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polyclonal specific antibody against whole fbn2 protein  (GenScript corporation)

 
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    GenScript corporation polyclonal specific antibody against whole fbn2 protein
    Isolation of the <t>fbn2</t> knockout mutant. (A) Schematic illustration of the genomic DNA fragment containing the FBN2 gene. The T-DNA insertion in the first exon of FBN2 found in the SALK_124590 line is shown. The primers used in the analysis of wild-type (WT) or mutant FBN2 alleles are indicated. (B) PCR analysis of a homozygous fbn2 mutant plant. Only the mutant allele is detected. (C) Immunoblot analysis of leaf extracts of WT and fbn2 mutant plants using anti-FBN2 antibodies.
    Polyclonal Specific Antibody Against Whole Fbn2 Protein, supplied by GenScript corporation, 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/polyclonal specific antibody against whole fbn2 protein/product/GenScript corporation
    Average 90 stars, based on 1 article reviews
    polyclonal specific antibody against whole fbn2 protein - by Bioz Stars, 2026-03
    90/100 stars

    Images

    1) Product Images from "Arabidopsis fibrillin 1-2 subfamily members exert their functions via specific protein–protein interactions"

    Article Title: Arabidopsis fibrillin 1-2 subfamily members exert their functions via specific protein–protein interactions

    Journal: Journal of Experimental Botany

    doi: 10.1093/jxb/erab452

    Isolation of the fbn2 knockout mutant. (A) Schematic illustration of the genomic DNA fragment containing the FBN2 gene. The T-DNA insertion in the first exon of FBN2 found in the SALK_124590 line is shown. The primers used in the analysis of wild-type (WT) or mutant FBN2 alleles are indicated. (B) PCR analysis of a homozygous fbn2 mutant plant. Only the mutant allele is detected. (C) Immunoblot analysis of leaf extracts of WT and fbn2 mutant plants using anti-FBN2 antibodies.
    Figure Legend Snippet: Isolation of the fbn2 knockout mutant. (A) Schematic illustration of the genomic DNA fragment containing the FBN2 gene. The T-DNA insertion in the first exon of FBN2 found in the SALK_124590 line is shown. The primers used in the analysis of wild-type (WT) or mutant FBN2 alleles are indicated. (B) PCR analysis of a homozygous fbn2 mutant plant. Only the mutant allele is detected. (C) Immunoblot analysis of leaf extracts of WT and fbn2 mutant plants using anti-FBN2 antibodies.

    Techniques Used: Isolation, Knock-Out, Mutagenesis, Western Blot

    Localization of FBN2. (A) Full-length FBN2 or FBN4 cDNAs were fused to GFP and transiently expressed in N. benthamiana leaves. Fluorescence was monitored by confocal microscopy. The GFP fluorescence, chlorophyll autofluorescence, and merged images are shown. (B) Chloroplasts isolated from Arabidopsis rosette leaves were disrupted and the soluble (S) and membrane fractions (M) were isolated by ultracentrifugation at 100000 g for 1h at 4 °C. The pellet (membrane fraction) was resuspended in the same volume as the supernatant and 20 µg of protein from each fraction was loaded on to SDS-PAGE gels. The proteins were blotted on to a PVDF filter and hybridized with specific antibodies against FBN2, FBN4, plastidial glutamine synthetase (GS) (a marker of stromal protein), and psbA (a marker of thylakoid membranes).
    Figure Legend Snippet: Localization of FBN2. (A) Full-length FBN2 or FBN4 cDNAs were fused to GFP and transiently expressed in N. benthamiana leaves. Fluorescence was monitored by confocal microscopy. The GFP fluorescence, chlorophyll autofluorescence, and merged images are shown. (B) Chloroplasts isolated from Arabidopsis rosette leaves were disrupted and the soluble (S) and membrane fractions (M) were isolated by ultracentrifugation at 100000 g for 1h at 4 °C. The pellet (membrane fraction) was resuspended in the same volume as the supernatant and 20 µg of protein from each fraction was loaded on to SDS-PAGE gels. The proteins were blotted on to a PVDF filter and hybridized with specific antibodies against FBN2, FBN4, plastidial glutamine synthetase (GS) (a marker of stromal protein), and psbA (a marker of thylakoid membranes).

