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TaKaRa pgbkt7 bait vectors

GluTRBP interacts with LSD3 and regulates starch biosynthesis in rice leaves. (A) Interaction between GluTRBP and LSD3 detected by yeast two-hybrid (Y2H) assay. The interactions between pGADT7-T and <t>pGBKT7-53</t> and between pGADT7 and pGBKT7 were used as positive and negative controls, respectively. Yeast transformants were spotted onto control medium (SD/−Leu/−Trp, Double Dropout Medium, DDO) and selective medium (SD/−Leu/−Trp/−His/−Ade, Quadruple Dropout Medium, QDO). (B) Interaction between GluTRBP and LSD3 detected by GST pull-down assays. GST–LSD3 and His–GluTRBP were detected with anti-GST and anti-His antibodies, respectively. IB, immunoblotting. (C) Interaction between GluTRBP and LSD3 detected by bimolecular fluorescence complementation (BiFC) assay in rice protoplasts. Scale bars, 5 μm. (D) Co-localization of GluTRBP–GFP with chloroplast autofluorescence and GBSSII–CFP in rice protoplasts. CFP, cyan fluorescent protein. Scale bars, 5 μm. (E) Iodine staining of flag leaves from wild type and GluTRBP gene-edited mutants ( glutrbp-1 , glutrbp-2 ) at the end of the day. Scale bar, 1 cm. (F) Ultrastructure of chloroplasts in flag leaves at the end of the day. Starch granules (SGs) are indicated by red arrows. Scale bars, 20 μm. (G) Number of SGs per cell in flag leaves of wild type, glutrbp-1 , and glutrbp-2 . (H) Total starch content in flag leaves at the end of the day. DW, dry weight. (I) Percentage of amylose in total starch in flag leaves at the end of the day. (J) Sucrose content in flag leaves at the end of the day. Data in (G)–(J) are presented as means ± SD from three biological replicates. Different letters indicate significant differences at p < 0.05 according to ANOVA and Duncan’s test.

Pgbkt7 Bait Vectors, supplied by TaKaRa, used in various techniques. Bioz Stars score: 99/100, based on 4559 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "A glutamyl–tRNA reductase and its binding protein promote transitory starch biosynthesis and enhance grain quality and yield in rice"

Article Title: A glutamyl–tRNA reductase and its binding protein promote transitory starch biosynthesis and enhance grain quality and yield in rice

Journal: Plant Communications

doi: 10.1016/j.xplc.2025.101527

Figure Legend Snippet: GluTRBP interacts with LSD3 and regulates starch biosynthesis in rice leaves. (A) Interaction between GluTRBP and LSD3 detected by yeast two-hybrid (Y2H) assay. The interactions between pGADT7-T and pGBKT7-53 and between pGADT7 and pGBKT7 were used as positive and negative controls, respectively. Yeast transformants were spotted onto control medium (SD/−Leu/−Trp, Double Dropout Medium, DDO) and selective medium (SD/−Leu/−Trp/−His/−Ade, Quadruple Dropout Medium, QDO). (B) Interaction between GluTRBP and LSD3 detected by GST pull-down assays. GST–LSD3 and His–GluTRBP were detected with anti-GST and anti-His antibodies, respectively. IB, immunoblotting. (C) Interaction between GluTRBP and LSD3 detected by bimolecular fluorescence complementation (BiFC) assay in rice protoplasts. Scale bars, 5 μm. (D) Co-localization of GluTRBP–GFP with chloroplast autofluorescence and GBSSII–CFP in rice protoplasts. CFP, cyan fluorescent protein. Scale bars, 5 μm. (E) Iodine staining of flag leaves from wild type and GluTRBP gene-edited mutants ( glutrbp-1 , glutrbp-2 ) at the end of the day. Scale bar, 1 cm. (F) Ultrastructure of chloroplasts in flag leaves at the end of the day. Starch granules (SGs) are indicated by red arrows. Scale bars, 20 μm. (G) Number of SGs per cell in flag leaves of wild type, glutrbp-1 , and glutrbp-2 . (H) Total starch content in flag leaves at the end of the day. DW, dry weight. (I) Percentage of amylose in total starch in flag leaves at the end of the day. (J) Sucrose content in flag leaves at the end of the day. Data in (G)–(J) are presented as means ± SD from three biological replicates. Different letters indicate significant differences at p < 0.05 according to ANOVA and Duncan’s test.

