transfectants Search Results


94
Beyotime plant protoplast isolation kit
Subcellular localization of SbNF-YA6. Arabidopsis <t>protoplasts</t> were transfected with 35S:GFP (control) or 35S:SbNF-YA6 -GFP. The fluorescence signals were detected under a confocal microscope. Chlorophyll autofluorescence was used to visualize chloroplasts.
Plant Protoplast Isolation Kit, supplied by Beyotime, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/transfectants/Plant+Protoplasts+Transfection+Kit/pmc11961913-136-1-5
Average 94 stars, based on 1 article reviews
plant protoplast isolation kit - by Bioz Stars, 2026-10
94/100 stars
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96
Vazyme Biotech Co lipomaster 3000 transfection reagent
Subcellular localization of SbNF-YA6. Arabidopsis <t>protoplasts</t> were transfected with 35S:GFP (control) or 35S:SbNF-YA6 -GFP. The fluorescence signals were detected under a confocal microscope. Chlorophyll autofluorescence was used to visualize chloroplasts.
Lipomaster 3000 Transfection Reagent, supplied by Vazyme Biotech Co, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/transfectants/Lipomaster+3000+Transfection+Reagent/10__33549_slash_physiolres__935675-109-0-4
Average 96 stars, based on 1 article reviews
lipomaster 3000 transfection reagent - by Bioz Stars, 2026-10
96/100 stars
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99
Kyfora Bio pei max transfection grade linear polyethylenimine hydrochloride
Subcellular localization of SbNF-YA6. Arabidopsis <t>protoplasts</t> were transfected with 35S:GFP (control) or 35S:SbNF-YA6 -GFP. The fluorescence signals were detected under a confocal microscope. Chlorophyll autofluorescence was used to visualize chloroplasts.
Pei Max Transfection Grade Linear Polyethylenimine Hydrochloride, supplied by Kyfora Bio, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/transfectants/PEI+MAX+Transfection+Reagent/pmc13049657-24-0-9
Average 99 stars, based on 1 article reviews
pei max transfection grade linear polyethylenimine hydrochloride - by Bioz Stars, 2026-10
99/100 stars
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99
Beyotime beyopeitm transfection reagent
Subcellular localization of SbNF-YA6. Arabidopsis <t>protoplasts</t> were transfected with 35S:GFP (control) or 35S:SbNF-YA6 -GFP. The fluorescence signals were detected under a confocal microscope. Chlorophyll autofluorescence was used to visualize chloroplasts.
Beyopeitm Transfection Reagent, supplied by Beyotime, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/transfectants/BeyoPEI+Transfection+Reagent/pm40437612-73-6-9
Average 99 stars, based on 1 article reviews
beyopeitm transfection reagent - by Bioz Stars, 2026-10
99/100 stars
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98
Beyotime lipo6000 transfection reagent
Subcellular localization of SbNF-YA6. Arabidopsis <t>protoplasts</t> were transfected with 35S:GFP (control) or 35S:SbNF-YA6 -GFP. The fluorescence signals were detected under a confocal microscope. Chlorophyll autofluorescence was used to visualize chloroplasts.
Lipo6000 Transfection Reagent, supplied by Beyotime, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/transfectants/Lipo6000+Transfection+Reagent/pmc05682668-157-13-16
Average 98 stars, based on 1 article reviews
lipo6000 transfection reagent - by Bioz Stars, 2026-10
98/100 stars
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96
Kyfora Bio transporter 5 polysciences
Subcellular localization of SbNF-YA6. Arabidopsis <t>protoplasts</t> were transfected with 35S:GFP (control) or 35S:SbNF-YA6 -GFP. The fluorescence signals were detected under a confocal microscope. Chlorophyll autofluorescence was used to visualize chloroplasts.
Transporter 5 Polysciences, supplied by Kyfora Bio, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/transfectants/Transporter+5+Transfection+Reagent/10__1016_slash_j__isci__2026__115975-165-63-65
Average 96 stars, based on 1 article reviews