    Techniques Used: Fluorescence, Confocal Microscopy, Isolation, Membrane, SDS Page, Marker

    Anthocyanin accumulation in fbn mutants. (A) Knockout mutants fbn2 , fbn1a-1b , and fbn1a-1b-2 and WT plants were sown in soil and cultivated under normal conditions for 3 weeks. After this period, the plants were subjected to stress conditions (600 µmol m −2 s −1 light intensity and 10 °C temperature). Twelve rosette leaves from four plants per line were harvested after 0, 1, and 3 weeks of treatment, and the concentrations of anthocyanins were determined. (B) Plants cultivated under normal conditions were subjected to stress as described in (A) for 1 week with or without the addition of 2mM JA every 3 d, and the concentrations of anthocyanins were determined. In both panels, the values are presented as means ±SD. Two-way ANOVA was performed using PRISM software version 6.0. Tukey’s HSD test was used as a post hoc test. Significant differences ( P <0.01) between mean values are indicated with different letters.
    Figure Legend Snippet: Anthocyanin accumulation in fbn mutants. (A) Knockout mutants fbn2 , fbn1a-1b , and fbn1a-1b-2 and WT plants were sown in soil and cultivated under normal conditions for 3 weeks. After this period, the plants were subjected to stress conditions (600 µmol m −2 s −1 light intensity and 10 °C temperature). Twelve rosette leaves from four plants per line were harvested after 0, 1, and 3 weeks of treatment, and the concentrations of anthocyanins were determined. (B) Plants cultivated under normal conditions were subjected to stress as described in (A) for 1 week with or without the addition of 2mM JA every 3 d, and the concentrations of anthocyanins were determined. In both panels, the values are presented as means ±SD. Two-way ANOVA was performed using PRISM software version 6.0. Tukey’s HSD test was used as a post hoc test. Significant differences ( P <0.01) between mean values are indicated with different letters.

    Techniques Used: Knock-Out, Software

    PSII performance of fbn plants. The plants were sown in soil, cultivated under normal conditions for 3 weeks, and then stressed for 1 week with a combination of moderate high light and low temperature as described in . (A) Representative false-colour images of WT, fbn2 , fbn1a-1b , and fbn1a-1b-2 plants at 0 d, 1 d, and 1 week of stress. The images represent the maximum PSII quantum yield ( F v / F m ). The last column shows the phenotypes of plants after 1 week of stress. (B) Six fully expanded leaves from two plants per line at 0h, 24h, and 1 week of stress were used to determine the F v / F m values. (C) Concentrations of MDA in the leaves of 3-week-old plants subjected to high-light and cold stresses for 0h and 1 week. Four plants (three fully expanded leaves per plant) per line were used to determine the concentrations of MDA at each time point. In (B) and (C) the values are presented as means ±SD. PRISM software (version 6.0) was used to carry out a two-way ANOVA with Tukey’s post hoc test. Significant differences ( P <0.01) between mean values are indicated with different letters.
    Figure Legend Snippet: PSII performance of fbn plants. The plants were sown in soil, cultivated under normal conditions for 3 weeks, and then stressed for 1 week with a combination of moderate high light and low temperature as described in . (A) Representative false-colour images of WT, fbn2 , fbn1a-1b , and fbn1a-1b-2 plants at 0 d, 1 d, and 1 week of stress. The images represent the maximum PSII quantum yield ( F v / F m ). The last column shows the phenotypes of plants after 1 week of stress. (B) Six fully expanded leaves from two plants per line at 0h, 24h, and 1 week of stress were used to determine the F v / F m values. (C) Concentrations of MDA in the leaves of 3-week-old plants subjected to high-light and cold stresses for 0h and 1 week. Four plants (three fully expanded leaves per plant) per line were used to determine the concentrations of MDA at each time point. In (B) and (C) the values are presented as means ±SD. PRISM software (version 6.0) was used to carry out a two-way ANOVA with Tukey’s post hoc test. Significant differences ( P <0.01) between mean values are indicated with different letters.

