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polyclonal antibodies against β 1 3 glucanase  (Agrisera)

 
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    Agrisera polyclonal antibodies against β 1 3 glucanase
    Analysis of <t>β-1,3-glucanase</t> gene expression, protein accumulation, and enzymatic activity in leaves of potato genotypes challenged with Phytophthora infestans . Transcript levels determined by qRT-PCR in resistant (A) and susceptible (B) potato inoculated with P. infestans . Protein accumulation in leaves of the resistant (C) and susceptible (D) genotypes following challenge inoculation with the pathogen. Equal amounts of protein (25 µg per lane) were loaded onto SDS–PAGE gels, and Coomassie Brilliant Blue (CBB) staining was used as a loading control. Enzymatic activity of β-1,3-glucanases was measured spectrophotometrically using laminarin as substrate in resistant (E) and susceptible (F) potato after inoculation. Values represent the mean ± SD of at least three independent experiments (n = 9). Asterisks indicate values that differ significantly from mock-inoculated (control) potato leaves at *P < 0.05.
    Polyclonal Antibodies Against β 1 3 Glucanase, supplied by Agrisera, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/polyclonal+antibodies+against+%CE%B2+1+3+glucanase/pmc13133032-147-11-15?v=Agrisera
    Average 86 stars, based on 1 article reviews
    polyclonal antibodies against β 1 3 glucanase - by Bioz Stars, 2026-07
    86/100 stars

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    1) Product Images from "Peroxynitrite-mediated tyrosine nitration modulates β-1,3-glucanase activity and potato defense against Phytophthora infestans"

    Article Title: Peroxynitrite-mediated tyrosine nitration modulates β-1,3-glucanase activity and potato defense against Phytophthora infestans

    Journal: Frontiers in Plant Science

    doi: 10.3389/fpls.2026.1796014

    Analysis of β-1,3-glucanase gene expression, protein accumulation, and enzymatic activity in leaves of potato genotypes challenged with Phytophthora infestans . Transcript levels determined by qRT-PCR in resistant (A) and susceptible (B) potato inoculated with P. infestans . Protein accumulation in leaves of the resistant (C) and susceptible (D) genotypes following challenge inoculation with the pathogen. Equal amounts of protein (25 µg per lane) were loaded onto SDS–PAGE gels, and Coomassie Brilliant Blue (CBB) staining was used as a loading control. Enzymatic activity of β-1,3-glucanases was measured spectrophotometrically using laminarin as substrate in resistant (E) and susceptible (F) potato after inoculation. Values represent the mean ± SD of at least three independent experiments (n = 9). Asterisks indicate values that differ significantly from mock-inoculated (control) potato leaves at *P < 0.05.
    Figure Legend Snippet: Analysis of β-1,3-glucanase gene expression, protein accumulation, and enzymatic activity in leaves of potato genotypes challenged with Phytophthora infestans . Transcript levels determined by qRT-PCR in resistant (A) and susceptible (B) potato inoculated with P. infestans . Protein accumulation in leaves of the resistant (C) and susceptible (D) genotypes following challenge inoculation with the pathogen. Equal amounts of protein (25 µg per lane) were loaded onto SDS–PAGE gels, and Coomassie Brilliant Blue (CBB) staining was used as a loading control. Enzymatic activity of β-1,3-glucanases was measured spectrophotometrically using laminarin as substrate in resistant (E) and susceptible (F) potato after inoculation. Values represent the mean ± SD of at least three independent experiments (n = 9). Asterisks indicate values that differ significantly from mock-inoculated (control) potato leaves at *P < 0.05.

    Techniques Used: Gene Expression, Activity Assay, Quantitative RT-PCR, SDS Page, Staining, Control

    Effect of SIN-1 (ONOO – donor) on recombinant β-1,3-glucanase activity (A) , protein accumulation and tyrosine nitration (B) . Samples were incubated at varying concentrations of SIN-1 (0.05–2 mM). Equal amounts of recombinant protein (1 µg per lane) were loaded onto the SDS-PAGE gel. Coomassie Brilliant Blue (CBB) staining served as a loading control.
    Figure Legend Snippet: Effect of SIN-1 (ONOO – donor) on recombinant β-1,3-glucanase activity (A) , protein accumulation and tyrosine nitration (B) . Samples were incubated at varying concentrations of SIN-1 (0.05–2 mM). Equal amounts of recombinant protein (1 µg per lane) were loaded onto the SDS-PAGE gel. Coomassie Brilliant Blue (CBB) staining served as a loading control.