transporter 5 polysciences - by Bioz Stars, 2026-10
96/100 stars
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92
Sartorius AG expi293 medium
Structure of a VWF tubule. (A) Schematic of the domain organization of the VWF proprotein. Each D assembly except D′ is made of domains VWF type D domain, C8, TIL (trypsin inhibitor-like cysteine-rich domain), and E. D1 and D2 form a prodomain that is cleaved by furin protease before secretion. (B) Strategy to obtain VWF monomers and disulfide-linked dimers. VWF D1-A1 was expressed in <t>Expi293</t> cells and purified from the media as monomers and disulfide-linked dimers. The furin cleavage site was mutated to ASAS to prevent prodomain dissociation. (C) DLS experiments of purified D1-A1 incubated at indicated pH showing an increase in average hydrodynamic radius with a decrease in pH. Error bars represent the difference between the means from 2 replicates. (D) Representative micrographs from negative-stain electron microscopy showing VWF dimers incubated at pH 7.4 and 5.2 (scale bars, 50 nm). (E) Quantification of (D) showing particle lengths measured from 3 micrographs from samples incubated together overnight. The bottom, middle, and top lines of the shaded boxes represent the first quartile, the median, and the third quartile of measured particle length, respectively. The length of the whiskers below and above the box plot represent the lesser of the range of data or 1.5 multiplied by the interquartile range. (F) Schematic and cryo-EM structure of the dimer-derived tubule showing the bead-like arrangement. The structure forms a right-handed helix with a helical rise of 26.8 Å and a helical twist of 83.3°. The cryo-EM map has been Gaussian filtered for visualization.
Expi293 Medium, supplied by Sartorius AG, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/transfectants/FectoPRO/pmc09507011-31-6-12
Average 92 stars, based on 1 article reviews
expi293 medium - by Bioz Stars, 2026-10
92/100 stars
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99
Beyotime lipo293tm transfection reagent
Structure of a VWF tubule. (A) Schematic of the domain organization of the VWF proprotein. Each D assembly except D′ is made of domains VWF type D domain, C8, TIL (trypsin inhibitor-like cysteine-rich domain), and E. D1 and D2 form a prodomain that is cleaved by furin protease before secretion. (B) Strategy to obtain VWF monomers and disulfide-linked dimers. VWF D1-A1 was expressed in <t>Expi293</t> cells and purified from the media as monomers and disulfide-linked dimers. The furin cleavage site was mutated to ASAS to prevent prodomain dissociation. (C) DLS experiments of purified D1-A1 incubated at indicated pH showing an increase in average hydrodynamic radius with a decrease in pH. Error bars represent the difference between the means from 2 replicates. (D) Representative micrographs from negative-stain electron microscopy showing VWF dimers incubated at pH 7.4 and 5.2 (scale bars, 50 nm). (E) Quantification of (D) showing particle lengths measured from 3 micrographs from samples incubated together overnight. The bottom, middle, and top lines of the shaded boxes represent the first quartile, the median, and the third quartile of measured particle length, respectively. The length of the whiskers below and above the box plot represent the lesser of the range of data or 1.5 multiplied by the interquartile range. (F) Schematic and cryo-EM structure of the dimer-derived tubule showing the bead-like arrangement. The structure forms a right-handed helix with a helical rise of 26.8 Å and a helical twist of 83.3°. The cryo-EM map has been Gaussian filtered for visualization.
Lipo293tm Transfection Reagent, supplied by Beyotime, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/transfectants/Lipo293+Transfection+Reagent/pm37176078-368-12-15
Average 99 stars, based on 1 article reviews
lipo293tm transfection reagent - by Bioz Stars, 2026-10
99/100 stars