    Techniques Used: Software

    Accumulation of anthocyanins and F v / F m of fbn2 plants transformed with the FBN2 gene. (A) WT, fbn2 , and two transgenic plants transformed with a genomic DNA fragment containing the FBN2 gene and 1kb of its promoter region (plants T4.5 and T5.6) were cultivated in a growth chamber under normal conditions and then subjected to stress conditions as described in . Twelve rosette leaves from four plants per line were harvested after 0, 1, and 3 weeks of treatment, and the concentrations of anthocyanins were determined. (B) WT, T4.5, and T5.6 plants grown under normal conditions were subjected to high-light and cold stresses, and the F v / F m values of six fully expanded leaves from two plants per line were determined at 0 d, 1 d, and 1 week of treatment using an IMAGING-PAM device. In both panels, the values are presented as means ±SD. PRISM software (version 6.0) was used to carry out a two-way ANOVA with Tukey’s post hoc test analysis. Significant differences ( P <0.01) between mean values are indicated with different letters.
    Figure Legend Snippet: Accumulation of anthocyanins and F v / F m of fbn2 plants transformed with the FBN2 gene. (A) WT, fbn2 , and two transgenic plants transformed with a genomic DNA fragment containing the FBN2 gene and 1kb of its promoter region (plants T4.5 and T5.6) were cultivated in a growth chamber under normal conditions and then subjected to stress conditions as described in . Twelve rosette leaves from four plants per line were harvested after 0, 1, and 3 weeks of treatment, and the concentrations of anthocyanins were determined. (B) WT, T4.5, and T5.6 plants grown under normal conditions were subjected to high-light and cold stresses, and the F v / F m values of six fully expanded leaves from two plants per line were determined at 0 d, 1 d, and 1 week of treatment using an IMAGING-PAM device. In both panels, the values are presented as means ±SD. PRISM software (version 6.0) was used to carry out a two-way ANOVA with Tukey’s post hoc test analysis. Significant differences ( P <0.01) between mean values are indicated with different letters.

    Techniques Used: Transformation Assay, Transgenic Assay, Imaging, Software

    In vivo interaction of FBN2–FBN1a, FBN2–FBN1b, FBN2–FBN2, FBN2–FBN4, and FBN1a–FBN4. cDNAs encoding the full-length FBN1a or FBN2 proteins were fused to the N-terminal half of YFP and co-transformed into N. benthamiana leaves together with cDNAs encoding FBN2, FBN1a, FBN1b, or FBN4 fused to the C-terminal moiety of CFP. The images show the YFP/CFP (BiFC) fluorescence, the chlorophyll autofluorescence, and the merged images.
    Figure Legend Snippet: In vivo interaction of FBN2–FBN1a, FBN2–FBN1b, FBN2–FBN2, FBN2–FBN4, and FBN1a–FBN4. cDNAs encoding the full-length FBN1a or FBN2 proteins were fused to the N-terminal half of YFP and co-transformed into N. benthamiana leaves together with cDNAs encoding FBN2, FBN1a, FBN1b, or FBN4 fused to the C-terminal moiety of CFP. The images show the YFP/CFP (BiFC) fluorescence, the chlorophyll autofluorescence, and the merged images.

    Techniques Used: In Vivo, Transformation Assay, Fluorescence

    In vivo interaction of FBN2–AOS, FBN1a–AOS, and FBN1b–AOS. cDNAs encoding the full-length FBN1a, FBN1b, or FBN2 proteins were fused to the N-terminal half of YFP and co-transformed into N. benthamiana leaves together with cDNA encoding AOS fused to the C-terminal moiety of CFP. Images show the YFP/CFP (BiFC) fluorescence, the chlorophyll autofluorescence, and the merged images.
    Figure Legend Snippet: In vivo interaction of FBN2–AOS, FBN1a–AOS, and FBN1b–AOS. cDNAs encoding the full-length FBN1a, FBN1b, or FBN2 proteins were fused to the N-terminal half of YFP and co-transformed into N. benthamiana leaves together with cDNA encoding AOS fused to the C-terminal moiety of CFP. Images show the YFP/CFP (BiFC) fluorescence, the chlorophyll autofluorescence, and the merged images.

