d. pteronyssinus Search Results


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  • 90
    Greer Laboratories d pteronyssinus
    Translated Der f 1 polypeptide aligned with cysteine proteases of other mite species: Dermatophagoides <t>pteronyssinus</t> (Der p 1: present study, and U11695.1for Der p 1 to complete our partial signal peptide sequence), Euroglyphus maynei (Eur m 1:AAC82352.), Psoroptes ovis (Pso o 1:Q1EIQ3.1), Sarcoptes scabiei (Sar s 1: AAS93667.1), Acarus siro (Acr s: ABU50820.1), Blomia tropicalis (Blo t 1: AAQ24541.1) and Tyrophagus putrescentiae (Tyr p 1: ABM53753.1). Numbers inside triangles indicate the number of amino acids (aa). The “No data” box indicates missing 5′ ends.). AB034946 sequence was used to complete our partial Der f 1 signal peptide sequence.
    D Pteronyssinus, supplied by Greer Laboratories, used in various techniques. Bioz Stars score: 90/100, based on 45 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Greer Laboratories hdm d pteronyssinus
    Translated Der f 1 polypeptide aligned with cysteine proteases of other mite species: Dermatophagoides <t>pteronyssinus</t> (Der p 1: present study, and U11695.1for Der p 1 to complete our partial signal peptide sequence), Euroglyphus maynei (Eur m 1:AAC82352.), Psoroptes ovis (Pso o 1:Q1EIQ3.1), Sarcoptes scabiei (Sar s 1: AAS93667.1), Acarus siro (Acr s: ABU50820.1), Blomia tropicalis (Blo t 1: AAQ24541.1) and Tyrophagus putrescentiae (Tyr p 1: ABM53753.1). Numbers inside triangles indicate the number of amino acids (aa). The “No data” box indicates missing 5′ ends.). AB034946 sequence was used to complete our partial Der f 1 signal peptide sequence.
    Hdm D Pteronyssinus, supplied by Greer Laboratories, used in various techniques. Bioz Stars score: 93/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Greer Laboratories d pteronyssinus hdm lysate
    Translated Der f 1 polypeptide aligned with cysteine proteases of other mite species: Dermatophagoides <t>pteronyssinus</t> (Der p 1: present study, and U11695.1for Der p 1 to complete our partial signal peptide sequence), Euroglyphus maynei (Eur m 1:AAC82352.), Psoroptes ovis (Pso o 1:Q1EIQ3.1), Sarcoptes scabiei (Sar s 1: AAS93667.1), Acarus siro (Acr s: ABU50820.1), Blomia tropicalis (Blo t 1: AAQ24541.1) and Tyrophagus putrescentiae (Tyr p 1: ABM53753.1). Numbers inside triangles indicate the number of amino acids (aa). The “No data” box indicates missing 5′ ends.). AB034946 sequence was used to complete our partial Der f 1 signal peptide sequence.
    D Pteronyssinus Hdm Lysate, supplied by Greer Laboratories, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Allergon d pteronyssinus whole bodies
    Translated Der f 1 polypeptide aligned with cysteine proteases of other mite species: Dermatophagoides <t>pteronyssinus</t> (Der p 1: present study, and U11695.1for Der p 1 to complete our partial signal peptide sequence), Euroglyphus maynei (Eur m 1:AAC82352.), Psoroptes ovis (Pso o 1:Q1EIQ3.1), Sarcoptes scabiei (Sar s 1: AAS93667.1), Acarus siro (Acr s: ABU50820.1), Blomia tropicalis (Blo t 1: AAQ24541.1) and Tyrophagus putrescentiae (Tyr p 1: ABM53753.1). Numbers inside triangles indicate the number of amino acids (aa). The “No data” box indicates missing 5′ ends.). AB034946 sequence was used to complete our partial Der f 1 signal peptide sequence.
    D Pteronyssinus Whole Bodies, supplied by Allergon, used in various techniques. Bioz Stars score: 85/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cosmo Bio d pteronyssinus
    Translated Der f 1 polypeptide aligned with cysteine proteases of other mite species: Dermatophagoides <t>pteronyssinus</t> (Der p 1: present study, and U11695.1for Der p 1 to complete our partial signal peptide sequence), Euroglyphus maynei (Eur m 1:AAC82352.), Psoroptes ovis (Pso o 1:Q1EIQ3.1), Sarcoptes scabiei (Sar s 1: AAS93667.1), Acarus siro (Acr s: ABU50820.1), Blomia tropicalis (Blo t 1: AAQ24541.1) and Tyrophagus putrescentiae (Tyr p 1: ABM53753.1). Numbers inside triangles indicate the number of amino acids (aa). The “No data” box indicates missing 5′ ends.). AB034946 sequence was used to complete our partial Der f 1 signal peptide sequence.
    D Pteronyssinus, supplied by Cosmo Bio, used in various techniques. Bioz Stars score: 90/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    LETI Pharma GmBH d pteronyssinus
