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cdna encoding full-length atetr2  (GenScript corporation)

 
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    GenScript corporation cdna encoding full-length atetr2
    Expression and purification of recombinant <t>AtETR2.</t> (A) E. coli C43(DE) strain was used for heterologous expression of Arabidopsis thaliana receptor ETR2. Expression was analyzed by SDS-PAGE and immunoblotting. Protein expression was monitored 1 (lane 1) to 5 h (lane 5) after induction with IPTG and detected by an anti-His antibody. AtETR2 migrates on SDS gels with an apparent molecular mass of 120 kDa. (B) His-tagged AtETR2 was purified by IMAC, separated by SDS-PAGE and visualized by colloidal Coomassie staining and (C) immunoblotting using an anti-His antibody.
    Cdna Encoding Full Length Atetr2, 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/cdna encoding full-length atetr2/product/GenScript corporation
    Average 90 stars, based on 1 article reviews
    cdna encoding full-length atetr2 - by Bioz Stars, 2026-05
    90/100 stars

    Images

    1) Product Images from "Molecular Analysis of Protein-Protein Interactions in the Ethylene Pathway in the Different Ethylene Receptor Subfamilies"

    Article Title: Molecular Analysis of Protein-Protein Interactions in the Ethylene Pathway in the Different Ethylene Receptor Subfamilies

    Journal: Frontiers in Plant Science

    doi: 10.3389/fpls.2019.00726

    Expression and purification of recombinant AtETR2. (A) E. coli C43(DE) strain was used for heterologous expression of Arabidopsis thaliana receptor ETR2. Expression was analyzed by SDS-PAGE and immunoblotting. Protein expression was monitored 1 (lane 1) to 5 h (lane 5) after induction with IPTG and detected by an anti-His antibody. AtETR2 migrates on SDS gels with an apparent molecular mass of 120 kDa. (B) His-tagged AtETR2 was purified by IMAC, separated by SDS-PAGE and visualized by colloidal Coomassie staining and (C) immunoblotting using an anti-His antibody.
    Figure Legend Snippet: Expression and purification of recombinant AtETR2. (A) E. coli C43(DE) strain was used for heterologous expression of Arabidopsis thaliana receptor ETR2. Expression was analyzed by SDS-PAGE and immunoblotting. Protein expression was monitored 1 (lane 1) to 5 h (lane 5) after induction with IPTG and detected by an anti-His antibody. AtETR2 migrates on SDS gels with an apparent molecular mass of 120 kDa. (B) His-tagged AtETR2 was purified by IMAC, separated by SDS-PAGE and visualized by colloidal Coomassie staining and (C) immunoblotting using an anti-His antibody.

    Techniques Used: Expressing, Purification, Recombinant, SDS Page, Western Blot, Staining

    Circular dichroism spectra of AtETR2. (A) The far-UV spectra of AtETR2 was calculated and adjusted to molar extinction (∆ɛ) considering molecular weight and protein concentration of AtETR2. (B) Secondary structure content was calculated by CONTINLL (solid line) and CDSSTR (dashed line) from the CDpro software package.
    Figure Legend Snippet: Circular dichroism spectra of AtETR2. (A) The far-UV spectra of AtETR2 was calculated and adjusted to molar extinction (∆ɛ) considering molecular weight and protein concentration of AtETR2. (B) Secondary structure content was calculated by CONTINLL (solid line) and CDSSTR (dashed line) from the CDpro software package.

    Techniques Used: Circular Dichroism, Molecular Weight, Protein Concentration, Software

    Autophosphorylation of purified AtETR2 was performed with 0.1 mM [γ- 32 P]ATP and magnesium as cofactor. Proteins were detected by (A) Coomassie staining. (B) Incorporation of 32 P was measured by autoradiography for 6 days. Experiments were performed using AtETR2 solubilized and purified without ATP purification step (1) or chemically and thermally denatured AtETR2 (2).
    Figure Legend Snippet: Autophosphorylation of purified AtETR2 was performed with 0.1 mM [γ- 32 P]ATP and magnesium as cofactor. Proteins were detected by (A) Coomassie staining. (B) Incorporation of 32 P was measured by autoradiography for 6 days. Experiments were performed using AtETR2 solubilized and purified without ATP purification step (1) or chemically and thermally denatured AtETR2 (2).

