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anti gst antibody  (Cytiva Europe)
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Cytiva Europe anti gst antibody
Anti Gst Antibody, supplied by Cytiva Europe, 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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e18 gst ncegt1  (Kaneka Corp)
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Kaneka Corp e18 gst ncegt1
Effects of solubility tags and stability mutations on <t>NcEGT1</t> expression and EGT synthesis. (A) Expression analysis of recombinant proteins NcEGT1 and TrEGT1 in S. cerevisiae. Coomassie Blue-stained SDS-PAGE gel showing total protein extracts from different yeast strains: the parental strain (SC), strain expressing the wild-type Ncegt1 and Tregt2 genes (WT-EGT) and strain E1 expressing the codon-optimized Ncegt1 and Tregt2 genes (CO-EGT). Equal amounts of total protein were loaded. M: protein molecular weight marker. The arrowheads indicate the expected positions of NcEGT1 (≈99 kDa) and TrEGT2 (≈53 kDa). +: soluble crude extract. -: insoluble crude extract. (B) Soluble expression analysis of fusion proteins with different solubility tags. MBP-NcEGT1 (≈139.9 <t>kDa),</t> <t>GST-NcEGT1</t> (≈125 kDa), NusA-NcEGT1(≈154.4 kDa), TrxA-NcEGT1(≈111.3 kDa) (C) Effect of different solubility tags on EGT production. (D) Effect of single-point mutations on EGT production. (E) Spatial distribution of key stability-related mutation sites in NcEGT1. The structure predicted by AlphaFold2 shows mutation sites used in double-mutant construction: A458P (pink, optimal) and five high-effect sites (blue), each combined with A458P. (F) Effect of double-point mutations on EGT production. All data presented as mean ± S.D. from three (n = 3) biological independent replicates.
E18 Gst Ncegt1, supplied by Kaneka Corp, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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gst sc 138  (Santa Cruz Biotechnology)
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Santa Cruz Biotechnology gst sc 138
Effects of solubility tags and stability mutations on <t>NcEGT1</t> expression and EGT synthesis. (A) Expression analysis of recombinant proteins NcEGT1 and TrEGT1 in S. cerevisiae. Coomassie Blue-stained SDS-PAGE gel showing total protein extracts from different yeast strains: the parental strain (SC), strain expressing the wild-type Ncegt1 and Tregt2 genes (WT-EGT) and strain E1 expressing the codon-optimized Ncegt1 and Tregt2 genes (CO-EGT). Equal amounts of total protein were loaded. M: protein molecular weight marker. The arrowheads indicate the expected positions of NcEGT1 (≈99 kDa) and TrEGT2 (≈53 kDa). +: soluble crude extract. -: insoluble crude extract. (B) Soluble expression analysis of fusion proteins with different solubility tags. MBP-NcEGT1 (≈139.9 <t>kDa),</t> <t>GST-NcEGT1</t> (≈125 kDa), NusA-NcEGT1(≈154.4 kDa), TrxA-NcEGT1(≈111.3 kDa) (C) Effect of different solubility tags on EGT production. (D) Effect of single-point mutations on EGT production. (E) Spatial distribution of key stability-related mutation sites in NcEGT1. The structure predicted by AlphaFold2 shows mutation sites used in double-mutant construction: A458P (pink, optimal) and five high-effect sites (blue), each combined with A458P. (F) Effect of double-point mutations on EGT production. All data presented as mean ± S.D. from three (n = 3) biological independent replicates.
Gst Sc 138, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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anti gst  (ABclonal Biotechnology)
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ABclonal Biotechnology anti gst
Effects of solubility tags and stability mutations on <t>NcEGT1</t> expression and EGT synthesis. (A) Expression analysis of recombinant proteins NcEGT1 and TrEGT1 in S. cerevisiae. Coomassie Blue-stained SDS-PAGE gel showing total protein extracts from different yeast strains: the parental strain (SC), strain expressing the wild-type Ncegt1 and Tregt2 genes (WT-EGT) and strain E1 expressing the codon-optimized Ncegt1 and Tregt2 genes (CO-EGT). Equal amounts of total protein were loaded. M: protein molecular weight marker. The arrowheads indicate the expected positions of NcEGT1 (≈99 kDa) and TrEGT2 (≈53 kDa). +: soluble crude extract. -: insoluble crude extract. (B) Soluble expression analysis of fusion proteins with different solubility tags. MBP-NcEGT1 (≈139.9 <t>kDa),</t> <t>GST-NcEGT1</t> (≈125 kDa), NusA-NcEGT1(≈154.4 kDa), TrxA-NcEGT1(≈111.3 kDa) (C) Effect of different solubility tags on EGT production. (D) Effect of single-point mutations on EGT production. (E) Spatial distribution of key stability-related mutation sites in NcEGT1. The structure predicted by AlphaFold2 shows mutation sites used in double-mutant construction: A458P (pink, optimal) and five high-effect sites (blue), each combined with A458P. (F) Effect of double-point mutations on EGT production. All data presented as mean ± S.D. from three (n = 3) biological independent replicates.