    Translated Der f 1 polypeptide aligned with cysteine proteases of other mite species: Dermatophagoides <t>pteronyssinus</t> (Der p 1: present study, and U11695.1for Der p 1 to complete our partial signal peptide sequence), Euroglyphus maynei (Eur m 1:AAC82352.), Psoroptes ovis (Pso o 1:Q1EIQ3.1), Sarcoptes scabiei (Sar s 1: AAS93667.1), Acarus siro (Acr s: ABU50820.1), Blomia tropicalis (Blo t 1: AAQ24541.1) and Tyrophagus putrescentiae (Tyr p 1: ABM53753.1). Numbers inside triangles indicate the number of amino acids (aa). The “No data” box indicates missing 5′ ends.). AB034946 sequence was used to complete our partial Der f 1 signal peptide sequence.
    D Pteronyssinus, supplied by LETI Pharma GmBH, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    ALK-Abello d pteronyssinus
    Translated Der f 1 polypeptide aligned with cysteine proteases of other mite species: Dermatophagoides <t>pteronyssinus</t> (Der p 1: present study, and U11695.1for Der p 1 to complete our partial signal peptide sequence), Euroglyphus maynei (Eur m 1:AAC82352.), Psoroptes ovis (Pso o 1:Q1EIQ3.1), Sarcoptes scabiei (Sar s 1: AAS93667.1), Acarus siro (Acr s: ABU50820.1), Blomia tropicalis (Blo t 1: AAQ24541.1) and Tyrophagus putrescentiae (Tyr p 1: ABM53753.1). Numbers inside triangles indicate the number of amino acids (aa). The “No data” box indicates missing 5′ ends.). AB034946 sequence was used to complete our partial Der f 1 signal peptide sequence.
    D Pteronyssinus, supplied by ALK-Abello, used in various techniques. Bioz Stars score: 93/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Allergy Therapeutics PLC d pteronyssinus
    Translated Der f 1 polypeptide aligned with cysteine proteases of other mite species: Dermatophagoides <t>pteronyssinus</t> (Der p 1: present study, and U11695.1for Der p 1 to complete our partial signal peptide sequence), Euroglyphus maynei (Eur m 1:AAC82352.), Psoroptes ovis (Pso o 1:Q1EIQ3.1), Sarcoptes scabiei (Sar s 1: AAS93667.1), Acarus siro (Acr s: ABU50820.1), Blomia tropicalis (Blo t 1: AAQ24541.1) and Tyrophagus putrescentiae (Tyr p 1: ABM53753.1). Numbers inside triangles indicate the number of amino acids (aa). The “No data” box indicates missing 5′ ends.). AB034946 sequence was used to complete our partial Der f 1 signal peptide sequence.
    D Pteronyssinus, supplied by Allergy Therapeutics PLC, used in various techniques. Bioz Stars score: 90/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Indoor Biotechnologies d pteronyssinus
    Translated Der f 1 polypeptide aligned with cysteine proteases of other mite species: Dermatophagoides <t>pteronyssinus</t> (Der p 1: present study, and U11695.1for Der p 1 to complete our partial signal peptide sequence), Euroglyphus maynei (Eur m 1:AAC82352.), Psoroptes ovis (Pso o 1:Q1EIQ3.1), Sarcoptes scabiei (Sar s 1: AAS93667.1), Acarus siro (Acr s: ABU50820.1), Blomia tropicalis (Blo t 1: AAQ24541.1) and Tyrophagus putrescentiae (Tyr p 1: ABM53753.1). Numbers inside triangles indicate the number of amino acids (aa). The “No data” box indicates missing 5′ ends.). AB034946 sequence was used to complete our partial Der f 1 signal peptide sequence.
    D Pteronyssinus, supplied by Indoor Biotechnologies, used in various techniques. Bioz Stars score: 90/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher d pteronyssinus
    Translated Der f 1 polypeptide aligned with cysteine proteases of other mite species: Dermatophagoides <t>pteronyssinus</t> (Der p 1: present study, and U11695.1for Der p 1 to complete our partial signal peptide sequence), Euroglyphus maynei (Eur m 1:AAC82352.), Psoroptes ovis (Pso o 1:Q1EIQ3.1), Sarcoptes scabiei (Sar s 1: AAS93667.1), Acarus siro (Acr s: ABU50820.1), Blomia tropicalis (Blo t 1: AAQ24541.1) and Tyrophagus putrescentiae (Tyr p 1: ABM53753.1). Numbers inside triangles indicate the number of amino acids (aa). The “No data” box indicates missing 5′ ends.). AB034946 sequence was used to complete our partial Der f 1 signal peptide sequence.
    D Pteronyssinus, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 91/100, based on 95 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Immunotec d pteronyssinus extract
    A paired correlation chart between the symptom score of the NPT with D. <t>pteronyssinus</t> and the FEV 1 relative decrease after NPT in subjects with allergic rhinitis and a decrease in FEV 1 ≥ 1%.
    D Pteronyssinus Extract, supplied by Immunotec, used in various techniques. Bioz Stars score: 88/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Biomay d pteronyssinus 23