Techniques Used: Starch, Y2H Assay, Control, Western Blot, Bimolecular Fluorescence Complementation Assay, Staining

The LSD3–GluTRBP module regulates transitory starch biosynthesis by maintaining GBSSII protein stability and enzymatic activity. (A) Interaction between GluTRBP and GBSSII detected by Y2H assay. Interactions between pGADT7-T and pGBKT7-53, and between pGADT7 and pGBKT7, served as positive and negative controls, respectively. Control medium, SD/−Leu/−Trp (DDO); selective medium, SD/−Leu/−Trp/−His/−Ade (QDO). (B) Interaction between GBSSII and GluTRBP detected by BiFC assay in rice protoplasts. Scale bars, 5 μm. (C) Interaction between GBSSII and GluTRBP detected by GST pull-down assays. GST–GBSSII and His–GluTRBP were detected with anti-GST and anti-His antibodies, respectively. IB, immunoblotting. (D) Cell-free degradation assay of LSD3 in the absence or presence of GluTRBP. (E) Cell-free degradation assay of GluTRBP in the absence or presence of LSD3. (F) Cell-free degradation assay of GBSSII in the absence or presence of GluTRBP and/or LSD3. (G) Expression levels of GBSSII in leaves of wild type, lsd3 , and glutrbp . (H) Immunoblot analysis of GBSSII protein abundance in leaves of wild type and mutants. (I) Enzyme activity of GBSS in leaves of wild type and mutants. (J) Iodine staining of flag leaves from wild type and CRISPR–Cas9 gene-edited mutants of GBSSII ( gbssII-1 , gbssII-2 ) at the end of the day. Scale bar, 1 cm. (K) Ultrastructure of chloroplasts in flag leaves at the end of the day. Starch granules (SGs) are indicated by red arrows. Scale bars, 10 μm. (L) Total starch content in flag leaves of wild type and mutants at the end of the day. DW, dry weight. (M) Percentage of amylose in total starch in flag leaves at the end of the day. (N) Sucrose content in flag leaves at the end of the day. (O) Grain appearance of wild type and mutants. Scale bars, 1 cm. (P–R) Chalky-grain rate (P) , total starch content (Q) , and amylose content (R) in the endosperm of wild type and mutants. Data in (G) , (I) , (L)–(N), and (P)–(R) are presented as means ± SD from three biological replicates. n.d. in (M) , not detected. Different letters indicate significant differences at p < 0.05 according to ANOVA and Duncan’s test.

Figure Legend Snippet: The LSD3–GluTRBP module regulates transitory starch biosynthesis by maintaining GBSSII protein stability and enzymatic activity. (A) Interaction between GluTRBP and GBSSII detected by Y2H assay. Interactions between pGADT7-T and pGBKT7-53, and between pGADT7 and pGBKT7, served as positive and negative controls, respectively. Control medium, SD/−Leu/−Trp (DDO); selective medium, SD/−Leu/−Trp/−His/−Ade (QDO). (B) Interaction between GBSSII and GluTRBP detected by BiFC assay in rice protoplasts. Scale bars, 5 μm. (C) Interaction between GBSSII and GluTRBP detected by GST pull-down assays. GST–GBSSII and His–GluTRBP were detected with anti-GST and anti-His antibodies, respectively. IB, immunoblotting. (D) Cell-free degradation assay of LSD3 in the absence or presence of GluTRBP. (E) Cell-free degradation assay of GluTRBP in the absence or presence of LSD3. (F) Cell-free degradation assay of GBSSII in the absence or presence of GluTRBP and/or LSD3. (G) Expression levels of GBSSII in leaves of wild type, lsd3 , and glutrbp . (H) Immunoblot analysis of GBSSII protein abundance in leaves of wild type and mutants. (I) Enzyme activity of GBSS in leaves of wild type and mutants. (J) Iodine staining of flag leaves from wild type and CRISPR–Cas9 gene-edited mutants of GBSSII ( gbssII-1 , gbssII-2 ) at the end of the day. Scale bar, 1 cm. (K) Ultrastructure of chloroplasts in flag leaves at the end of the day. Starch granules (SGs) are indicated by red arrows. Scale bars, 10 μm. (L) Total starch content in flag leaves of wild type and mutants at the end of the day. DW, dry weight. (M) Percentage of amylose in total starch in flag leaves at the end of the day. (N) Sucrose content in flag leaves at the end of the day. (O) Grain appearance of wild type and mutants. Scale bars, 1 cm. (P–R) Chalky-grain rate (P) , total starch content (Q) , and amylose content (R) in the endosperm of wild type and mutants. Data in (G) , (I) , (L)–(N), and (P)–(R) are presented as means ± SD from three biological replicates. n.d. in (M) , not detected. Different letters indicate significant differences at p < 0.05 according to ANOVA and Duncan’s test.