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96
Beyotime calciumphosphate cell transfection kit
Structure of a VWF tubule. (A) Schematic of the domain organization of the VWF proprotein. Each D assembly except D′ is made of domains VWF type D domain, C8, TIL (trypsin inhibitor-like cysteine-rich domain), and E. D1 and D2 form a prodomain that is cleaved by furin protease before secretion. (B) Strategy to obtain VWF monomers and disulfide-linked dimers. VWF D1-A1 was expressed in <t>Expi293</t> cells and purified from the media as monomers and disulfide-linked dimers. The furin cleavage site was mutated to ASAS to prevent prodomain dissociation. (C) DLS experiments of purified D1-A1 incubated at indicated pH showing an increase in average hydrodynamic radius with a decrease in pH. Error bars represent the difference between the means from 2 replicates. (D) Representative micrographs from negative-stain electron microscopy showing VWF dimers incubated at pH 7.4 and 5.2 (scale bars, 50 nm). (E) Quantification of (D) showing particle lengths measured from 3 micrographs from samples incubated together overnight. The bottom, middle, and top lines of the shaded boxes represent the first quartile, the median, and the third quartile of measured particle length, respectively. The length of the whiskers below and above the box plot represent the lesser of the range of data or 1.5 multiplied by the interquartile range. (F) Schematic and cryo-EM structure of the dimer-derived tubule showing the bead-like arrangement. The structure forms a right-handed helix with a helical rise of 26.8 Å and a helical twist of 83.3°. The cryo-EM map has been Gaussian filtered for visualization.
Calciumphosphate Cell Transfection Kit, supplied by Beyotime, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/transfectants/Calcium+Phosphate+Cell+Transfection+Kit/pm37606180-249-23-27
Average 96 stars, based on 1 article reviews
calciumphosphate cell transfection kit - by Bioz Stars, 2026-10
96/100 stars
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92
Sartorius AG pcmv sb100x
Structure of a VWF tubule. (A) Schematic of the domain organization of the VWF proprotein. Each D assembly except D′ is made of domains VWF type D domain, C8, TIL (trypsin inhibitor-like cysteine-rich domain), and E. D1 and D2 form a prodomain that is cleaved by furin protease before secretion. (B) Strategy to obtain VWF monomers and disulfide-linked dimers. VWF D1-A1 was expressed in <t>Expi293</t> cells and purified from the media as monomers and disulfide-linked dimers. The furin cleavage site was mutated to ASAS to prevent prodomain dissociation. (C) DLS experiments of purified D1-A1 incubated at indicated pH showing an increase in average hydrodynamic radius with a decrease in pH. Error bars represent the difference between the means from 2 replicates. (D) Representative micrographs from negative-stain electron microscopy showing VWF dimers incubated at pH 7.4 and 5.2 (scale bars, 50 nm). (E) Quantification of (D) showing particle lengths measured from 3 micrographs from samples incubated together overnight. The bottom, middle, and top lines of the shaded boxes represent the first quartile, the median, and the third quartile of measured particle length, respectively. The length of the whiskers below and above the box plot represent the lesser of the range of data or 1.5 multiplied by the interquartile range. (F) Schematic and cryo-EM structure of the dimer-derived tubule showing the bead-like arrangement. The structure forms a right-handed helix with a helical rise of 26.8 Å and a helical twist of 83.3°. The cryo-EM map has been Gaussian filtered for visualization.
Pcmv Sb100x, supplied by Sartorius AG, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/transfectants/in+vivo-jetPEI/pmc05893599-175-14-18
Average 92 stars, based on 1 article reviews
pcmv sb100x - by Bioz Stars, 2026-10
92/100 stars
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92
