mturquoise2 Search Results


paav gfabcid 2xnls mturquoise2  (Addgene inc)
90
Addgene inc paav gfabcid 2xnls mturquoise2
Paav Gfabcid 2xnls Mturquoise2, supplied by Addgene inc, 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/paav gfabcid 2xnls mturquoise2/product/Addgene inc
Average 90 stars, based on 1 article reviews
paav gfabcid 2xnls mturquoise2 - by Bioz Stars, 2026-03
90/100 stars
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plifeact mturquoise2  (Addgene inc)
93
Addgene inc plifeact mturquoise2
Plifeact Mturquoise2, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 93 stars, based on 1 article reviews
plifeact mturquoise2 - by Bioz Stars, 2026-03
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pmturquoise2 n1  (Addgene inc)
94
Addgene inc pmturquoise2 n1
Pmturquoise2 N1, supplied by Addgene inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 94 stars, based on 1 article reviews
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mturquoise2  (Addgene inc)
93
Addgene inc mturquoise2
Workflow: a) We selected 3,750 de novo emerged human sequences from the sORFs database and generated a library of comparable random sequences. Protein structure properties were predicted computationally. After ordering the libraries as oligonucleotides they were cloned into the pETMF plasmid and transformed into E. coli for the FRET-FACS assay. b) The FACS was performed in two sequential rounds for both libraries separately. Presorted cells containing single library sequences were sorted into FRET-positive (on the left in green) and FRET-negative (on the right in red) samples. Samples with * were recovered, sent for next-generation sequencing (NGS) and used for enrichment analysis. c) The library sORF proteins (gray) are tagged with fluorescent proteins (FP) mVenus (acceptor FP in yellow) and <t>mTurquoise2</t> (donor FP in blue) on the termini with GGS spacers. Compact library sORF proteins place the fluorescent proteins in close proximity and are expected to cause FRET. Disordered or fibrillar library proteins are expected to be FRET-negative. d) The presorted samples contain all library protein structures. The first round is expected to result in separation of compact and disordered structures, which becomes more pronounced in the second round. The FRET-negative proteins should have an increased N- to C-terminal distance and disorder, while the FRET-positive proteins show increased compactness and folding. Made with BioRender.
Mturquoise2, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/mturquoise2/product/Addgene inc
Average 93 stars, based on 1 article reviews
mturquoise2 - by Bioz Stars, 2026-03
93/100 stars
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pcam140 apr smr  (Addgene inc)
93
Addgene inc pcam140 apr smr
Workflow: a) We selected 3,750 de novo emerged human sequences from the sORFs database and generated a library of comparable random sequences. Protein structure properties were predicted computationally. After ordering the libraries as oligonucleotides they were cloned into the pETMF plasmid and transformed into E. coli for the FRET-FACS assay. b) The FACS was performed in two sequential rounds for both libraries separately. Presorted cells containing single library sequences were sorted into FRET-positive (on the left in green) and FRET-negative (on the right in red) samples. Samples with * were recovered, sent for next-generation sequencing (NGS) and used for enrichment analysis. c) The library sORF proteins (gray) are tagged with fluorescent proteins (FP) mVenus (acceptor FP in yellow) and <t>mTurquoise2</t> (donor FP in blue) on the termini with GGS spacers. Compact library sORF proteins place the fluorescent proteins in close proximity and are expected to cause FRET. Disordered or fibrillar library proteins are expected to be FRET-negative. d) The presorted samples contain all library protein structures. The first round is expected to result in separation of compact and disordered structures, which becomes more pronounced in the second round. The FRET-negative proteins should have an increased N- to C-terminal distance and disorder, while the FRET-positive proteins show increased compactness and folding. Made with BioRender.
Pcam140 Apr Smr, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/pcam140 apr smr/product/Addgene inc
Average 93 stars, based on 1 article reviews
pcam140 apr smr - by Bioz Stars, 2026-03
93/100 stars
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mturquoise2 slbp 18 126 ires h1 mmaroon1  (Addgene inc)
93
Addgene inc mturquoise2 slbp 18 126 ires h1 mmaroon1
Workflow: a) We selected 3,750 de novo emerged human sequences from the sORFs database and generated a library of comparable random sequences. Protein structure properties were predicted computationally. After ordering the libraries as oligonucleotides they were cloned into the pETMF plasmid and transformed into E. coli for the FRET-FACS assay. b) The FACS was performed in two sequential rounds for both libraries separately. Presorted cells containing single library sequences were sorted into FRET-positive (on the left in green) and FRET-negative (on the right in red) samples. Samples with * were recovered, sent for next-generation sequencing (NGS) and used for enrichment analysis. c) The library sORF proteins (gray) are tagged with fluorescent proteins (FP) mVenus (acceptor FP in yellow) and <t>mTurquoise2</t> (donor FP in blue) on the termini with GGS spacers. Compact library sORF proteins place the fluorescent proteins in close proximity and are expected to cause FRET. Disordered or fibrillar library proteins are expected to be FRET-negative. d) The presorted samples contain all library protein structures. The first round is expected to result in separation of compact and disordered structures, which becomes more pronounced in the second round. The FRET-negative proteins should have an increased N- to C-terminal distance and disorder, while the FRET-positive proteins show increased compactness and folding. Made with BioRender.