    Techniques Used: Recombinant, Activity Assay, Nitration, Incubation, SDS Page, Staining, Control

    Structure of potato β-1,3-glucanase. The tertiary structure was generated by homology modeling, based on the coordinates of β-1,3-glucanase from Hevea brasiliensis (PDB ID: 4HPG, chain A). Surface active pocket identification by CASTp server: (A) Light Green, Red, and light yellow color boxes highlight the amino acid residues present in the binding site. (B) Shows the Tyr 59 and Tyr 203 in the catalytic pocket of β-1,3-glucanase. Calculated distances between the two Tyr residues (in Å) and the catalytic acid (E120) or the nucleophile (E265) (C, D) . Yellow dashed lines indicate distances between the residues.
    Figure Legend Snippet: Structure of potato β-1,3-glucanase. The tertiary structure was generated by homology modeling, based on the coordinates of β-1,3-glucanase from Hevea brasiliensis (PDB ID: 4HPG, chain A). Surface active pocket identification by CASTp server: (A) Light Green, Red, and light yellow color boxes highlight the amino acid residues present in the binding site. (B) Shows the Tyr 59 and Tyr 203 in the catalytic pocket of β-1,3-glucanase. Calculated distances between the two Tyr residues (in Å) and the catalytic acid (E120) or the nucleophile (E265) (C, D) . Yellow dashed lines indicate distances between the residues.

    Techniques Used: Generated, Binding Assay

    Evolutionary conservation of amino acid residues of potato β-1,3-glucanase (accession number P52401 ) was analyzed using the ConSurf server. Each residue was assigned a conservation grade ranging from 1 (variable) to 9 (highly conserved) based on a multiple-sequence alignment of homologous proteins. Residues located in the catalytic pocket are marked in black frames (A) . Characterization of the six highly conserved tyrosine (Y) residues (conservation score 9/9) present in potato β-1,3-glucanase in terms of amino acid content within a nine-residue window of linear sequence around the tyrosine (Primary structure), solvent-accessible surface area (ASA), secondary-structure organization, and residues within 5 Å from the two carbons susceptible to nitration. Residues meeting the nearby-residue criterion (basic amino acids in the immediate vicinity of the tyrosine residue within the primary sequence and/or the acidic residues within 5 Å from the atom susceptible to nitration) are shown in bold (B) .
    Figure Legend Snippet: Evolutionary conservation of amino acid residues of potato β-1,3-glucanase (accession number P52401 ) was analyzed using the ConSurf server. Each residue was assigned a conservation grade ranging from 1 (variable) to 9 (highly conserved) based on a multiple-sequence alignment of homologous proteins. Residues located in the catalytic pocket are marked in black frames (A) . Characterization of the six highly conserved tyrosine (Y) residues (conservation score 9/9) present in potato β-1,3-glucanase in terms of amino acid content within a nine-residue window of linear sequence around the tyrosine (Primary structure), solvent-accessible surface area (ASA), secondary-structure organization, and residues within 5 Å from the two carbons susceptible to nitration. Residues meeting the nearby-residue criterion (basic amino acids in the immediate vicinity of the tyrosine residue within the primary sequence and/or the acidic residues within 5 Å from the atom susceptible to nitration) are shown in bold (B) .