    A paired correlation chart between the symptom score of the NPT with D. <t>pteronyssinus</t> and the FEV 1 relative decrease after NPT in subjects with allergic rhinitis and a decrease in FEV 1 ≥ 1%.
    D Pteronyssinus 23, supplied by Biomay, used in various techniques. Bioz Stars score: 92/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    ALK-Abello endotoxin free d pteronyssinus antigen
    A paired correlation chart between the symptom score of the NPT with D. <t>pteronyssinus</t> and the FEV 1 relative decrease after NPT in subjects with allergic rhinitis and a decrease in FEV 1 ≥ 1%.
    Endotoxin Free D Pteronyssinus Antigen, supplied by ALK-Abello, used in various techniques. Bioz Stars score: 85/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Janssen d pteronyssinus culture
    Secondary structures of non-coding regions of the mt genome of D. <t>pteronyssinus</t> . Secondary structure of non-coding regions between (A) trnF and trnS 1 (large non-coding region); (B) trnS 2 and trnA; (C) trnA and trnP; (D) nad1 and nad6 . All structures were constructed using Mfold [ 103 ]. Inferred Watson-Crick bonds are illustrated by lines, whereas GU bonds are illustrated by dots.
    D Pteronyssinus Culture, supplied by Janssen, used in various techniques. Bioz Stars score: 85/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Stallergenes d pteronyssinus spt solutions
    Secondary structures of non-coding regions of the mt genome of D. <t>pteronyssinus</t> . Secondary structure of non-coding regions between (A) trnF and trnS 1 (large non-coding region); (B) trnS 2 and trnA; (C) trnA and trnP; (D) nad1 and nad6 . All structures were constructed using Mfold [ 103 ]. Inferred Watson-Crick bonds are illustrated by lines, whereas GU bonds are illustrated by dots.
    D Pteronyssinus Spt Solutions, supplied by Stallergenes, used in various techniques. Bioz Stars score: 85/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Greer Laboratories d pteronyssinus soluble extract
    Secondary structures of non-coding regions of the mt genome of D. <t>pteronyssinus</t> . Secondary structure of non-coding regions between (A) trnF and trnS 1 (large non-coding region); (B) trnS 2 and trnA; (C) trnA and trnP; (D) nad1 and nad6 . All structures were constructed using Mfold [ 103 ]. Inferred Watson-Crick bonds are illustrated by lines, whereas GU bonds are illustrated by dots.
    D Pteronyssinus Soluble Extract, supplied by Greer Laboratories, used in various techniques. Bioz Stars score: 93/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Eppendorf AG 1000 d pteronyssinus mites
    Secondary structures of non-coding regions of the mt genome of D. <t>pteronyssinus</t> . Secondary structure of non-coding regions between (A) trnF and trnS 1 (large non-coding region); (B) trnS 2 and trnA; (C) trnA and trnP; (D) nad1 and nad6 . All structures were constructed using Mfold [ 103 ]. Inferred Watson-Crick bonds are illustrated by lines, whereas GU bonds are illustrated by dots.
    1000 D Pteronyssinus Mites, supplied by Eppendorf AG, used in various techniques. Bioz Stars score: 85/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    Allergon allergen extract preparation lyophilized d pteronyssinus mites
    Secondary structures of non-coding regions of the mt genome of D. <t>pteronyssinus</t> . Secondary structure of non-coding regions between (A) trnF and trnS 1 (large non-coding region); (B) trnS 2 and trnA; (C) trnA and trnP; (D) nad1 and nad6 . All structures were constructed using Mfold [ 103 ]. Inferred Watson-Crick bonds are illustrated by lines, whereas GU bonds are illustrated by dots.
    Allergen Extract Preparation Lyophilized D Pteronyssinus Mites, supplied by Allergon, used in various techniques. Bioz Stars score: 89/100, based on 36 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Translated Der f 1 polypeptide aligned with cysteine proteases of other mite species: Dermatophagoides pteronyssinus (Der p 1: present study, and U11695.1for Der p 1 to complete our partial signal peptide sequence), Euroglyphus maynei (Eur m 1:AAC82352.), Psoroptes ovis (Pso o 1:Q1EIQ3.1), Sarcoptes scabiei (Sar s 1: AAS93667.1), Acarus siro (Acr s: ABU50820.1), Blomia tropicalis (Blo t 1: AAQ24541.1) and Tyrophagus putrescentiae (Tyr p 1: ABM53753.1). Numbers inside triangles indicate the number of amino acids (aa). The “No data” box indicates missing 5′ ends.). AB034946 sequence was used to complete our partial Der f 1 signal peptide sequence.