Techniques Used: Starch, Activity Assay, Y2H Assay, Control, Bimolecular Fluorescence Complementation Assay, Western Blot, Degradation Assay, Expressing, Quantitative Proteomics, Staining, CRISPR

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Journal: Plant Communications

Article Title: A glutamyl–tRNA reductase and its binding protein promote transitory starch biosynthesis and enhance grain quality and yield in rice

doi: 10.1016/j.xplc.2025.101527

Figure Lengend Snippet: GluTRBP interacts with LSD3 and regulates starch biosynthesis in rice leaves. (A) Interaction between GluTRBP and LSD3 detected by yeast two-hybrid (Y2H) assay. The interactions between pGADT7-T and pGBKT7-53 and between pGADT7 and pGBKT7 were used as positive and negative controls, respectively. Yeast transformants were spotted onto control medium (SD/−Leu/−Trp, Double Dropout Medium, DDO) and selective medium (SD/−Leu/−Trp/−His/−Ade, Quadruple Dropout Medium, QDO). (B) Interaction between GluTRBP and LSD3 detected by GST pull-down assays. GST–LSD3 and His–GluTRBP were detected with anti-GST and anti-His antibodies, respectively. IB, immunoblotting. (C) Interaction between GluTRBP and LSD3 detected by bimolecular fluorescence complementation (BiFC) assay in rice protoplasts. Scale bars, 5 μm. (D) Co-localization of GluTRBP–GFP with chloroplast autofluorescence and GBSSII–CFP in rice protoplasts. CFP, cyan fluorescent protein. Scale bars, 5 μm. (E) Iodine staining of flag leaves from wild type and GluTRBP gene-edited mutants ( glutrbp-1 , glutrbp-2 ) at the end of the day. Scale bar, 1 cm. (F) Ultrastructure of chloroplasts in flag leaves at the end of the day. Starch granules (SGs) are indicated by red arrows. Scale bars, 20 μm. (G) Number of SGs per cell in flag leaves of wild type, glutrbp-1 , and glutrbp-2 . (H) Total starch content in flag leaves at the end of the day. DW, dry weight. (I) Percentage of amylose in total starch in flag leaves at the end of the day. (J) Sucrose content in flag leaves at the end of the day. Data in (G)–(J) are presented as means ± SD from three biological replicates. Different letters indicate significant differences at p < 0.05 according to ANOVA and Duncan’s test.

Article Snippet: For Y2H assays, the coding sequences of LSD3 , GluTRBP , and GBSSII were cloned into pGADT7 (prey) or pGBKT7 (bait) vectors, and the fusion constructs were transferred into the GAL4 Y2H system (Clontech, Dalian, China).

Techniques: Starch, Y2H Assay, Control, Western Blot, Bimolecular Fluorescence Complementation Assay, Staining

Journal: Plant Communications

Article Title: A glutamyl–tRNA reductase and its binding protein promote transitory starch biosynthesis and enhance grain quality and yield in rice

doi: 10.1016/j.xplc.2025.101527

Figure Lengend Snippet: The LSD3–GluTRBP module regulates transitory starch biosynthesis by maintaining GBSSII protein stability and enzymatic activity. (A) Interaction between GluTRBP and GBSSII detected by Y2H assay. Interactions between pGADT7-T and pGBKT7-53, and between pGADT7 and pGBKT7, served as positive and negative controls, respectively. Control medium, SD/−Leu/−Trp (DDO); selective medium, SD/−Leu/−Trp/−His/−Ade (QDO). (B) Interaction between GBSSII and GluTRBP detected by BiFC assay in rice protoplasts. Scale bars, 5 μm. (C) Interaction between GBSSII and GluTRBP detected by GST pull-down assays. GST–GBSSII and His–GluTRBP were detected with anti-GST and anti-His antibodies, respectively. IB, immunoblotting. (D) Cell-free degradation assay of LSD3 in the absence or presence of GluTRBP. (E) Cell-free degradation assay of GluTRBP in the absence or presence of LSD3. (F) Cell-free degradation assay of GBSSII in the absence or presence of GluTRBP and/or LSD3. (G) Expression levels of GBSSII in leaves of wild type, lsd3 , and glutrbp . (H) Immunoblot analysis of GBSSII protein abundance in leaves of wild type and mutants. (I) Enzyme activity of GBSS in leaves of wild type and mutants. (J) Iodine staining of flag leaves from wild type and CRISPR–Cas9 gene-edited mutants of GBSSII ( gbssII-1 , gbssII-2 ) at the end of the day. Scale bar, 1 cm. (K) Ultrastructure of chloroplasts in flag leaves at the end of the day. Starch granules (SGs) are indicated by red arrows. Scale bars, 10 μm. (L) Total starch content in flag leaves of wild type and mutants at the end of the day. DW, dry weight. (M) Percentage of amylose in total starch in flag leaves at the end of the day. (N) Sucrose content in flag leaves at the end of the day. (O) Grain appearance of wild type and mutants. Scale bars, 1 cm. (P–R) Chalky-grain rate (P) , total starch content (Q) , and amylose content (R) in the endosperm of wild type and mutants. Data in (G) , (I) , (L)–(N), and (P)–(R) are presented as means ± SD from three biological replicates. n.d. in (M) , not detected. Different letters indicate significant differences at p < 0.05 according to ANOVA and Duncan’s test.