    Techniques Used: In Vivo, Transformation Assay, Fluorescence

    Schematic model of the arrangement of FBNs1-2 subgroup proteins on the surface of PGs. FBN2 (red) may form homodimers or heterodimers with FBN1a (light brown) or FBN1b (dark brown). We have previously shown that FBN1a and FBN1b may form hetero-oligomers ( Gámez-Arjona et al , 2014 a ). These interactions allow the formation of a FBNs1-2-based network around the surface of PGs. Other proteins, such as those described in , associate with PGs via interactions with these FBNs. The degree of functional redundancy between these FBNs has not been characterized and might vary for each PG-associated protein. Their elimination would affect the localization and function of some PG-associated proteins. The functions of other FBNs associated with PGs (FBN4, FBN7a, FBN7b, and FBN8, indicated in light blue) have not been determined yet.
    Figure Legend Snippet: Schematic model of the arrangement of FBNs1-2 subgroup proteins on the surface of PGs. FBN2 (red) may form homodimers or heterodimers with FBN1a (light brown) or FBN1b (dark brown). We have previously shown that FBN1a and FBN1b may form hetero-oligomers ( Gámez-Arjona et al , 2014 a ). These interactions allow the formation of a FBNs1-2-based network around the surface of PGs. Other proteins, such as those described in , associate with PGs via interactions with these FBNs. The degree of functional redundancy between these FBNs has not been characterized and might vary for each PG-associated protein. Their elimination would affect the localization and function of some PG-associated proteins. The functions of other FBNs associated with PGs (FBN4, FBN7a, FBN7b, and FBN8, indicated in light blue) have not been determined yet.

    Techniques Used: Functional Assay



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    polyclonal specific antibody against whole fbn2 protein  (GenScript corporation)
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    GenScript corporation polyclonal specific antibody against whole fbn2 protein
    Isolation of the <t>fbn2</t> knockout mutant. (A) Schematic illustration of the genomic DNA fragment containing the FBN2 gene. The T-DNA insertion in the first exon of FBN2 found in the SALK_124590 line is shown. The primers used in the analysis of wild-type (WT) or mutant FBN2 alleles are indicated. (B) PCR analysis of a homozygous fbn2 mutant plant. Only the mutant allele is detected. (C) Immunoblot analysis of leaf extracts of WT and fbn2 mutant plants using anti-FBN2 antibodies.
    Polyclonal Specific Antibody Against Whole Fbn2 Protein, supplied by GenScript corporation, 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/polyclonal specific antibody against whole fbn2 protein/product/GenScript corporation
    Average 90 stars, based on 1 article reviews
    polyclonal specific antibody against whole fbn2 protein - by Bioz Stars, 2026-03
    90/100 stars
    		  Buy from Supplier

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    Isolation of the fbn2 knockout mutant. (A) Schematic illustration of the genomic DNA fragment containing the FBN2 gene. The T-DNA insertion in the first exon of FBN2 found in the SALK_124590 line is shown. The primers used in the analysis of wild-type (WT) or mutant FBN2 alleles are indicated. (B) PCR analysis of a homozygous fbn2 mutant plant. Only the mutant allele is detected. (C) Immunoblot analysis of leaf extracts of WT and fbn2 mutant plants using anti-FBN2 antibodies.

    Journal: Journal of Experimental Botany

    Article Title: Arabidopsis fibrillin 1-2 subfamily members exert their functions via specific protein–protein interactions

    doi: 10.1093/jxb/erab452

    Figure Lengend Snippet: Isolation of the fbn2 knockout mutant. (A) Schematic illustration of the genomic DNA fragment containing the FBN2 gene. The T-DNA insertion in the first exon of FBN2 found in the SALK_124590 line is shown. The primers used in the analysis of wild-type (WT) or mutant FBN2 alleles are indicated. (B) PCR analysis of a homozygous fbn2 mutant plant. Only the mutant allele is detected. (C) Immunoblot analysis of leaf extracts of WT and fbn2 mutant plants using anti-FBN2 antibodies.