    Techniques Used: Purification, Staining, Autoradiography

    Interaction studies of Arabidopsis ETR2 and EIN2 by MST. Dissociation constants of the interactions were obtained from the related binding curves. Titration of unlabeled AtEIN2 479-1294 to AtETR2 (●) is described by a dissociation constant ( K d ) of 161(30) nM. Chemically and thermally denatured AtEIN2 479-1294 shows no binding event to AtETR2 (▲). Binding of unlabeled AtETR2 to AtEIN2 479-129 is represented by a K d value of 147(15) nM (○). All data represent the mean (SD) of three independent measurements (●, ○) and duplicates (▲), respectively.
    Figure Legend Snippet: Interaction studies of Arabidopsis ETR2 and EIN2 by MST. Dissociation constants of the interactions were obtained from the related binding curves. Titration of unlabeled AtEIN2 479-1294 to AtETR2 (●) is described by a dissociation constant ( K d ) of 161(30) nM. Chemically and thermally denatured AtEIN2 479-1294 shows no binding event to AtETR2 (▲). Binding of unlabeled AtETR2 to AtEIN2 479-129 is represented by a K d value of 147(15) nM (○). All data represent the mean (SD) of three independent measurements (●, ○) and duplicates (▲), respectively.

    Techniques Used: Binding Assay, Titration

    MST based protein-protein interaction assay between AtCTR1 and receptor proteins AtETR1 and AtETR2. Binding of AtETR1 to fluorescently labeled AtCTR1 measured by MST resulted in a K d value of 169(15) nM (○). For AtCTR1-AtETR2 complex formation a K d value of 165(20) nM was obtained (●). As negative control, titration of chemically denatured AtCTR1 with AtETR2 is shown. Here, no binding event was observed (▲). Data are given as the mean (SD) of independent triplicates (●, ○) and duplicates (▲), respectively.
    Figure Legend Snippet: MST based protein-protein interaction assay between AtCTR1 and receptor proteins AtETR1 and AtETR2. Binding of AtETR1 to fluorescently labeled AtCTR1 measured by MST resulted in a K d value of 169(15) nM (○). For AtCTR1-AtETR2 complex formation a K d value of 165(20) nM was obtained (●). As negative control, titration of chemically denatured AtCTR1 with AtETR2 is shown. Here, no binding event was observed (▲). Data are given as the mean (SD) of independent triplicates (●, ○) and duplicates (▲), respectively.

    Techniques Used: Protein Protein Interaction Assay, Binding Assay, Labeling, Negative Control, Titration

    Quantification of receptor-receptor interactions by microscale thermophoresis. (A) For the homomeric AtETR1-AtETR1 complex formation a K d value of 326(18) nM (○) was obtained. As negative control chemically denatured AtETR1 was used showing no binding event (△). From the binding curve of the homomeric AtETR2-AtETR2 complex a K d value of 96(18) nM (●) was calculated. Chemically denatured AtETR2 indicates no interaction of the binding partners (▲). All data represent the mean (SD) of independent triplicates (○, ●) and duplicates (△, ▲). (B) Summary of the dissociation constants K d for receptor-receptor interactions obtained by MST, also see . All data represent the mean (SD) of three independent measurements.
    Figure Legend Snippet: Quantification of receptor-receptor interactions by microscale thermophoresis. (A) For the homomeric AtETR1-AtETR1 complex formation a K d value of 326(18) nM (○) was obtained. As negative control chemically denatured AtETR1 was used showing no binding event (△). From the binding curve of the homomeric AtETR2-AtETR2 complex a K d value of 96(18) nM (●) was calculated. Chemically denatured AtETR2 indicates no interaction of the binding partners (▲). All data represent the mean (SD) of independent triplicates (○, ●) and duplicates (△, ▲). (B) Summary of the dissociation constants K d for receptor-receptor interactions obtained by MST, also see . All data represent the mean (SD) of three independent measurements.

    Techniques Used: Microscale Thermophoresis, Negative Control, Binding Assay



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    cdna encoding full-length atetr2  (GenScript corporation)
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    GenScript corporation cdna encoding full-length atetr2
    Expression and purification of recombinant <t>AtETR2.</t> (A) E. coli C43(DE) strain was used for heterologous expression of Arabidopsis thaliana receptor ETR2. Expression was analyzed by SDS-PAGE and immunoblotting. Protein expression was monitored 1 (lane 1) to 5 h (lane 5) after induction with IPTG and detected by an anti-His antibody. AtETR2 migrates on SDS gels with an apparent molecular mass of 120 kDa. (B) His-tagged AtETR2 was purified by IMAC, separated by SDS-PAGE and visualized by colloidal Coomassie staining and (C) immunoblotting using an anti-His antibody.
    Cdna Encoding Full Length Atetr2, 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/cdna encoding full-length atetr2/product/GenScript corporation
    Average 90 stars, based on 1 article reviews
    cdna encoding full-length atetr2 - by Bioz Stars, 2026-05
    90/100 stars
    		  Buy from Supplier

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    Expression and purification of recombinant AtETR2. (A) E. coli C43(DE) strain was used for heterologous expression of Arabidopsis thaliana receptor ETR2. Expression was analyzed by SDS-PAGE and immunoblotting. Protein expression was monitored 1 (lane 1) to 5 h (lane 5) after induction with IPTG and detected by an anti-His antibody. AtETR2 migrates on SDS gels with an apparent molecular mass of 120 kDa. (B) His-tagged AtETR2 was purified by IMAC, separated by SDS-PAGE and visualized by colloidal Coomassie staining and (C) immunoblotting using an anti-His antibody.