Mturquoise2 Slbp 18 126 Ires H1 Mmaroon1, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/mturquoise2 slbp 18 126 ires h1 mmaroon1/product/Addgene inc
Average 93 stars, based on 1 article reviews
mturquoise2 slbp 18 126 ires h1 mmaroon1 - by Bioz Stars, 2026-03
93/100 stars
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mturquoise2 giantin  (Addgene inc)
93
Addgene inc mturquoise2 giantin
Workflow: a) We selected 3,750 de novo emerged human sequences from the sORFs database and generated a library of comparable random sequences. Protein structure properties were predicted computationally. After ordering the libraries as oligonucleotides they were cloned into the pETMF plasmid and transformed into E. coli for the FRET-FACS assay. b) The FACS was performed in two sequential rounds for both libraries separately. Presorted cells containing single library sequences were sorted into FRET-positive (on the left in green) and FRET-negative (on the right in red) samples. Samples with * were recovered, sent for next-generation sequencing (NGS) and used for enrichment analysis. c) The library sORF proteins (gray) are tagged with fluorescent proteins (FP) mVenus (acceptor FP in yellow) and <t>mTurquoise2</t> (donor FP in blue) on the termini with GGS spacers. Compact library sORF proteins place the fluorescent proteins in close proximity and are expected to cause FRET. Disordered or fibrillar library proteins are expected to be FRET-negative. d) The presorted samples contain all library protein structures. The first round is expected to result in separation of compact and disordered structures, which becomes more pronounced in the second round. The FRET-negative proteins should have an increased N- to C-terminal distance and disorder, while the FRET-positive proteins show increased compactness and folding. Made with BioRender.
Mturquoise2 Giantin, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/mturquoise2 giantin/product/Addgene inc
Average 93 stars, based on 1 article reviews
mturquoise2 giantin - by Bioz Stars, 2026-03
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ppalmitoyl turquoise2  (Addgene inc)
93
Addgene inc ppalmitoyl turquoise2
Workflow: a) We selected 3,750 de novo emerged human sequences from the sORFs database and generated a library of comparable random sequences. Protein structure properties were predicted computationally. After ordering the libraries as oligonucleotides they were cloned into the pETMF plasmid and transformed into E. coli for the FRET-FACS assay. b) The FACS was performed in two sequential rounds for both libraries separately. Presorted cells containing single library sequences were sorted into FRET-positive (on the left in green) and FRET-negative (on the right in red) samples. Samples with * were recovered, sent for next-generation sequencing (NGS) and used for enrichment analysis. c) The library sORF proteins (gray) are tagged with fluorescent proteins (FP) mVenus (acceptor FP in yellow) and <t>mTurquoise2</t> (donor FP in blue) on the termini with GGS spacers. Compact library sORF proteins place the fluorescent proteins in close proximity and are expected to cause FRET. Disordered or fibrillar library proteins are expected to be FRET-negative. d) The presorted samples contain all library protein structures. The first round is expected to result in separation of compact and disordered structures, which becomes more pronounced in the second round. The FRET-negative proteins should have an increased N- to C-terminal distance and disorder, while the FRET-positive proteins show increased compactness and folding. Made with BioRender.
Ppalmitoyl Turquoise2, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/ppalmitoyl turquoise2/product/Addgene inc
Average 93 stars, based on 1 article reviews
ppalmitoyl turquoise2 - by Bioz Stars, 2026-03
93/100 stars
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psd 95 binding nanobody construct pcag xph15 mturquoise2 ccr5tc  (Addgene inc)
93
Addgene inc psd 95 binding nanobody construct pcag xph15 mturquoise2 ccr5tc
Workflow: a) We selected 3,750 de novo emerged human sequences from the sORFs database and generated a library of comparable random sequences. Protein structure properties were predicted computationally. After ordering the libraries as oligonucleotides they were cloned into the pETMF plasmid and transformed into E. coli for the FRET-FACS assay. b) The FACS was performed in two sequential rounds for both libraries separately. Presorted cells containing single library sequences were sorted into FRET-positive (on the left in green) and FRET-negative (on the right in red) samples. Samples with * were recovered, sent for next-generation sequencing (NGS) and used for enrichment analysis. c) The library sORF proteins (gray) are tagged with fluorescent proteins (FP) mVenus (acceptor FP in yellow) and <t>mTurquoise2</t> (donor FP in blue) on the termini with GGS spacers. Compact library sORF proteins place the fluorescent proteins in close proximity and are expected to cause FRET. Disordered or fibrillar library proteins are expected to be FRET-negative. d) The presorted samples contain all library protein structures. The first round is expected to result in separation of compact and disordered structures, which becomes more pronounced in the second round. The FRET-negative proteins should have an increased N- to C-terminal distance and disorder, while the FRET-positive proteins show increased compactness and folding. Made with BioRender.