    Article Snippet: The pellet was discarded and the supernatant was subjected to co-immunoprecipitation (Co-IP) analysis using a polyclonal specific antibody against the whole FBN2 protein (produced by GENSCRIPT) and a Dynabeads Co-Immunoprecipitation Kit (Life Technologies, http://lifetechnologies.com ) following the manufacturer’s instructions.

    Techniques: Isolation, Knock-Out, Mutagenesis, Western Blot

    Localization of FBN2. (A) Full-length FBN2 or FBN4 cDNAs were fused to GFP and transiently expressed in N. benthamiana leaves. Fluorescence was monitored by confocal microscopy. The GFP fluorescence, chlorophyll autofluorescence, and merged images are shown. (B) Chloroplasts isolated from Arabidopsis rosette leaves were disrupted and the soluble (S) and membrane fractions (M) were isolated by ultracentrifugation at 100000 g for 1h at 4 °C. The pellet (membrane fraction) was resuspended in the same volume as the supernatant and 20 µg of protein from each fraction was loaded on to SDS-PAGE gels. The proteins were blotted on to a PVDF filter and hybridized with specific antibodies against FBN2, FBN4, plastidial glutamine synthetase (GS) (a marker of stromal protein), and psbA (a marker of thylakoid membranes).

    Journal: Journal of Experimental Botany

    Article Title: Arabidopsis fibrillin 1-2 subfamily members exert their functions via specific protein–protein interactions

    doi: 10.1093/jxb/erab452

    Figure Lengend Snippet: Localization of FBN2. (A) Full-length FBN2 or FBN4 cDNAs were fused to GFP and transiently expressed in N. benthamiana leaves. Fluorescence was monitored by confocal microscopy. The GFP fluorescence, chlorophyll autofluorescence, and merged images are shown. (B) Chloroplasts isolated from Arabidopsis rosette leaves were disrupted and the soluble (S) and membrane fractions (M) were isolated by ultracentrifugation at 100000 g for 1h at 4 °C. The pellet (membrane fraction) was resuspended in the same volume as the supernatant and 20 µg of protein from each fraction was loaded on to SDS-PAGE gels. The proteins were blotted on to a PVDF filter and hybridized with specific antibodies against FBN2, FBN4, plastidial glutamine synthetase (GS) (a marker of stromal protein), and psbA (a marker of thylakoid membranes).

    Article Snippet: The pellet was discarded and the supernatant was subjected to co-immunoprecipitation (Co-IP) analysis using a polyclonal specific antibody against the whole FBN2 protein (produced by GENSCRIPT) and a Dynabeads Co-Immunoprecipitation Kit (Life Technologies, http://lifetechnologies.com ) following the manufacturer’s instructions.

    Techniques: Fluorescence, Confocal Microscopy, Isolation, Membrane, SDS Page, Marker

    Anthocyanin accumulation in fbn mutants. (A) Knockout mutants fbn2 , fbn1a-1b , and fbn1a-1b-2 and WT plants were sown in soil and cultivated under normal conditions for 3 weeks. After this period, the plants were subjected to stress conditions (600 µmol m −2 s −1 light intensity and 10 °C temperature). Twelve rosette leaves from four plants per line were harvested after 0, 1, and 3 weeks of treatment, and the concentrations of anthocyanins were determined. (B) Plants cultivated under normal conditions were subjected to stress as described in (A) for 1 week with or without the addition of 2mM JA every 3 d, and the concentrations of anthocyanins were determined. In both panels, the values are presented as means ±SD. Two-way ANOVA was performed using PRISM software version 6.0. Tukey’s HSD test was used as a post hoc test. Significant differences ( P <0.01) between mean values are indicated with different letters.