    Journal: PLoS ONE

    Article Title: Group 1 Allergen Genes in Two Species of House Dust Mites, Dermatophagoides farinae and D. pteronyssinus (Acari: Pyroglyphidae): Direct Sequencing, Characterization and Polymorphism

    doi: 10.1371/journal.pone.0114636

    Figure Lengend Snippet: Translated Der f 1 polypeptide aligned with cysteine proteases of other mite species: Dermatophagoides pteronyssinus (Der p 1: present study, and U11695.1for Der p 1 to complete our partial signal peptide sequence), Euroglyphus maynei (Eur m 1:AAC82352.), Psoroptes ovis (Pso o 1:Q1EIQ3.1), Sarcoptes scabiei (Sar s 1: AAS93667.1), Acarus siro (Acr s: ABU50820.1), Blomia tropicalis (Blo t 1: AAQ24541.1) and Tyrophagus putrescentiae (Tyr p 1: ABM53753.1). Numbers inside triangles indicate the number of amino acids (aa). The “No data” box indicates missing 5′ ends.). AB034946 sequence was used to complete our partial Der f 1 signal peptide sequence.

    Article Snippet: Specimens of D. pteronyssinus originated from cultures in Greer Laboratories, North Carolina, USA.

    Techniques: Sequencing

    Competitive blocking assay for anti-Dectin-2 monoclonal antibodies in Dectin-2.Fc fusion protein to house dust mite, ( a ) The house dust mite Dermatophagoides pteronyssinus was coated and placed on an ELISA plate; then, the anti-Dectin-2 MoAbs 6A4G7 and 17A1D10 were added to compete the binding between D. pteronyssinus and Dectin-2.Fc. b and c Dectin-2.Fc fusion protein (10 μg/mL) was incubated on either the non-coated plates or the D. pteronyssinus -coated plates in the presence or absence of the anti-Dectin-2 MoAb 6A4G7 ( b ) or 17A1D10 ( c ) and IgG2a. HRP-conjugated goat anti-mouse MoAb was added, and absorbance at 450 nm was measured using a spectrophotometer. In non-coated plates (white column), binding of Dectin-2.Fc with any of the MoAbs was not observed. Conversely, Dectin-2.Fc was found to bind to D. pteronyssinus -coated plates (black column) in the presence and absence of IgG2a. Student’s t-test was used to compare MoAb treatment with the control IgG2a. * p

    Journal: Journal of Biomedical Science

    Article Title: Antibody blockade of Dectin-2 suppresses house dust mite-induced Th2 cytokine production in dendritic cell- and monocyte-depleted peripheral blood mononuclear cell co-cultures from asthma patients

    doi: 10.1186/s12929-019-0598-6

    Figure Lengend Snippet: Competitive blocking assay for anti-Dectin-2 monoclonal antibodies in Dectin-2.Fc fusion protein to house dust mite, ( a ) The house dust mite Dermatophagoides pteronyssinus was coated and placed on an ELISA plate; then, the anti-Dectin-2 MoAbs 6A4G7 and 17A1D10 were added to compete the binding between D. pteronyssinus and Dectin-2.Fc. b and c Dectin-2.Fc fusion protein (10 μg/mL) was incubated on either the non-coated plates or the D. pteronyssinus -coated plates in the presence or absence of the anti-Dectin-2 MoAb 6A4G7 ( b ) or 17A1D10 ( c ) and IgG2a. HRP-conjugated goat anti-mouse MoAb was added, and absorbance at 450 nm was measured using a spectrophotometer. In non-coated plates (white column), binding of Dectin-2.Fc with any of the MoAbs was not observed. Conversely, Dectin-2.Fc was found to bind to D. pteronyssinus -coated plates (black column) in the presence and absence of IgG2a. Student’s t-test was used to compare MoAb treatment with the control IgG2a. * p

    Article Snippet: D. pteronyssinus extract (lot number 215941, 23.0 EU/mg endotoxin, Greer Laboratories, Inc., Lenoir, NC, USA), at a final concentration of 30 μg/mL in 100 mM sodium bicarbonate (pH 9.6), was incubated with polymyxin B (PMB) (Sigma Cheical Co., St. Louis, MO, USA), at a final concentration of 1 μg/mL of at 37 °C for 1 hh, to remove lipopolysaccharide (LPS) contamination and was coated overnight at 4 °C onto 96-well plates at 50 μL per well.