    Techniques Used: Residue, Sequencing, Solvent, Nitration



    Similar Products

    polyclonal antibodies against β 1 3 glucanase  (Agrisera)
    86
    Agrisera polyclonal antibodies against β 1 3 glucanase
    Analysis of <t>β-1,3-glucanase</t> gene expression, protein accumulation, and enzymatic activity in leaves of potato genotypes challenged with Phytophthora infestans . Transcript levels determined by qRT-PCR in resistant (A) and susceptible (B) potato inoculated with P. infestans . Protein accumulation in leaves of the resistant (C) and susceptible (D) genotypes following challenge inoculation with the pathogen. Equal amounts of protein (25 µg per lane) were loaded onto SDS–PAGE gels, and Coomassie Brilliant Blue (CBB) staining was used as a loading control. Enzymatic activity of β-1,3-glucanases was measured spectrophotometrically using laminarin as substrate in resistant (E) and susceptible (F) potato after inoculation. Values represent the mean ± SD of at least three independent experiments (n = 9). Asterisks indicate values that differ significantly from mock-inoculated (control) potato leaves at *P < 0.05.
    Polyclonal Antibodies Against β 1 3 Glucanase, supplied by Agrisera, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/polyclonal+antibodies+against+%CE%B2+1+3+glucanase/pmc13133032-147-11-15?v=Agrisera
    Average 86 stars, based on 1 article reviews
    polyclonal antibodies against β 1 3 glucanase - by Bioz Stars, 2026-07
    86/100 stars
    		  Buy from Supplier

    Image Search Results


    Analysis of β-1,3-glucanase gene expression, protein accumulation, and enzymatic activity in leaves of potato genotypes challenged with Phytophthora infestans . Transcript levels determined by qRT-PCR in resistant (A) and susceptible (B) potato inoculated with P. infestans . Protein accumulation in leaves of the resistant (C) and susceptible (D) genotypes following challenge inoculation with the pathogen. Equal amounts of protein (25 µg per lane) were loaded onto SDS–PAGE gels, and Coomassie Brilliant Blue (CBB) staining was used as a loading control. Enzymatic activity of β-1,3-glucanases was measured spectrophotometrically using laminarin as substrate in resistant (E) and susceptible (F) potato after inoculation. Values represent the mean ± SD of at least three independent experiments (n = 9). Asterisks indicate values that differ significantly from mock-inoculated (control) potato leaves at *P < 0.05.

    Journal: Frontiers in Plant Science

    Article Title: Peroxynitrite-mediated tyrosine nitration modulates β-1,3-glucanase activity and potato defense against Phytophthora infestans

    doi: 10.3389/fpls.2026.1796014

    Figure Lengend Snippet: Analysis of β-1,3-glucanase gene expression, protein accumulation, and enzymatic activity in leaves of potato genotypes challenged with Phytophthora infestans . Transcript levels determined by qRT-PCR in resistant (A) and susceptible (B) potato inoculated with P. infestans . Protein accumulation in leaves of the resistant (C) and susceptible (D) genotypes following challenge inoculation with the pathogen. Equal amounts of protein (25 µg per lane) were loaded onto SDS–PAGE gels, and Coomassie Brilliant Blue (CBB) staining was used as a loading control. Enzymatic activity of β-1,3-glucanases was measured spectrophotometrically using laminarin as substrate in resistant (E) and susceptible (F) potato after inoculation. Values represent the mean ± SD of at least three independent experiments (n = 9). Asterisks indicate values that differ significantly from mock-inoculated (control) potato leaves at *P < 0.05.

    Article Snippet: After transfer, the membranes were blocked (3% BSA) and incubated with polyclonal antibodies against β-1,3-glucanase (Agrisera) at a 1:1000 dilution.

    Techniques: Gene Expression, Activity Assay, Quantitative RT-PCR, SDS Page, Staining, Control

    Effect of SIN-1 (ONOO – donor) on recombinant β-1,3-glucanase activity (A) , protein accumulation and tyrosine nitration (B) . Samples were incubated at varying concentrations of SIN-1 (0.05–2 mM). Equal amounts of recombinant protein (1 µg per lane) were loaded onto the SDS-PAGE gel. Coomassie Brilliant Blue (CBB) staining served as a loading control.

    Journal: Frontiers in Plant Science

    Article Title: Peroxynitrite-mediated tyrosine nitration modulates β-1,3-glucanase activity and potato defense against Phytophthora infestans

    doi: 10.3389/fpls.2026.1796014

    Figure Lengend Snippet: Effect of SIN-1 (ONOO – donor) on recombinant β-1,3-glucanase activity (A) , protein accumulation and tyrosine nitration (B) . Samples were incubated at varying concentrations of SIN-1 (0.05–2 mM). Equal amounts of recombinant protein (1 µg per lane) were loaded onto the SDS-PAGE gel. Coomassie Brilliant Blue (CBB) staining served as a loading control.