    Journal: Frontiers in Plant Science

    Article Title: Molecular Analysis of Protein-Protein Interactions in the Ethylene Pathway in the Different Ethylene Receptor Subfamilies

    doi: 10.3389/fpls.2019.00726

    Figure Lengend Snippet: Expression and purification of recombinant AtETR2. (A) E. coli C43(DE) strain was used for heterologous expression of Arabidopsis thaliana receptor ETR2. Expression was analyzed by SDS-PAGE and immunoblotting. Protein expression was monitored 1 (lane 1) to 5 h (lane 5) after induction with IPTG and detected by an anti-His antibody. AtETR2 migrates on SDS gels with an apparent molecular mass of 120 kDa. (B) His-tagged AtETR2 was purified by IMAC, separated by SDS-PAGE and visualized by colloidal Coomassie staining and (C) immunoblotting using an anti-His antibody.

    Article Snippet: Codon optimized cDNA encoding full-length AtETR2 (UniProt ID: Q0WPQ2) was purchased from GenScript USA according to the published sequence (NCBI ID: NM_113216.3).

    Techniques: Expressing, Purification, Recombinant, SDS Page, Western Blot, Staining

    Circular dichroism spectra of AtETR2. (A) The far-UV spectra of AtETR2 was calculated and adjusted to molar extinction (∆ɛ) considering molecular weight and protein concentration of AtETR2. (B) Secondary structure content was calculated by CONTINLL (solid line) and CDSSTR (dashed line) from the CDpro software package.

    Journal: Frontiers in Plant Science

    Article Title: Molecular Analysis of Protein-Protein Interactions in the Ethylene Pathway in the Different Ethylene Receptor Subfamilies

    doi: 10.3389/fpls.2019.00726

    Figure Lengend Snippet: Circular dichroism spectra of AtETR2. (A) The far-UV spectra of AtETR2 was calculated and adjusted to molar extinction (∆ɛ) considering molecular weight and protein concentration of AtETR2. (B) Secondary structure content was calculated by CONTINLL (solid line) and CDSSTR (dashed line) from the CDpro software package.

    Article Snippet: Codon optimized cDNA encoding full-length AtETR2 (UniProt ID: Q0WPQ2) was purchased from GenScript USA according to the published sequence (NCBI ID: NM_113216.3).

    Techniques: Circular Dichroism, Molecular Weight, Protein Concentration, Software

    Autophosphorylation of purified AtETR2 was performed with 0.1 mM [γ- 32 P]ATP and magnesium as cofactor. Proteins were detected by (A) Coomassie staining. (B) Incorporation of 32 P was measured by autoradiography for 6 days. Experiments were performed using AtETR2 solubilized and purified without ATP purification step (1) or chemically and thermally denatured AtETR2 (2).

    Journal: Frontiers in Plant Science

    Article Title: Molecular Analysis of Protein-Protein Interactions in the Ethylene Pathway in the Different Ethylene Receptor Subfamilies

    doi: 10.3389/fpls.2019.00726

    Figure Lengend Snippet: Autophosphorylation of purified AtETR2 was performed with 0.1 mM [γ- 32 P]ATP and magnesium as cofactor. Proteins were detected by (A) Coomassie staining. (B) Incorporation of 32 P was measured by autoradiography for 6 days. Experiments were performed using AtETR2 solubilized and purified without ATP purification step (1) or chemically and thermally denatured AtETR2 (2).

    Article Snippet: Codon optimized cDNA encoding full-length AtETR2 (UniProt ID: Q0WPQ2) was purchased from GenScript USA according to the published sequence (NCBI ID: NM_113216.3).

    Techniques: Purification, Staining, Autoradiography

    Interaction studies of Arabidopsis ETR2 and EIN2 by MST. Dissociation constants of the interactions were obtained from the related binding curves. Titration of unlabeled AtEIN2 479-1294 to AtETR2 (●) is described by a dissociation constant ( K d ) of 161(30) nM. Chemically and thermally denatured AtEIN2 479-1294 shows no binding event to AtETR2 (▲). Binding of unlabeled AtETR2 to AtEIN2 479-129 is represented by a K d value of 147(15) nM (○). All data represent the mean (SD) of three independent measurements (●, ○) and duplicates (▲), respectively.