    Techniques: Blocking Assay, Enzyme-linked Immunosorbent Assay, Binding Assay, Incubation, Spectrophotometry

    Anti-Dectin-2 monoclonal antibodies inhibited Der p 2-stimulated T-helper 2 cell cytokine production in monocyte-derived DC/CD14 − PBMC co-culture, PBMCs were obtained from six patients with asthma with high level of anti-D. pteronyssinus IgE. Monocyte-derived DCs (MoDCs) and CD14 − PBMCs were prepared as described in the Materials and Methods section. Der p 2 was added to the co-cultures of MoDCs and CD14 − PBMC at a final concentration of 1 ( a ) or 3 ( b ) μg/mL. Anti-Dectin-2 monoclonal antibody (MoAb) 6A4G7 and 17A1D10 were added at a final concentration of 0.3, 1, or 3 μg/mL. IgG2a, at a final concentration of 3 μg/mL, was used as an isotype control. After second stimulation, the supernatant was harvested and IL-5 and IL-13 levels were measured by ELISA. Mann–Whitney U test was used to compare the percent inhibition of cytokine release between anti-Dectin-2 MoAb and IgG2a. * p

    Journal: Journal of Biomedical Science

    Article Title: Antibody blockade of Dectin-2 suppresses house dust mite-induced Th2 cytokine production in dendritic cell- and monocyte-depleted peripheral blood mononuclear cell co-cultures from asthma patients

    doi: 10.1186/s12929-019-0598-6

    Figure Lengend Snippet: Anti-Dectin-2 monoclonal antibodies inhibited Der p 2-stimulated T-helper 2 cell cytokine production in monocyte-derived DC/CD14 − PBMC co-culture, PBMCs were obtained from six patients with asthma with high level of anti-D. pteronyssinus IgE. Monocyte-derived DCs (MoDCs) and CD14 − PBMCs were prepared as described in the Materials and Methods section. Der p 2 was added to the co-cultures of MoDCs and CD14 − PBMC at a final concentration of 1 ( a ) or 3 ( b ) μg/mL. Anti-Dectin-2 monoclonal antibody (MoAb) 6A4G7 and 17A1D10 were added at a final concentration of 0.3, 1, or 3 μg/mL. IgG2a, at a final concentration of 3 μg/mL, was used as an isotype control. After second stimulation, the supernatant was harvested and IL-5 and IL-13 levels were measured by ELISA. Mann–Whitney U test was used to compare the percent inhibition of cytokine release between anti-Dectin-2 MoAb and IgG2a. * p

    Article Snippet: D. pteronyssinus extract (lot number 215941, 23.0 EU/mg endotoxin, Greer Laboratories, Inc., Lenoir, NC, USA), at a final concentration of 30 μg/mL in 100 mM sodium bicarbonate (pH 9.6), was incubated with polymyxin B (PMB) (Sigma Cheical Co., St. Louis, MO, USA), at a final concentration of 1 μg/mL of at 37 °C for 1 hh, to remove lipopolysaccharide (LPS) contamination and was coated overnight at 4 °C onto 96-well plates at 50 μL per well.

    Techniques: Derivative Assay, Co-Culture Assay, Concentration Assay, Enzyme-linked Immunosorbent Assay, MANN-WHITNEY, Inhibition

    Anti-Dectin-2 monoclonal antibodies inhibited Dermatophagoides pteronyssinus -stimulated T-helper 2 cell cytokine production in monocyte-derived DC/CD14 − PBMC co-culture, PBMCs were obtained from six patients with asthma with high level of anti-D. pteronyssinus IgE. Monocyte-derived DCs (MoDCs) and CD14 − PBMCs were prepared as described in the Materials and Methods section. D. pteronyssinus was added to the co-cultures of MoDCs and CD14 − PBMC at a final concentration of 1 ( a ) or 3 ( b ) μg/mL. Anti-Dectin-2 monoclonal antibody (MoAb) 6A4G7 or 17A1D10 was added at a final concentration of 0.3, 1, or 3 μg/mL. IgG2a, at a final concentration of 3 μg/mL, was used as an isotype control. After 6 days of co-culture, the supernatant was removed, and the cells were co-cultured with the same concentration of D. pteronyssinus and anti-Dectin-2 MoAbs for another 6 days. The supernatant was harvested, and IL-5 and IL-13 levels were measured by ELISA. Mann–Whitney U test was used to compare the percent inhibition of cytokine release between anti-Dectin-2 MoAb and IgG2a. * p

    Journal: Journal of Biomedical Science

    Article Title: Antibody blockade of Dectin-2 suppresses house dust mite-induced Th2 cytokine production in dendritic cell- and monocyte-depleted peripheral blood mononuclear cell co-cultures from asthma patients

    doi: 10.1186/s12929-019-0598-6

    Figure Lengend Snippet: Anti-Dectin-2 monoclonal antibodies inhibited Dermatophagoides pteronyssinus -stimulated T-helper 2 cell cytokine production in monocyte-derived DC/CD14 − PBMC co-culture, PBMCs were obtained from six patients with asthma with high level of anti-D. pteronyssinus IgE. Monocyte-derived DCs (MoDCs) and CD14 − PBMCs were prepared as described in the Materials and Methods section. D. pteronyssinus was added to the co-cultures of MoDCs and CD14 − PBMC at a final concentration of 1 ( a ) or 3 ( b ) μg/mL. Anti-Dectin-2 monoclonal antibody (MoAb) 6A4G7 or 17A1D10 was added at a final concentration of 0.3, 1, or 3 μg/mL. IgG2a, at a final concentration of 3 μg/mL, was used as an isotype control. After 6 days of co-culture, the supernatant was removed, and the cells were co-cultured with the same concentration of D. pteronyssinus and anti-Dectin-2 MoAbs for another 6 days. The supernatant was harvested, and IL-5 and IL-13 levels were measured by ELISA. Mann–Whitney U test was used to compare the percent inhibition of cytokine release between anti-Dectin-2 MoAb and IgG2a. * p