Anti Gst, supplied by ABclonal Biotechnology, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/gst/Rabbit+anti+GST-Tag+pAb/pm42838988-445-17-18
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anti gst - by Bioz Stars, 2026-10
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gst tag  (Cytiva Europe)
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Cytiva Europe gst tag
Effects of solubility tags and stability mutations on <t>NcEGT1</t> expression and EGT synthesis. (A) Expression analysis of recombinant proteins NcEGT1 and TrEGT1 in S. cerevisiae. Coomassie Blue-stained SDS-PAGE gel showing total protein extracts from different yeast strains: the parental strain (SC), strain expressing the wild-type Ncegt1 and Tregt2 genes (WT-EGT) and strain E1 expressing the codon-optimized Ncegt1 and Tregt2 genes (CO-EGT). Equal amounts of total protein were loaded. M: protein molecular weight marker. The arrowheads indicate the expected positions of NcEGT1 (≈99 kDa) and TrEGT2 (≈53 kDa). +: soluble crude extract. -: insoluble crude extract. (B) Soluble expression analysis of fusion proteins with different solubility tags. MBP-NcEGT1 (≈139.9 <t>kDa),</t> <t>GST-NcEGT1</t> (≈125 kDa), NusA-NcEGT1(≈154.4 kDa), TrxA-NcEGT1(≈111.3 kDa) (C) Effect of different solubility tags on EGT production. (D) Effect of single-point mutations on EGT production. (E) Spatial distribution of key stability-related mutation sites in NcEGT1. The structure predicted by AlphaFold2 shows mutation sites used in double-mutant construction: A458P (pink, optimal) and five high-effect sites (blue), each combined with A458P. (F) Effect of double-point mutations on EGT production. All data presented as mean ± S.D. from three (n = 3) biological independent replicates.
Gst Tag, supplied by Cytiva Europe, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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protino glutathione agarose 4b  (MACHEREY NAGEL)
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MACHEREY NAGEL protino glutathione agarose 4b
Effects of solubility tags and stability mutations on <t>NcEGT1</t> expression and EGT synthesis. (A) Expression analysis of recombinant proteins NcEGT1 and TrEGT1 in S. cerevisiae. Coomassie Blue-stained SDS-PAGE gel showing total protein extracts from different yeast strains: the parental strain (SC), strain expressing the wild-type Ncegt1 and Tregt2 genes (WT-EGT) and strain E1 expressing the codon-optimized Ncegt1 and Tregt2 genes (CO-EGT). Equal amounts of total protein were loaded. M: protein molecular weight marker. The arrowheads indicate the expected positions of NcEGT1 (≈99 kDa) and TrEGT2 (≈53 kDa). +: soluble crude extract. -: insoluble crude extract. (B) Soluble expression analysis of fusion proteins with different solubility tags. MBP-NcEGT1 (≈139.9 <t>kDa),</t> <t>GST-NcEGT1</t> (≈125 kDa), NusA-NcEGT1(≈154.4 kDa), TrxA-NcEGT1(≈111.3 kDa) (C) Effect of different solubility tags on EGT production. (D) Effect of single-point mutations on EGT production. (E) Spatial distribution of key stability-related mutation sites in NcEGT1. The structure predicted by AlphaFold2 shows mutation sites used in double-mutant construction: A458P (pink, optimal) and five high-effect sites (blue), each combined with A458P. (F) Effect of double-point mutations on EGT production. All data presented as mean ± S.D. from three (n = 3) biological independent replicates.