    Journal: Journal of Experimental Botany

    Article Title: Arabidopsis fibrillin 1-2 subfamily members exert their functions via specific protein–protein interactions

    doi: 10.1093/jxb/erab452

    Figure Lengend Snippet: Anthocyanin accumulation in fbn mutants. (A) Knockout mutants fbn2 , fbn1a-1b , and fbn1a-1b-2 and WT plants were sown in soil and cultivated under normal conditions for 3 weeks. After this period, the plants were subjected to stress conditions (600 µmol m −2 s −1 light intensity and 10 °C temperature). Twelve rosette leaves from four plants per line were harvested after 0, 1, and 3 weeks of treatment, and the concentrations of anthocyanins were determined. (B) Plants cultivated under normal conditions were subjected to stress as described in (A) for 1 week with or without the addition of 2mM JA every 3 d, and the concentrations of anthocyanins were determined. In both panels, the values are presented as means ±SD. Two-way ANOVA was performed using PRISM software version 6.0. Tukey’s HSD test was used as a post hoc test. Significant differences ( P <0.01) between mean values are indicated with different letters.

    Article Snippet: The pellet was discarded and the supernatant was subjected to co-immunoprecipitation (Co-IP) analysis using a polyclonal specific antibody against the whole FBN2 protein (produced by GENSCRIPT) and a Dynabeads Co-Immunoprecipitation Kit (Life Technologies, http://lifetechnologies.com ) following the manufacturer’s instructions.

    Techniques: Knock-Out, Software

    PSII performance of fbn plants. The plants were sown in soil, cultivated under normal conditions for 3 weeks, and then stressed for 1 week with a combination of moderate high light and low temperature as described in . (A) Representative false-colour images of WT, fbn2 , fbn1a-1b , and fbn1a-1b-2 plants at 0 d, 1 d, and 1 week of stress. The images represent the maximum PSII quantum yield ( F v / F m ). The last column shows the phenotypes of plants after 1 week of stress. (B) Six fully expanded leaves from two plants per line at 0h, 24h, and 1 week of stress were used to determine the F v / F m values. (C) Concentrations of MDA in the leaves of 3-week-old plants subjected to high-light and cold stresses for 0h and 1 week. Four plants (three fully expanded leaves per plant) per line were used to determine the concentrations of MDA at each time point. In (B) and (C) the values are presented as means ±SD. PRISM software (version 6.0) was used to carry out a two-way ANOVA with Tukey’s post hoc test. Significant differences ( P <0.01) between mean values are indicated with different letters.

    Journal: Journal of Experimental Botany

    Article Title: Arabidopsis fibrillin 1-2 subfamily members exert their functions via specific protein–protein interactions

    doi: 10.1093/jxb/erab452

    Figure Lengend Snippet: PSII performance of fbn plants. The plants were sown in soil, cultivated under normal conditions for 3 weeks, and then stressed for 1 week with a combination of moderate high light and low temperature as described in . (A) Representative false-colour images of WT, fbn2 , fbn1a-1b , and fbn1a-1b-2 plants at 0 d, 1 d, and 1 week of stress. The images represent the maximum PSII quantum yield ( F v / F m ). The last column shows the phenotypes of plants after 1 week of stress. (B) Six fully expanded leaves from two plants per line at 0h, 24h, and 1 week of stress were used to determine the F v / F m values. (C) Concentrations of MDA in the leaves of 3-week-old plants subjected to high-light and cold stresses for 0h and 1 week. Four plants (three fully expanded leaves per plant) per line were used to determine the concentrations of MDA at each time point. In (B) and (C) the values are presented as means ±SD. PRISM software (version 6.0) was used to carry out a two-way ANOVA with Tukey’s post hoc test. Significant differences ( P <0.01) between mean values are indicated with different letters.

    Article Snippet: The pellet was discarded and the supernatant was subjected to co-immunoprecipitation (Co-IP) analysis using a polyclonal specific antibody against the whole FBN2 protein (produced by GENSCRIPT) and a Dynabeads Co-Immunoprecipitation Kit (Life Technologies, http://lifetechnologies.com ) following the manufacturer’s instructions.