Psd 95 Binding Nanobody Construct Pcag Xph15 Mturquoise2 Ccr5tc, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/psd 95 binding nanobody construct pcag xph15 mturquoise2 ccr5tc/product/Addgene inc
Average 93 stars, based on 1 article reviews
psd 95 binding nanobody construct pcag xph15 mturquoise2 ccr5tc - by Bioz Stars, 2026-03
93/100 stars
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paav cag mturquoise2 plasmid  (Addgene inc)
91
Addgene inc paav cag mturquoise2 plasmid
Workflow: a) We selected 3,750 de novo emerged human sequences from the sORFs database and generated a library of comparable random sequences. Protein structure properties were predicted computationally. After ordering the libraries as oligonucleotides they were cloned into the pETMF plasmid and transformed into E. coli for the FRET-FACS assay. b) The FACS was performed in two sequential rounds for both libraries separately. Presorted cells containing single library sequences were sorted into FRET-positive (on the left in green) and FRET-negative (on the right in red) samples. Samples with * were recovered, sent for next-generation sequencing (NGS) and used for enrichment analysis. c) The library sORF proteins (gray) are tagged with fluorescent proteins (FP) mVenus (acceptor FP in yellow) and <t>mTurquoise2</t> (donor FP in blue) on the termini with GGS spacers. Compact library sORF proteins place the fluorescent proteins in close proximity and are expected to cause FRET. Disordered or fibrillar library proteins are expected to be FRET-negative. d) The presorted samples contain all library protein structures. The first round is expected to result in separation of compact and disordered structures, which becomes more pronounced in the second round. The FRET-negative proteins should have an increased N- to C-terminal distance and disorder, while the FRET-positive proteins show increased compactness and folding. Made with BioRender.
Paav Cag Mturquoise2 Plasmid, supplied by Addgene inc, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/paav cag mturquoise2 plasmid/product/Addgene inc
Average 91 stars, based on 1 article reviews
paav cag mturquoise2 plasmid - by Bioz Stars, 2026-03
91/100 stars
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lysosome marker lamp1 mturquoise2  (Addgene inc)
93
Addgene inc lysosome marker lamp1 mturquoise2
Workflow: a) We selected 3,750 de novo emerged human sequences from the sORFs database and generated a library of comparable random sequences. Protein structure properties were predicted computationally. After ordering the libraries as oligonucleotides they were cloned into the pETMF plasmid and transformed into E. coli for the FRET-FACS assay. b) The FACS was performed in two sequential rounds for both libraries separately. Presorted cells containing single library sequences were sorted into FRET-positive (on the left in green) and FRET-negative (on the right in red) samples. Samples with * were recovered, sent for next-generation sequencing (NGS) and used for enrichment analysis. c) The library sORF proteins (gray) are tagged with fluorescent proteins (FP) mVenus (acceptor FP in yellow) and <t>mTurquoise2</t> (donor FP in blue) on the termini with GGS spacers. Compact library sORF proteins place the fluorescent proteins in close proximity and are expected to cause FRET. Disordered or fibrillar library proteins are expected to be FRET-negative. d) The presorted samples contain all library protein structures. The first round is expected to result in separation of compact and disordered structures, which becomes more pronounced in the second round. The FRET-negative proteins should have an increased N- to C-terminal distance and disorder, while the FRET-positive proteins show increased compactness and folding. Made with BioRender.
Lysosome Marker Lamp1 Mturquoise2, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/lysosome marker lamp1 mturquoise2/product/Addgene inc
Average 93 stars, based on 1 article reviews
lysosome marker lamp1 mturquoise2 - by Bioz Stars, 2026-03
93/100 stars
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pdd315  (Addgene inc)
93
Addgene inc pdd315
Workflow: a) We selected 3,750 de novo emerged human sequences from the sORFs database and generated a library of comparable random sequences. Protein structure properties were predicted computationally. After ordering the libraries as oligonucleotides they were cloned into the pETMF plasmid and transformed into E. coli for the FRET-FACS assay. b) The FACS was performed in two sequential rounds for both libraries separately. Presorted cells containing single library sequences were sorted into FRET-positive (on the left in green) and FRET-negative (on the right in red) samples. Samples with * were recovered, sent for next-generation sequencing (NGS) and used for enrichment analysis. c) The library sORF proteins (gray) are tagged with fluorescent proteins (FP) mVenus (acceptor FP in yellow) and <t>mTurquoise2</t> (donor FP in blue) on the termini with GGS spacers. Compact library sORF proteins place the fluorescent proteins in close proximity and are expected to cause FRET. Disordered or fibrillar library proteins are expected to be FRET-negative. d) The presorted samples contain all library protein structures. The first round is expected to result in separation of compact and disordered structures, which becomes more pronounced in the second round. The FRET-negative proteins should have an increased N- to C-terminal distance and disorder, while the FRET-positive proteins show increased compactness and folding. Made with BioRender.
Pdd315, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/pdd315/product/Addgene inc
Average 93 stars, based on 1 article reviews
pdd315 - by Bioz Stars, 2026-03
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Image Search Results