    Journal: Frontiers in Plant Science

    Article Title: Molecular Analysis of Protein-Protein Interactions in the Ethylene Pathway in the Different Ethylene Receptor Subfamilies

    doi: 10.3389/fpls.2019.00726

    Figure Lengend Snippet: Interaction studies of Arabidopsis ETR2 and EIN2 by MST. Dissociation constants of the interactions were obtained from the related binding curves. Titration of unlabeled AtEIN2 479-1294 to AtETR2 (●) is described by a dissociation constant ( K d ) of 161(30) nM. Chemically and thermally denatured AtEIN2 479-1294 shows no binding event to AtETR2 (▲). Binding of unlabeled AtETR2 to AtEIN2 479-129 is represented by a K d value of 147(15) nM (○). All data represent the mean (SD) of three independent measurements (●, ○) and duplicates (▲), respectively.

    Article Snippet: Codon optimized cDNA encoding full-length AtETR2 (UniProt ID: Q0WPQ2) was purchased from GenScript USA according to the published sequence (NCBI ID: NM_113216.3).

    Techniques: Binding Assay, Titration

    MST based protein-protein interaction assay between AtCTR1 and receptor proteins AtETR1 and AtETR2. Binding of AtETR1 to fluorescently labeled AtCTR1 measured by MST resulted in a K d value of 169(15) nM (○). For AtCTR1-AtETR2 complex formation a K d value of 165(20) nM was obtained (●). As negative control, titration of chemically denatured AtCTR1 with AtETR2 is shown. Here, no binding event was observed (▲). Data are given as the mean (SD) of independent triplicates (●, ○) and duplicates (▲), respectively.

    Journal: Frontiers in Plant Science

    Article Title: Molecular Analysis of Protein-Protein Interactions in the Ethylene Pathway in the Different Ethylene Receptor Subfamilies

    doi: 10.3389/fpls.2019.00726

    Figure Lengend Snippet: MST based protein-protein interaction assay between AtCTR1 and receptor proteins AtETR1 and AtETR2. Binding of AtETR1 to fluorescently labeled AtCTR1 measured by MST resulted in a K d value of 169(15) nM (○). For AtCTR1-AtETR2 complex formation a K d value of 165(20) nM was obtained (●). As negative control, titration of chemically denatured AtCTR1 with AtETR2 is shown. Here, no binding event was observed (▲). Data are given as the mean (SD) of independent triplicates (●, ○) and duplicates (▲), respectively.

    Article Snippet: Codon optimized cDNA encoding full-length AtETR2 (UniProt ID: Q0WPQ2) was purchased from GenScript USA according to the published sequence (NCBI ID: NM_113216.3).

    Techniques: Protein Protein Interaction Assay, Binding Assay, Labeling, Negative Control, Titration

    Quantification of receptor-receptor interactions by microscale thermophoresis. (A) For the homomeric AtETR1-AtETR1 complex formation a K d value of 326(18) nM (○) was obtained. As negative control chemically denatured AtETR1 was used showing no binding event (△). From the binding curve of the homomeric AtETR2-AtETR2 complex a K d value of 96(18) nM (●) was calculated. Chemically denatured AtETR2 indicates no interaction of the binding partners (▲). All data represent the mean (SD) of independent triplicates (○, ●) and duplicates (△, ▲). (B) Summary of the dissociation constants K d for receptor-receptor interactions obtained by MST, also see . All data represent the mean (SD) of three independent measurements.

    Journal: Frontiers in Plant Science

    Article Title: Molecular Analysis of Protein-Protein Interactions in the Ethylene Pathway in the Different Ethylene Receptor Subfamilies

    doi: 10.3389/fpls.2019.00726

    Figure Lengend Snippet: Quantification of receptor-receptor interactions by microscale thermophoresis. (A) For the homomeric AtETR1-AtETR1 complex formation a K d value of 326(18) nM (○) was obtained. As negative control chemically denatured AtETR1 was used showing no binding event (△). From the binding curve of the homomeric AtETR2-AtETR2 complex a K d value of 96(18) nM (●) was calculated. Chemically denatured AtETR2 indicates no interaction of the binding partners (▲). All data represent the mean (SD) of independent triplicates (○, ●) and duplicates (△, ▲). (B) Summary of the dissociation constants K d for receptor-receptor interactions obtained by MST, also see . All data represent the mean (SD) of three independent measurements.

    Article Snippet: Codon optimized cDNA encoding full-length AtETR2 (UniProt ID: Q0WPQ2) was purchased from GenScript USA according to the published sequence (NCBI ID: NM_113216.3).

    Techniques: Microscale Thermophoresis, Negative Control, Binding Assay