    Article Snippet: D. pteronyssinus extract (lot number 215941, 23.0 EU/mg endotoxin, Greer Laboratories, Inc., Lenoir, NC, USA), at a final concentration of 30 μg/mL in 100 mM sodium bicarbonate (pH 9.6), was incubated with polymyxin B (PMB) (Sigma Cheical Co., St. Louis, MO, USA), at a final concentration of 1 μg/mL of at 37 °C for 1 hh, to remove lipopolysaccharide (LPS) contamination and was coated overnight at 4 °C onto 96-well plates at 50 μL per well.

    Techniques: Derivative Assay, Co-Culture Assay, Concentration Assay, Cell Culture, Enzyme-linked Immunosorbent Assay, MANN-WHITNEY, Inhibition

    A paired correlation chart between the symptom score of the NPT with D. pteronyssinus and the FEV 1 relative decrease after NPT in subjects with allergic rhinitis and a decrease in FEV 1 ≥ 1%.

    Journal: Allergy & Rhinology

    Article Title: Assessment of allergen-induced respiratory hyperresponsiveness before the prescription of a specific immunotherapy

    doi: 10.2500/ar.2015.6.0122

    Figure Lengend Snippet: A paired correlation chart between the symptom score of the NPT with D. pteronyssinus and the FEV 1 relative decrease after NPT in subjects with allergic rhinitis and a decrease in FEV 1 ≥ 1%.

    Article Snippet: An isotonic, buffered neutral pH aqueous solution (100 μL) with 10% w/v D. pteronyssinus extract (Immunotech, Rio de Janeiro, Brazil) adapted to room temperature was applied with a pump spray device to both nostrils of the subject.

    Techniques:

    A paired correlation chart between the symptom score of the NPT with D. pteronyssinus and the PEF relative decrease after NPT in subjects with allergic rhinitis and a decrease in PEF ≥15%.

    Journal: Allergy & Rhinology

    Article Title: Assessment of allergen-induced respiratory hyperresponsiveness before the prescription of a specific immunotherapy

    doi: 10.2500/ar.2015.6.0122

    Figure Lengend Snippet: A paired correlation chart between the symptom score of the NPT with D. pteronyssinus and the PEF relative decrease after NPT in subjects with allergic rhinitis and a decrease in PEF ≥15%.

    Article Snippet: An isotonic, buffered neutral pH aqueous solution (100 μL) with 10% w/v D. pteronyssinus extract (Immunotech, Rio de Janeiro, Brazil) adapted to room temperature was applied with a pump spray device to both nostrils of the subject.

    Techniques:

    A paired correlation chart between the symptom score of the NPT with D. pteronyssinus and the FVC relative decrease after NPT in subjects with allergic rhinitis and a decrease in FVC ≥ 0%.

    Journal: Allergy & Rhinology

    Article Title: Assessment of allergen-induced respiratory hyperresponsiveness before the prescription of a specific immunotherapy

    doi: 10.2500/ar.2015.6.0122

    Figure Lengend Snippet: A paired correlation chart between the symptom score of the NPT with D. pteronyssinus and the FVC relative decrease after NPT in subjects with allergic rhinitis and a decrease in FVC ≥ 0%.

    Article Snippet: An isotonic, buffered neutral pH aqueous solution (100 μL) with 10% w/v D. pteronyssinus extract (Immunotech, Rio de Janeiro, Brazil) adapted to room temperature was applied with a pump spray device to both nostrils of the subject.

    Techniques:

    Flow-volume and volume/time charts of the subject who was most reactive pre- and post-NPT with D. pteronyssinus (a 28-year-old woman who had an NPT-SS = 10; PEF dif% = −42%; FVC dif% = −17%; FEV 1 -FVC dif% = −9%, and FEV 1dif% = −25% after allergen-specific NPT).

    Journal: Allergy & Rhinology

    Article Title: Assessment of allergen-induced respiratory hyperresponsiveness before the prescription of a specific immunotherapy

    doi: 10.2500/ar.2015.6.0122

    Figure Lengend Snippet: Flow-volume and volume/time charts of the subject who was most reactive pre- and post-NPT with D. pteronyssinus (a 28-year-old woman who had an NPT-SS = 10; PEF dif% = −42%; FVC dif% = −17%; FEV 1 -FVC dif% = −9%, and FEV 1dif% = −25% after allergen-specific NPT).