OriGene 293hek cells
Structure of a VWF tubule. (A) Schematic of the domain organization of the VWF proprotein. Each D assembly except D′ is made of domains VWF type D domain, C8, TIL (trypsin inhibitor-like cysteine-rich domain), and E. D1 and D2 form a prodomain that is cleaved by furin protease before secretion. (B) Strategy to obtain VWF monomers and disulfide-linked dimers. VWF D1-A1 was expressed in <t>Expi293</t> cells and purified from the media as monomers and disulfide-linked dimers. The furin cleavage site was mutated to ASAS to prevent prodomain dissociation. (C) DLS experiments of purified D1-A1 incubated at indicated pH showing an increase in average hydrodynamic radius with a decrease in pH. Error bars represent the difference between the means from 2 replicates. (D) Representative micrographs from negative-stain electron microscopy showing VWF dimers incubated at pH 7.4 and 5.2 (scale bars, 50 nm). (E) Quantification of (D) showing particle lengths measured from 3 micrographs from samples incubated together overnight. The bottom, middle, and top lines of the shaded boxes represent the first quartile, the median, and the third quartile of measured particle length, respectively. The length of the whiskers below and above the box plot represent the lesser of the range of data or 1.5 multiplied by the interquartile range. (F) Schematic and cryo-EM structure of the dimer-derived tubule showing the bead-like arrangement. The structure forms a right-handed helix with a helical rise of 26.8 Å and a helical twist of 83.3°. The cryo-EM map has been Gaussian filtered for visualization.
293hek Cells, supplied by OriGene, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/transfectants/HEK293T+Cells+Un-transfected+Negative+Control/pm38448588-702-28-25
Average 92 stars, based on 1 article reviews
293hek cells - by Bioz Stars, 2026-10
92/100 stars
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96
OriGene sitran 1 0 sirna transfection reagent
Structure of a VWF tubule. (A) Schematic of the domain organization of the VWF proprotein. Each D assembly except D′ is made of domains VWF type D domain, C8, TIL (trypsin inhibitor-like cysteine-rich domain), and E. D1 and D2 form a prodomain that is cleaved by furin protease before secretion. (B) Strategy to obtain VWF monomers and disulfide-linked dimers. VWF D1-A1 was expressed in <t>Expi293</t> cells and purified from the media as monomers and disulfide-linked dimers. The furin cleavage site was mutated to ASAS to prevent prodomain dissociation. (C) DLS experiments of purified D1-A1 incubated at indicated pH showing an increase in average hydrodynamic radius with a decrease in pH. Error bars represent the difference between the means from 2 replicates. (D) Representative micrographs from negative-stain electron microscopy showing VWF dimers incubated at pH 7.4 and 5.2 (scale bars, 50 nm). (E) Quantification of (D) showing particle lengths measured from 3 micrographs from samples incubated together overnight. The bottom, middle, and top lines of the shaded boxes represent the first quartile, the median, and the third quartile of measured particle length, respectively. The length of the whiskers below and above the box plot represent the lesser of the range of data or 1.5 multiplied by the interquartile range. (F) Schematic and cryo-EM structure of the dimer-derived tubule showing the bead-like arrangement. The structure forms a right-handed helix with a helical rise of 26.8 Å and a helical twist of 83.3°. The cryo-EM map has been Gaussian filtered for visualization.
Sitran 1 0 Sirna Transfection Reagent, supplied by OriGene, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/transfectants/siTran+2%2E0+siRNA+transfection+reagent/pm31071489-225-28-34
Average 96 stars, based on 1 article reviews
sitran 1 0 sirna transfection reagent - by Bioz Stars, 2026-10
96/100 stars
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Image Search Results