Workflow: a) We selected 3,750 de novo emerged human sequences from the sORFs database and generated a library of comparable random sequences. Protein structure properties were predicted computationally. After ordering the libraries as oligonucleotides they were cloned into the pETMF plasmid and transformed into E. coli for the FRET-FACS assay. b) The FACS was performed in two sequential rounds for both libraries separately. Presorted cells containing single library sequences were sorted into FRET-positive (on the left in green) and FRET-negative (on the right in red) samples. Samples with * were recovered, sent for next-generation sequencing (NGS) and used for enrichment analysis. c) The library sORF proteins (gray) are tagged with fluorescent proteins (FP) mVenus (acceptor FP in yellow) and mTurquoise2 (donor FP in blue) on the termini with GGS spacers. Compact library sORF proteins place the fluorescent proteins in close proximity and are expected to cause FRET. Disordered or fibrillar library proteins are expected to be FRET-negative. d) The presorted samples contain all library protein structures. The first round is expected to result in separation of compact and disordered structures, which becomes more pronounced in the second round. The FRET-negative proteins should have an increased N- to C-terminal distance and disorder, while the FRET-positive proteins show increased compactness and folding. Made with BioRender.

Journal: Genome Biology and Evolution

Article Title: High-throughput Selection of Human de novo -emerged sORFs with High Folding Potential

doi: 10.1093/gbe/evae069

Figure Lengend Snippet: Workflow: a) We selected 3,750 de novo emerged human sequences from the sORFs database and generated a library of comparable random sequences. Protein structure properties were predicted computationally. After ordering the libraries as oligonucleotides they were cloned into the pETMF plasmid and transformed into E. coli for the FRET-FACS assay. b) The FACS was performed in two sequential rounds for both libraries separately. Presorted cells containing single library sequences were sorted into FRET-positive (on the left in green) and FRET-negative (on the right in red) samples. Samples with * were recovered, sent for next-generation sequencing (NGS) and used for enrichment analysis. c) The library sORF proteins (gray) are tagged with fluorescent proteins (FP) mVenus (acceptor FP in yellow) and mTurquoise2 (donor FP in blue) on the termini with GGS spacers. Compact library sORF proteins place the fluorescent proteins in close proximity and are expected to cause FRET. Disordered or fibrillar library proteins are expected to be FRET-negative. d) The presorted samples contain all library protein structures. The first round is expected to result in separation of compact and disordered structures, which becomes more pronounced in the second round. The FRET-negative proteins should have an increased N- to C-terminal distance and disorder, while the FRET-positive proteins show increased compactness and folding. Made with BioRender.

Article Snippet: Plasmid harboring mVenus was obtained from Addgene (catalogue no.: 103,986) and mTurquoise2 was a gift from Ondrej Havranek (coding sequence corresponding to Addgene catalog no.: 61,602).

Techniques: Generated, Clone Assay, Plasmid Preparation, Transformation Assay, Next-Generation Sequencing

Fluorescence Lifetime of Different Control Proteins Measured in vivo

Journal: Genome Biology and Evolution

Article Title: High-throughput Selection of Human de novo -emerged sORFs with High Folding Potential

doi: 10.1093/gbe/evae069

Figure Lengend Snippet: Fluorescence Lifetime of Different Control Proteins Measured in vivo

Article Snippet: Plasmid harboring mVenus was obtained from Addgene (catalogue no.: 103,986) and mTurquoise2 was a gift from Ondrej Havranek (coding sequence corresponding to Addgene catalog no.: 61,602).

Techniques: Fluorescence, Control