    Techniques: Software

    Accumulation of anthocyanins and F v / F m of fbn2 plants transformed with the FBN2 gene. (A) WT, fbn2 , and two transgenic plants transformed with a genomic DNA fragment containing the FBN2 gene and 1kb of its promoter region (plants T4.5 and T5.6) were cultivated in a growth chamber under normal conditions and then subjected to stress conditions as described in . Twelve rosette leaves from four plants per line were harvested after 0, 1, and 3 weeks of treatment, and the concentrations of anthocyanins were determined. (B) WT, T4.5, and T5.6 plants grown under normal conditions were subjected to high-light and cold stresses, and the F v / F m values of six fully expanded leaves from two plants per line were determined at 0 d, 1 d, and 1 week of treatment using an IMAGING-PAM device. In both panels, the values are presented as means ±SD. PRISM software (version 6.0) was used to carry out a two-way ANOVA with Tukey’s post hoc test analysis. Significant differences ( P <0.01) between mean values are indicated with different letters.

    Journal: Journal of Experimental Botany

    Article Title: Arabidopsis fibrillin 1-2 subfamily members exert their functions via specific protein–protein interactions

    doi: 10.1093/jxb/erab452

    Figure Lengend Snippet: Accumulation of anthocyanins and F v / F m of fbn2 plants transformed with the FBN2 gene. (A) WT, fbn2 , and two transgenic plants transformed with a genomic DNA fragment containing the FBN2 gene and 1kb of its promoter region (plants T4.5 and T5.6) were cultivated in a growth chamber under normal conditions and then subjected to stress conditions as described in . Twelve rosette leaves from four plants per line were harvested after 0, 1, and 3 weeks of treatment, and the concentrations of anthocyanins were determined. (B) WT, T4.5, and T5.6 plants grown under normal conditions were subjected to high-light and cold stresses, and the F v / F m values of six fully expanded leaves from two plants per line were determined at 0 d, 1 d, and 1 week of treatment using an IMAGING-PAM device. In both panels, the values are presented as means ±SD. PRISM software (version 6.0) was used to carry out a two-way ANOVA with Tukey’s post hoc test analysis. Significant differences ( P <0.01) between mean values are indicated with different letters.

    Article Snippet: The pellet was discarded and the supernatant was subjected to co-immunoprecipitation (Co-IP) analysis using a polyclonal specific antibody against the whole FBN2 protein (produced by GENSCRIPT) and a Dynabeads Co-Immunoprecipitation Kit (Life Technologies, http://lifetechnologies.com ) following the manufacturer’s instructions.

    Techniques: Transformation Assay, Transgenic Assay, Imaging, Software

    In vivo interaction of FBN2–FBN1a, FBN2–FBN1b, FBN2–FBN2, FBN2–FBN4, and FBN1a–FBN4. cDNAs encoding the full-length FBN1a or FBN2 proteins were fused to the N-terminal half of YFP and co-transformed into N. benthamiana leaves together with cDNAs encoding FBN2, FBN1a, FBN1b, or FBN4 fused to the C-terminal moiety of CFP. The images show the YFP/CFP (BiFC) fluorescence, the chlorophyll autofluorescence, and the merged images.

    Journal: Journal of Experimental Botany

    Article Title: Arabidopsis fibrillin 1-2 subfamily members exert their functions via specific protein–protein interactions

    doi: 10.1093/jxb/erab452

    Figure Lengend Snippet: In vivo interaction of FBN2–FBN1a, FBN2–FBN1b, FBN2–FBN2, FBN2–FBN4, and FBN1a–FBN4. cDNAs encoding the full-length FBN1a or FBN2 proteins were fused to the N-terminal half of YFP and co-transformed into N. benthamiana leaves together with cDNAs encoding FBN2, FBN1a, FBN1b, or FBN4 fused to the C-terminal moiety of CFP. The images show the YFP/CFP (BiFC) fluorescence, the chlorophyll autofluorescence, and the merged images.