Subcellular localization of SbNF-YA6. Arabidopsis protoplasts were transfected with 35S:GFP (control) or 35S:SbNF-YA6 -GFP. The fluorescence signals were detected under a confocal microscope. Chlorophyll autofluorescence was used to visualize chloroplasts.

Journal: Frontiers in Plant Science

Article Title: Identification of nuclear factor YA6 genes in sorghum and characterization of their involvement in drought tolerance

doi: 10.3389/fpls.2025.1524066

Figure Lengend Snippet: Subcellular localization of SbNF-YA6. Arabidopsis protoplasts were transfected with 35S:GFP (control) or 35S:SbNF-YA6 -GFP. The fluorescence signals were detected under a confocal microscope. Chlorophyll autofluorescence was used to visualize chloroplasts.

Article Snippet: A plant protoplast isolation kit (Beyotime, Beijing, China) was used to isolate protoplasts from Arabidopsis plants at the five- to six-leaf stage.

Techniques: Transfection, Control, Fluorescence, Microscopy

Structure of a VWF tubule. (A) Schematic of the domain organization of the VWF proprotein. Each D assembly except D′ is made of domains VWF type D domain, C8, TIL (trypsin inhibitor-like cysteine-rich domain), and E. D1 and D2 form a prodomain that is cleaved by furin protease before secretion. (B) Strategy to obtain VWF monomers and disulfide-linked dimers. VWF D1-A1 was expressed in Expi293 cells and purified from the media as monomers and disulfide-linked dimers. The furin cleavage site was mutated to ASAS to prevent prodomain dissociation. (C) DLS experiments of purified D1-A1 incubated at indicated pH showing an increase in average hydrodynamic radius with a decrease in pH. Error bars represent the difference between the means from 2 replicates. (D) Representative micrographs from negative-stain electron microscopy showing VWF dimers incubated at pH 7.4 and 5.2 (scale bars, 50 nm). (E) Quantification of (D) showing particle lengths measured from 3 micrographs from samples incubated together overnight. The bottom, middle, and top lines of the shaded boxes represent the first quartile, the median, and the third quartile of measured particle length, respectively. The length of the whiskers below and above the box plot represent the lesser of the range of data or 1.5 multiplied by the interquartile range. (F) Schematic and cryo-EM structure of the dimer-derived tubule showing the bead-like arrangement. The structure forms a right-handed helix with a helical rise of 26.8 Å and a helical twist of 83.3°. The cryo-EM map has been Gaussian filtered for visualization.

Journal: Blood

Article Title: Structures of VWF tubules before and after concatemerization reveal a mechanism of disulfide bond exchange

doi: 10.1182/blood.2022016467

Figure Lengend Snippet: Structure of a VWF tubule. (A) Schematic of the domain organization of the VWF proprotein. Each D assembly except D′ is made of domains VWF type D domain, C8, TIL (trypsin inhibitor-like cysteine-rich domain), and E. D1 and D2 form a prodomain that is cleaved by furin protease before secretion. (B) Strategy to obtain VWF monomers and disulfide-linked dimers. VWF D1-A1 was expressed in Expi293 cells and purified from the media as monomers and disulfide-linked dimers. The furin cleavage site was mutated to ASAS to prevent prodomain dissociation. (C) DLS experiments of purified D1-A1 incubated at indicated pH showing an increase in average hydrodynamic radius with a decrease in pH. Error bars represent the difference between the means from 2 replicates. (D) Representative micrographs from negative-stain electron microscopy showing VWF dimers incubated at pH 7.4 and 5.2 (scale bars, 50 nm). (E) Quantification of (D) showing particle lengths measured from 3 micrographs from samples incubated together overnight. The bottom, middle, and top lines of the shaded boxes represent the first quartile, the median, and the third quartile of measured particle length, respectively. The length of the whiskers below and above the box plot represent the lesser of the range of data or 1.5 multiplied by the interquartile range. (F) Schematic and cryo-EM structure of the dimer-derived tubule showing the bead-like arrangement. The structure forms a right-handed helix with a helical rise of 26.8 Å and a helical twist of 83.3°. The cryo-EM map has been Gaussian filtered for visualization.

Article Snippet: 1 L of Expi293 cells in Expi293 medium were transfected using FectoPRO (Polyplus, #101000014).

Techniques: Purification, Incubation, Staining, Electron Microscopy, Cryo-EM Sample Prep, Derivative Assay