Protino Glutathione Agarose 4b, supplied by MACHEREY NAGEL, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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gst tag  (Proteintech)
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Proteintech gst tag
Effects of solubility tags and stability mutations on <t>NcEGT1</t> expression and EGT synthesis. (A) Expression analysis of recombinant proteins NcEGT1 and TrEGT1 in S. cerevisiae. Coomassie Blue-stained SDS-PAGE gel showing total protein extracts from different yeast strains: the parental strain (SC), strain expressing the wild-type Ncegt1 and Tregt2 genes (WT-EGT) and strain E1 expressing the codon-optimized Ncegt1 and Tregt2 genes (CO-EGT). Equal amounts of total protein were loaded. M: protein molecular weight marker. The arrowheads indicate the expected positions of NcEGT1 (≈99 kDa) and TrEGT2 (≈53 kDa). +: soluble crude extract. -: insoluble crude extract. (B) Soluble expression analysis of fusion proteins with different solubility tags. MBP-NcEGT1 (≈139.9 <t>kDa),</t> <t>GST-NcEGT1</t> (≈125 kDa), NusA-NcEGT1(≈154.4 kDa), TrxA-NcEGT1(≈111.3 kDa) (C) Effect of different solubility tags on EGT production. (D) Effect of single-point mutations on EGT production. (E) Spatial distribution of key stability-related mutation sites in NcEGT1. The structure predicted by AlphaFold2 shows mutation sites used in double-mutant construction: A458P (pink, optimal) and five high-effect sites (blue), each combined with A458P. (F) Effect of double-point mutations on EGT production. All data presented as mean ± S.D. from three (n = 3) biological independent replicates.
Gst Tag, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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mouse anti gst  (Santa Cruz Biotechnology)
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Santa Cruz Biotechnology mouse anti gst
Effects of solubility tags and stability mutations on <t>NcEGT1</t> expression and EGT synthesis. (A) Expression analysis of recombinant proteins NcEGT1 and TrEGT1 in S. cerevisiae. Coomassie Blue-stained SDS-PAGE gel showing total protein extracts from different yeast strains: the parental strain (SC), strain expressing the wild-type Ncegt1 and Tregt2 genes (WT-EGT) and strain E1 expressing the codon-optimized Ncegt1 and Tregt2 genes (CO-EGT). Equal amounts of total protein were loaded. M: protein molecular weight marker. The arrowheads indicate the expected positions of NcEGT1 (≈99 kDa) and TrEGT2 (≈53 kDa). +: soluble crude extract. -: insoluble crude extract. (B) Soluble expression analysis of fusion proteins with different solubility tags. MBP-NcEGT1 (≈139.9 <t>kDa),</t> <t>GST-NcEGT1</t> (≈125 kDa), NusA-NcEGT1(≈154.4 kDa), TrxA-NcEGT1(≈111.3 kDa) (C) Effect of different solubility tags on EGT production. (D) Effect of single-point mutations on EGT production. (E) Spatial distribution of key stability-related mutation sites in NcEGT1. The structure predicted by AlphaFold2 shows mutation sites used in double-mutant construction: A458P (pink, optimal) and five high-effect sites (blue), each combined with A458P. (F) Effect of double-point mutations on EGT production. All data presented as mean ± S.D. from three (n = 3) biological independent replicates.
Mouse Anti Gst, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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immunoblotting  (Cusabio)
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Cusabio immunoblotting
Effects of solubility tags and stability mutations on <t>NcEGT1</t> expression and EGT synthesis. (A) Expression analysis of recombinant proteins NcEGT1 and TrEGT1 in S. cerevisiae. Coomassie Blue-stained SDS-PAGE gel showing total protein extracts from different yeast strains: the parental strain (SC), strain expressing the wild-type Ncegt1 and Tregt2 genes (WT-EGT) and strain E1 expressing the codon-optimized Ncegt1 and Tregt2 genes (CO-EGT). Equal amounts of total protein were loaded. M: protein molecular weight marker. The arrowheads indicate the expected positions of NcEGT1 (≈99 kDa) and TrEGT2 (≈53 kDa). +: soluble crude extract. -: insoluble crude extract. (B) Soluble expression analysis of fusion proteins with different solubility tags. MBP-NcEGT1 (≈139.9 <t>kDa),</t> <t>GST-NcEGT1</t> (≈125 kDa), NusA-NcEGT1(≈154.4 kDa), TrxA-NcEGT1(≈111.3 kDa) (C) Effect of different solubility tags on EGT production. (D) Effect of single-point mutations on EGT production. (E) Spatial distribution of key stability-related mutation sites in NcEGT1. The structure predicted by AlphaFold2 shows mutation sites used in double-mutant construction: A458P (pink, optimal) and five high-effect sites (blue), each combined with A458P. (F) Effect of double-point mutations on EGT production. All data presented as mean ± S.D. from three (n = 3) biological independent replicates.