    Article Snippet: After transfer, the membranes were blocked (3% BSA) and incubated with polyclonal antibodies against β-1,3-glucanase (Agrisera) at a 1:1000 dilution.

    Techniques: Recombinant, Activity Assay, Nitration, Incubation, SDS Page, Staining, Control

    Structure of potato β-1,3-glucanase. The tertiary structure was generated by homology modeling, based on the coordinates of β-1,3-glucanase from Hevea brasiliensis (PDB ID: 4HPG, chain A). Surface active pocket identification by CASTp server: (A) Light Green, Red, and light yellow color boxes highlight the amino acid residues present in the binding site. (B) Shows the Tyr 59 and Tyr 203 in the catalytic pocket of β-1,3-glucanase. Calculated distances between the two Tyr residues (in Å) and the catalytic acid (E120) or the nucleophile (E265) (C, D) . Yellow dashed lines indicate distances between the residues.

    Journal: Frontiers in Plant Science

    Article Title: Peroxynitrite-mediated tyrosine nitration modulates β-1,3-glucanase activity and potato defense against Phytophthora infestans

    doi: 10.3389/fpls.2026.1796014

    Figure Lengend Snippet: Structure of potato β-1,3-glucanase. The tertiary structure was generated by homology modeling, based on the coordinates of β-1,3-glucanase from Hevea brasiliensis (PDB ID: 4HPG, chain A). Surface active pocket identification by CASTp server: (A) Light Green, Red, and light yellow color boxes highlight the amino acid residues present in the binding site. (B) Shows the Tyr 59 and Tyr 203 in the catalytic pocket of β-1,3-glucanase. Calculated distances between the two Tyr residues (in Å) and the catalytic acid (E120) or the nucleophile (E265) (C, D) . Yellow dashed lines indicate distances between the residues.

    Article Snippet: After transfer, the membranes were blocked (3% BSA) and incubated with polyclonal antibodies against β-1,3-glucanase (Agrisera) at a 1:1000 dilution.

    Techniques: Generated, Binding Assay

    Evolutionary conservation of amino acid residues of potato β-1,3-glucanase (accession number P52401 ) was analyzed using the ConSurf server. Each residue was assigned a conservation grade ranging from 1 (variable) to 9 (highly conserved) based on a multiple-sequence alignment of homologous proteins. Residues located in the catalytic pocket are marked in black frames (A) . Characterization of the six highly conserved tyrosine (Y) residues (conservation score 9/9) present in potato β-1,3-glucanase in terms of amino acid content within a nine-residue window of linear sequence around the tyrosine (Primary structure), solvent-accessible surface area (ASA), secondary-structure organization, and residues within 5 Å from the two carbons susceptible to nitration. Residues meeting the nearby-residue criterion (basic amino acids in the immediate vicinity of the tyrosine residue within the primary sequence and/or the acidic residues within 5 Å from the atom susceptible to nitration) are shown in bold (B) .

    Journal: Frontiers in Plant Science

    Article Title: Peroxynitrite-mediated tyrosine nitration modulates β-1,3-glucanase activity and potato defense against Phytophthora infestans

    doi: 10.3389/fpls.2026.1796014

    Figure Lengend Snippet: Evolutionary conservation of amino acid residues of potato β-1,3-glucanase (accession number P52401 ) was analyzed using the ConSurf server. Each residue was assigned a conservation grade ranging from 1 (variable) to 9 (highly conserved) based on a multiple-sequence alignment of homologous proteins. Residues located in the catalytic pocket are marked in black frames (A) . Characterization of the six highly conserved tyrosine (Y) residues (conservation score 9/9) present in potato β-1,3-glucanase in terms of amino acid content within a nine-residue window of linear sequence around the tyrosine (Primary structure), solvent-accessible surface area (ASA), secondary-structure organization, and residues within 5 Å from the two carbons susceptible to nitration. Residues meeting the nearby-residue criterion (basic amino acids in the immediate vicinity of the tyrosine residue within the primary sequence and/or the acidic residues within 5 Å from the atom susceptible to nitration) are shown in bold (B) .

    Article Snippet: After transfer, the membranes were blocked (3% BSA) and incubated with polyclonal antibodies against β-1,3-glucanase (Agrisera) at a 1:1000 dilution.

    Techniques: Residue, Sequencing, Solvent, Nitration