infected with 500 PFU/well Influenza A virus strain A/PR/8/34 (H1N1) for 1 h. Before the infection the virus was incubated in the presence or absence of 20 μg/mL of either human BPI-peptide (huBPI), murine BPI-peptide (mBPI), human BPI-peptide N 1 D (mutant 1), human BPI-peptide K 11 M (mutant 2), human BPI-peptide N 1 D and K 11 M (mutant 3) or left untreated (control) for 1 h (B) or incubated in the presence or absence of 20 μg/mL of either human BPI-peptide (huBPI), murine BPI-peptide (mBPI), mouse BPI-peptide D 1 N and M 11 K (mutant 4) or left untreated (control) for 1 h (C). After the infection the virus containing supernatant was removed and the cells were grown for additional 13 h. Thereafter, the fixed and permeabilized cells were incubated with the mouse anti–nucleoprotein IAV monoclonal antibody. The binding of the antibody was detected by a donkey anti-mouse IgG-HRP antiserum and adding of the reagent TMB Super Sensitive One Component HRP Microwell Substrate. Substrate conversion was detected by 450 nm. One representative experiment out of 3 performed is shown. Statistically significant differences are given as p values (*** <0.001); n.s. is not significant; n = 5 ± SEM.

Techniques: Infection, Incubation, Staining, Mutagenesis, Binding Assay

Virus particles were incubated either with 100 (100) and 500 μg/mL (500) of human (A) or murine BPI-peptides (B) for 1 h or left untreated (C). After the incubation the virus particles were visualized by transmission electron microscopy. Therefore, the particles were negatively stained with 2% uranylacetate and transmission electron microscopy was carried out using a JEOL TEM 2100 at 120kV. Micrographs were recorded with a fast-scan 2k x 2k CCD camera F214. One representative experiment out of 3 performed is displayed.

Journal: PLoS ONE

Article Title: The Human Antimicrobial Protein Bactericidal/Permeability-Increasing Protein (BPI) Inhibits the Infectivity of Influenza A Virus

doi: 10.1371/journal.pone.0156929

Figure Lengend Snippet: Virus particles were incubated either with 100 (100) and 500 μg/mL (500) of human (A) or murine BPI-peptides (B) for 1 h or left untreated (C). After the incubation the virus particles were visualized by transmission electron microscopy. Therefore, the particles were negatively stained with 2% uranylacetate and transmission electron microscopy was carried out using a JEOL TEM 2100 at 120kV. Micrographs were recorded with a fast-scan 2k x 2k CCD camera F214. One representative experiment out of 3 performed is displayed.

Techniques: Incubation, Transmission Assay, Electron Microscopy, Staining

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