    Article Snippet: The pellet was discarded and the supernatant was subjected to co-immunoprecipitation (Co-IP) analysis using a polyclonal specific antibody against the whole FBN2 protein (produced by GENSCRIPT) and a Dynabeads Co-Immunoprecipitation Kit (Life Technologies, http://lifetechnologies.com ) following the manufacturer’s instructions.

    Techniques: In Vivo, Transformation Assay, Fluorescence

    In vivo interaction of FBN2–AOS, FBN1a–AOS, and FBN1b–AOS. cDNAs encoding the full-length FBN1a, FBN1b, or FBN2 proteins were fused to the N-terminal half of YFP and co-transformed into N. benthamiana leaves together with cDNA encoding AOS fused to the C-terminal moiety of CFP. Images show the YFP/CFP (BiFC) fluorescence, the chlorophyll autofluorescence, and the merged images.

    Journal: Journal of Experimental Botany

    Article Title: Arabidopsis fibrillin 1-2 subfamily members exert their functions via specific protein–protein interactions

    doi: 10.1093/jxb/erab452

    Figure Lengend Snippet: In vivo interaction of FBN2–AOS, FBN1a–AOS, and FBN1b–AOS. cDNAs encoding the full-length FBN1a, FBN1b, or FBN2 proteins were fused to the N-terminal half of YFP and co-transformed into N. benthamiana leaves together with cDNA encoding AOS fused to the C-terminal moiety of CFP. Images show the YFP/CFP (BiFC) fluorescence, the chlorophyll autofluorescence, and the merged images.

    Article Snippet: The pellet was discarded and the supernatant was subjected to co-immunoprecipitation (Co-IP) analysis using a polyclonal specific antibody against the whole FBN2 protein (produced by GENSCRIPT) and a Dynabeads Co-Immunoprecipitation Kit (Life Technologies, http://lifetechnologies.com ) following the manufacturer’s instructions.

    Techniques: In Vivo, Transformation Assay, Fluorescence

    Schematic model of the arrangement of FBNs1-2 subgroup proteins on the surface of PGs. FBN2 (red) may form homodimers or heterodimers with FBN1a (light brown) or FBN1b (dark brown). We have previously shown that FBN1a and FBN1b may form hetero-oligomers ( Gámez-Arjona et al , 2014 a ). These interactions allow the formation of a FBNs1-2-based network around the surface of PGs. Other proteins, such as those described in , associate with PGs via interactions with these FBNs. The degree of functional redundancy between these FBNs has not been characterized and might vary for each PG-associated protein. Their elimination would affect the localization and function of some PG-associated proteins. The functions of other FBNs associated with PGs (FBN4, FBN7a, FBN7b, and FBN8, indicated in light blue) have not been determined yet.

    Journal: Journal of Experimental Botany

    Article Title: Arabidopsis fibrillin 1-2 subfamily members exert their functions via specific protein–protein interactions

    doi: 10.1093/jxb/erab452

    Figure Lengend Snippet: Schematic model of the arrangement of FBNs1-2 subgroup proteins on the surface of PGs. FBN2 (red) may form homodimers or heterodimers with FBN1a (light brown) or FBN1b (dark brown). We have previously shown that FBN1a and FBN1b may form hetero-oligomers ( Gámez-Arjona et al , 2014 a ). These interactions allow the formation of a FBNs1-2-based network around the surface of PGs. Other proteins, such as those described in , associate with PGs via interactions with these FBNs. The degree of functional redundancy between these FBNs has not been characterized and might vary for each PG-associated protein. Their elimination would affect the localization and function of some PG-associated proteins. The functions of other FBNs associated with PGs (FBN4, FBN7a, FBN7b, and FBN8, indicated in light blue) have not been determined yet.

    Article Snippet: The pellet was discarded and the supernatant was subjected to co-immunoprecipitation (Co-IP) analysis using a polyclonal specific antibody against the whole FBN2 protein (produced by GENSCRIPT) and a Dynabeads Co-Immunoprecipitation Kit (Life Technologies, http://lifetechnologies.com ) following the manufacturer’s instructions.

    Techniques: Functional Assay