Techniques: Starch, Activity Assay, Y2H Assay, Control, Bimolecular Fluorescence Complementation Assay, Western Blot, Degradation Assay, Expressing, Quantitative Proteomics, Staining, CRISPR

PtrLAZY1 transcription is unaffected in TAC1‐CRISPR hybrid poplars, and PtrTAC1 does not interact with PtrLAZY1 at the protein level. (a) Semi‐quantitative RT‐PCR analysis of PtrTAC1‐1 , PtrTAC1‐2 , PtrWEEP and PtrLAZY1 expression in BH, TAC1‐CRISPR lines (#24 and #26) and Lombardy poplar. PtrACTIN2 was used as a loading control. (b) Schematic showing the upper and lower petiole regions used for tissue‐specific transcriptional analysis in (c). The upper and lower parts were separated by the red dashed line. (c) Semi‐quantitative RT‐PCR analysis of PtrTAC1‐1 , PtrLAZY1 and PtrWEEP in the upper and lower petiole tissues of BH and TAC1‐CRISPR lines (#24 and #26) with PtrACTIN2 as a control. (d) Yeast two‐hybrid (Y2H) assay testing protein–protein interaction between PtrTAC1‐1 and PtrLAZY1. Y2H assay was performed by using various combinations of vector constructions (right, see Section ). AtSTM/AD+PtrTALE12ΔC/BD serves as a positive control (Bae et al. ). Yeast was grown on selective media: SD‐W (−Trp), SD‐LW (−Leu, −Trp) and SD‐AHLW (−Ade, –His, −Leu, −Trp). AD and BD represent pGADT7 (activation domain, Leu selection) and pGBKT7 (binding domain, Trp selection) vectors, respectively.

Journal: Plant Biotechnology Journal

Article Title: Elucidating the Genetic Basis of Columnar Upright Architecture in Populus Through CRISPR Disruption of TILLER ANGLE CONTROL1

doi: 10.1111/pbi.70415

Figure Lengend Snippet: PtrLAZY1 transcription is unaffected in TAC1‐CRISPR hybrid poplars, and PtrTAC1 does not interact with PtrLAZY1 at the protein level. (a) Semi‐quantitative RT‐PCR analysis of PtrTAC1‐1 , PtrTAC1‐2 , PtrWEEP and PtrLAZY1 expression in BH, TAC1‐CRISPR lines (#24 and #26) and Lombardy poplar. PtrACTIN2 was used as a loading control. (b) Schematic showing the upper and lower petiole regions used for tissue‐specific transcriptional analysis in (c). The upper and lower parts were separated by the red dashed line. (c) Semi‐quantitative RT‐PCR analysis of PtrTAC1‐1 , PtrLAZY1 and PtrWEEP in the upper and lower petiole tissues of BH and TAC1‐CRISPR lines (#24 and #26) with PtrACTIN2 as a control. (d) Yeast two‐hybrid (Y2H) assay testing protein–protein interaction between PtrTAC1‐1 and PtrLAZY1. Y2H assay was performed by using various combinations of vector constructions (right, see Section ). AtSTM/AD+PtrTALE12ΔC/BD serves as a positive control (Bae et al. ). Yeast was grown on selective media: SD‐W (−Trp), SD‐LW (−Leu, −Trp) and SD‐AHLW (−Ade, –His, −Leu, −Trp). AD and BD represent pGADT7 (activation domain, Leu selection) and pGBKT7 (binding domain, Trp selection) vectors, respectively.

Article Snippet: Briefly, the full‐length PtrTAC1‐1 cDNA was cloned into the pGBKT7 bait vector (Addgene #61703), fused in‐frame with the GAL4 DNA‐binding domain, and selected using tryptophan (Trp) dropout media.

Techniques: CRISPR, Quantitative RT-PCR, Expressing, Control, Y2H Assay, Plasmid Preparation, Positive Control, Activation Assay, Selection, Binding Assay

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