    Article Snippet: An isotonic, buffered neutral pH aqueous solution (100 μL) with 10% w/v D. pteronyssinus extract (Immunotech, Rio de Janeiro, Brazil) adapted to room temperature was applied with a pump spray device to both nostrils of the subject.

    Techniques: Flow Cytometry

    Secondary structures of non-coding regions of the mt genome of D. pteronyssinus . Secondary structure of non-coding regions between (A) trnF and trnS 1 (large non-coding region); (B) trnS 2 and trnA; (C) trnA and trnP; (D) nad1 and nad6 . All structures were constructed using Mfold [ 103 ]. Inferred Watson-Crick bonds are illustrated by lines, whereas GU bonds are illustrated by dots.

    Journal: BMC Genomics

    Article Title: The complete mitochondrial genome of the house dust mite Dermatophagoides pteronyssinus (Trouessart): a novel gene arrangement among arthropods

    doi: 10.1186/1471-2164-10-107

    Figure Lengend Snippet: Secondary structures of non-coding regions of the mt genome of D. pteronyssinus . Secondary structure of non-coding regions between (A) trnF and trnS 1 (large non-coding region); (B) trnS 2 and trnA; (C) trnA and trnP; (D) nad1 and nad6 . All structures were constructed using Mfold [ 103 ]. Inferred Watson-Crick bonds are illustrated by lines, whereas GU bonds are illustrated by dots.

    Article Snippet: Mite strain, mass rearing and isolation The initial D. pteronyssinus culture was provided by D. Bylemans (Janssen Pharmaceutica, Belgium).

    Techniques: Construct

    Restriction digest of rolling circle amplified mitochondrial DNA of D. pteronyssinus . Rolling circle amplified mtDNA, undigested (lane 3) and digested with Xmn I (lane2) and Eco RI (lane 4). Molecular marker used was MassRuler DNA ladder Mix (Fermentas) (lane 1).

    Journal: BMC Genomics

    Article Title: The complete mitochondrial genome of the house dust mite Dermatophagoides pteronyssinus (Trouessart): a novel gene arrangement among arthropods

    doi: 10.1186/1471-2164-10-107

    Figure Lengend Snippet: Restriction digest of rolling circle amplified mitochondrial DNA of D. pteronyssinus . Rolling circle amplified mtDNA, undigested (lane 3) and digested with Xmn I (lane2) and Eco RI (lane 4). Molecular marker used was MassRuler DNA ladder Mix (Fermentas) (lane 1).

    Article Snippet: Mite strain, mass rearing and isolation The initial D. pteronyssinus culture was provided by D. Bylemans (Janssen Pharmaceutica, Belgium).

    Techniques: Amplification, Marker

    Mitochondrial gene arrangement of Limulus polyphemus, Dermatophagoides pteronyssinus and Steganacarus magnus . Graphical linearisation of mt genomes is presented according to [ 32 ]. Gene sizes are not drawn to scale. J stands for majority and N for minority strand. Protein coding and rRNA genes are abbreviated as in the abbreviations section. tRNA genes are abbreviated using the one-letter amino acid code, with L 1 = CUN; L 2 = UUR; S 1 = AGN; S 2 = UCN. White boxes represent genes with the same relative position as in the arthropod ground pattern, L. polyphemus . Light-gray boxes represent genes that changed positions relative to L. polyphemus ; dark-gray boxes represent genes that changed both position and orientation. Circular dots between the genes of D. pteronyssinus represent conserved gene boundaries compared to L. polyphemus . Square dots between the genes of S. magnus represent conserved gene boundaries compared to D. pteronyssinus .

    Journal: BMC Genomics

    Article Title: The complete mitochondrial genome of the house dust mite Dermatophagoides pteronyssinus (Trouessart): a novel gene arrangement among arthropods

    doi: 10.1186/1471-2164-10-107

    Figure Lengend Snippet: Mitochondrial gene arrangement of Limulus polyphemus, Dermatophagoides pteronyssinus and Steganacarus magnus . Graphical linearisation of mt genomes is presented according to [ 32 ]. Gene sizes are not drawn to scale. J stands for majority and N for minority strand. Protein coding and rRNA genes are abbreviated as in the abbreviations section. tRNA genes are abbreviated using the one-letter amino acid code, with L 1 = CUN; L 2 = UUR; S 1 = AGN; S 2 = UCN. White boxes represent genes with the same relative position as in the arthropod ground pattern, L. polyphemus . Light-gray boxes represent genes that changed positions relative to L. polyphemus ; dark-gray boxes represent genes that changed both position and orientation. Circular dots between the genes of D. pteronyssinus represent conserved gene boundaries compared to L. polyphemus . Square dots between the genes of S. magnus represent conserved gene boundaries compared to D. pteronyssinus .