Immunoblotting, supplied by Cusabio, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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gst antibody  (Cell Signaling Technology Inc)
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Cell Signaling Technology Inc gst antibody
Effects of solubility tags and stability mutations on <t>NcEGT1</t> expression and EGT synthesis. (A) Expression analysis of recombinant proteins NcEGT1 and TrEGT1 in S. cerevisiae. Coomassie Blue-stained SDS-PAGE gel showing total protein extracts from different yeast strains: the parental strain (SC), strain expressing the wild-type Ncegt1 and Tregt2 genes (WT-EGT) and strain E1 expressing the codon-optimized Ncegt1 and Tregt2 genes (CO-EGT). Equal amounts of total protein were loaded. M: protein molecular weight marker. The arrowheads indicate the expected positions of NcEGT1 (≈99 kDa) and TrEGT2 (≈53 kDa). +: soluble crude extract. -: insoluble crude extract. (B) Soluble expression analysis of fusion proteins with different solubility tags. MBP-NcEGT1 (≈139.9 <t>kDa),</t> <t>GST-NcEGT1</t> (≈125 kDa), NusA-NcEGT1(≈154.4 kDa), TrxA-NcEGT1(≈111.3 kDa) (C) Effect of different solubility tags on EGT production. (D) Effect of single-point mutations on EGT production. (E) Spatial distribution of key stability-related mutation sites in NcEGT1. The structure predicted by AlphaFold2 shows mutation sites used in double-mutant construction: A458P (pink, optimal) and five high-effect sites (blue), each combined with A458P. (F) Effect of double-point mutations on EGT production. All data presented as mean ± S.D. from three (n = 3) biological independent replicates.
Gst Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Effects of solubility tags and stability mutations on NcEGT1 expression and EGT synthesis. (A) Expression analysis of recombinant proteins NcEGT1 and TrEGT1 in S. cerevisiae. Coomassie Blue-stained SDS-PAGE gel showing total protein extracts from different yeast strains: the parental strain (SC), strain expressing the wild-type Ncegt1 and Tregt2 genes (WT-EGT) and strain E1 expressing the codon-optimized Ncegt1 and Tregt2 genes (CO-EGT). Equal amounts of total protein were loaded. M: protein molecular weight marker. The arrowheads indicate the expected positions of NcEGT1 (≈99 kDa) and TrEGT2 (≈53 kDa). +: soluble crude extract. -: insoluble crude extract. (B) Soluble expression analysis of fusion proteins with different solubility tags. MBP-NcEGT1 (≈139.9 kDa), GST-NcEGT1 (≈125 kDa), NusA-NcEGT1(≈154.4 kDa), TrxA-NcEGT1(≈111.3 kDa) (C) Effect of different solubility tags on EGT production. (D) Effect of single-point mutations on EGT production. (E) Spatial distribution of key stability-related mutation sites in NcEGT1. The structure predicted by AlphaFold2 shows mutation sites used in double-mutant construction: A458P (pink, optimal) and five high-effect sites (blue), each combined with A458P. (F) Effect of double-point mutations on EGT production. All data presented as mean ± S.D. from three (n = 3) biological independent replicates.

Journal: Synthetic and Systems Biotechnology

Article Title: Metabolic engineering of Saccharomyces cerevisiae for co-production of ergothioneine, salidroside and gadusol

doi: 10.1016/j.synbio.2026.04.010

Figure Lengend Snippet: Effects of solubility tags and stability mutations on NcEGT1 expression and EGT synthesis. (A) Expression analysis of recombinant proteins NcEGT1 and TrEGT1 in S. cerevisiae. Coomassie Blue-stained SDS-PAGE gel showing total protein extracts from different yeast strains: the parental strain (SC), strain expressing the wild-type Ncegt1 and Tregt2 genes (WT-EGT) and strain E1 expressing the codon-optimized Ncegt1 and Tregt2 genes (CO-EGT). Equal amounts of total protein were loaded. M: protein molecular weight marker. The arrowheads indicate the expected positions of NcEGT1 (≈99 kDa) and TrEGT2 (≈53 kDa). +: soluble crude extract. -: insoluble crude extract. (B) Soluble expression analysis of fusion proteins with different solubility tags. MBP-NcEGT1 (≈139.9 kDa), GST-NcEGT1 (≈125 kDa), NusA-NcEGT1(≈154.4 kDa), TrxA-NcEGT1(≈111.3 kDa) (C) Effect of different solubility tags on EGT production. (D) Effect of single-point mutations on EGT production. (E) Spatial distribution of key stability-related mutation sites in NcEGT1. The structure predicted by AlphaFold2 shows mutation sites used in double-mutant construction: A458P (pink, optimal) and five high-effect sites (blue), each combined with A458P. (F) Effect of double-point mutations on EGT production. All data presented as mean ± S.D. from three (n = 3) biological independent replicates.

Article Snippet: Among the constructed variants, a 33% increase in EGT production was observed in mutant E26 (GST-NcEGT1 A458P ) over that of E18 (GST-NcEGT1) ( D).

Techniques: Solubility, Expressing, Recombinant, Staining, SDS Page, Molecular Weight, Marker, Mutagenesis