    Article Snippet: Mite strain, mass rearing and isolation The initial D. pteronyssinus culture was provided by D. Bylemans (Janssen Pharmaceutica, Belgium).

    Techniques:

    Inferred secondary structures of the 22 mitochondrial tRNAs from D. pteronyssinus . tRNAs are shown in the order of occurrence in the mt genome starting from cox1 . Locations of adjacent gene boundaries are indicated with arrows. Green font indicates that the sequence is part of the adjacent gene. Inferred Watson-Crick bonds are illustrated by lines, whereas GU bonds are illustrated by dots.

    Journal: BMC Genomics

    Article Title: The complete mitochondrial genome of the house dust mite Dermatophagoides pteronyssinus (Trouessart): a novel gene arrangement among arthropods

    doi: 10.1186/1471-2164-10-107

    Figure Lengend Snippet: Inferred secondary structures of the 22 mitochondrial tRNAs from D. pteronyssinus . tRNAs are shown in the order of occurrence in the mt genome starting from cox1 . Locations of adjacent gene boundaries are indicated with arrows. Green font indicates that the sequence is part of the adjacent gene. Inferred Watson-Crick bonds are illustrated by lines, whereas GU bonds are illustrated by dots.

    Article Snippet: Mite strain, mass rearing and isolation The initial D. pteronyssinus culture was provided by D. Bylemans (Janssen Pharmaceutica, Belgium).

    Techniques: Sequencing

    16S-rRNA and 12S-rRNA secondary structures of the mitochondrial genome of D. pteronyssinus . The numbering of the stem-loops is after de Rijk et al . [ 75 ] for 16S-rRNA and after van de Peer et al . [ 76 ] for 12S-rRNA . Blue coloured nucleotides show 100% identity when aligned to 12S-rRNA and 16S-rRNA genes from other Acariformes (as listed in Table 1). Inferred Watson-Crick bonds are illustrated by lines, whereas GU bonds are illustrated by dots.

    Journal: BMC Genomics

    Article Title: The complete mitochondrial genome of the house dust mite Dermatophagoides pteronyssinus (Trouessart): a novel gene arrangement among arthropods

    doi: 10.1186/1471-2164-10-107

    Figure Lengend Snippet: 16S-rRNA and 12S-rRNA secondary structures of the mitochondrial genome of D. pteronyssinus . The numbering of the stem-loops is after de Rijk et al . [ 75 ] for 16S-rRNA and after van de Peer et al . [ 76 ] for 12S-rRNA . Blue coloured nucleotides show 100% identity when aligned to 12S-rRNA and 16S-rRNA genes from other Acariformes (as listed in Table 1). Inferred Watson-Crick bonds are illustrated by lines, whereas GU bonds are illustrated by dots.

    Article Snippet: Mite strain, mass rearing and isolation The initial D. pteronyssinus culture was provided by D. Bylemans (Janssen Pharmaceutica, Belgium).

    Techniques:

    Schematic representation of the mt genome of D. pteronyssinus . Except for atp8 (= 8) and nad4 (= 4L) protein coding and ribosomal genes are presented as outlined in the abbreviations section. tRNA genes are abbreviated using the one-letter amino acid code, with L 1 = CUN; L 2 = UUR; S 1 = AGN; S 2 = UCN. RNAs on the N-strand are underlined. Numbers at gene junctions indicate the length of small non-coding regions where negative numbers indicate overlap between genes. A-,T-,G- and C-content of the mt genome is represented using a red, blue, green and purple colour graded circle, respectively. Black curved lines on the outside of these circles represent mt genome coverage by Dermatophagoides ESTs (see additional file 5 for sequences of Dermatophagoides ESTs covering the mt genome of D. pteronyssinus ).

    Journal: BMC Genomics

    Article Title: The complete mitochondrial genome of the house dust mite Dermatophagoides pteronyssinus (Trouessart): a novel gene arrangement among arthropods

    doi: 10.1186/1471-2164-10-107

    Figure Lengend Snippet: Schematic representation of the mt genome of D. pteronyssinus . Except for atp8 (= 8) and nad4 (= 4L) protein coding and ribosomal genes are presented as outlined in the abbreviations section. tRNA genes are abbreviated using the one-letter amino acid code, with L 1 = CUN; L 2 = UUR; S 1 = AGN; S 2 = UCN. RNAs on the N-strand are underlined. Numbers at gene junctions indicate the length of small non-coding regions where negative numbers indicate overlap between genes. A-,T-,G- and C-content of the mt genome is represented using a red, blue, green and purple colour graded circle, respectively. Black curved lines on the outside of these circles represent mt genome coverage by Dermatophagoides ESTs (see additional file 5 for sequences of Dermatophagoides ESTs covering the mt genome of D. pteronyssinus ).

    Article Snippet: Mite strain, mass rearing and isolation The initial D. pteronyssinus culture was provided by D. Bylemans (Janssen Pharmaceutica, Belgium).

    Techniques: