1 m dtt Search Results


0.1 m dtt  (Promega)
90
Promega 0.1 m dtt
0.1 M Dtt, supplied by Promega, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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0.1 m dtt - by Bioz Stars, 2026-11
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dldithiothreitol (dtt) solution 1 m in water  (Merck KGaA)
90
Merck KGaA dldithiothreitol (dtt) solution 1 m in water
Dldithiothreitol (Dtt) Solution 1 M In Water, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 90 stars, based on 1 article reviews
dldithiothreitol (dtt) solution 1 m in water - by Bioz Stars, 2026-11
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nutrient broth with 15% glycerol  (Merck KGaA)
90
Merck KGaA nutrient broth with 15% glycerol
Nutrient Broth With 15% Glycerol, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 90 stars, based on 1 article reviews
nutrient broth with 15% glycerol - by Bioz Stars, 2026-11
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sdt-lysis buffer (4% (w/v) sds, 100 mm tris-hcl ph 7.6, 0.1 m dtt)  (Omni International)
90
Omni International sdt-lysis buffer (4% (w/v) sds, 100 mm tris-hcl ph 7.6, 0.1 m dtt)
Sdt Lysis Buffer (4% (W/V) Sds, 100 Mm Tris Hcl Ph 7.6, 0.1 M Dtt), supplied by Omni International, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 90 stars, based on 1 article reviews
sdt-lysis buffer (4% (w/v) sds, 100 mm tris-hcl ph 7.6, 0.1 m dtt) - by Bioz Stars, 2026-11
90/100 stars
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500 µl sds lysis buffer (0.05 m tris–hcl; 0.5% sds; 1 mm dtt; ph 8.0)  (Omni International)
90
Omni International 500 µl sds lysis buffer (0.05 m tris–hcl; 0.5% sds; 1 mm dtt; ph 8.0)
500 µl Sds Lysis Buffer (0.05 M Tris–Hcl; 0.5% Sds; 1 Mm Dtt; Ph 8.0), supplied by Omni International, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 90 stars, based on 1 article reviews
500 µl sds lysis buffer (0.05 m tris–hcl; 0.5% sds; 1 mm dtt; ph 8.0) - by Bioz Stars, 2026-11
90/100 stars
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10% 1 m dtt promega 0000085706  (Promega)
90
Promega 10% 1 m dtt promega 0000085706
10% 1 M Dtt Promega 0000085706, supplied by Promega, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 90 stars, based on 1 article reviews
10% 1 m dtt promega 0000085706 - by Bioz Stars, 2026-11
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zymolyase buffer (50 mm tris, ph 7.4, 10 mm mgcl2, 1 m sorbitol, and 30 mm dtt)  (Seikagaku corporation)
90
Seikagaku corporation zymolyase buffer (50 mm tris, ph 7.4, 10 mm mgcl2, 1 m sorbitol, and 30 mm dtt)
Zymolyase Buffer (50 Mm Tris, Ph 7.4, 10 Mm Mgcl2, 1 M Sorbitol, And 30 Mm Dtt), supplied by Seikagaku corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 90 stars, based on 1 article reviews
zymolyase buffer (50 mm tris, ph 7.4, 10 mm mgcl2, 1 m sorbitol, and 30 mm dtt) - by Bioz Stars, 2026-11
90/100 stars
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25 mm dtt  (Applichem inc)
90
Applichem inc 25 mm dtt
25 Mm Dtt, supplied by Applichem 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/product/1+m+dtt/0+1+m+dtt/pmc08274284-157-5-6
Average 90 stars, based on 1 article reviews
25 mm dtt - by Bioz Stars, 2026-11
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tetracolor one 5 mmol/l tetrazolium monosodium salt and 0.2 mmol/l 1-methoxy-5-methyl phenazinium methylsulfate  (Seikagaku corporation)
90
Seikagaku corporation tetracolor one 5 mmol/l tetrazolium monosodium salt and 0.2 mmol/l 1-methoxy-5-methyl phenazinium methylsulfate
Tetracolor One 5 Mmol/L Tetrazolium Monosodium Salt And 0.2 Mmol/L 1 Methoxy 5 Methyl Phenazinium Methylsulfate, supplied by Seikagaku corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 90 stars, based on 1 article reviews
tetracolor one 5 mmol/l tetrazolium monosodium salt and 0.2 mmol/l 1-methoxy-5-methyl phenazinium methylsulfate - by Bioz Stars, 2026-11
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1.4 mg/ml purified denatured (boiling in 1% sds, 0.1 m dtt) hbv core protein  (Moravian Biotech)
90
Moravian Biotech 1.4 mg/ml purified denatured (boiling in 1% sds, 0.1 m dtt) hbv core protein
( A ) Huh7 cells expressing HBV precore precursor were metabolically labeled for 30 min with 35 S, lysed, and subjected to immunoprecipitation with anti-core antibody. Immunoprecipitated samples were untreated (−) or treated (+) with λ protein phosphatase and separated by <t>SDS-PAGE.</t> The electrophoretic mobility of precore related proteins was analyzed by autoradiography. The migration positions of the HBV precore forms p25 p , p25, and p22 are indicated. ( B ) Ratios of individual precore protein forms produced in the presence (+) or absence (−) of <t>dithiothreitol</t> <t>(DTT).</t> Huh7 cells expressing the precore precursor were metabolically labeled for 30 min with 35 S under standard or reducing (5 mM DTT) conditions. HBV precore-derived proteins were immunoprecipitated from the harvested cells with anti-core antibody, separated by SDS-PAGE, and analyzed by autoradiography. ( C ) Electrophoretic mobility comparison of HBe and the HBe3CA mutant. The experiment was performed as for , (+) phosphorylation of HBe3CA p25 protein was demonstrated by λ-PP treatment. ( D ) Pulse-chase analysis of precore protein processing and secretion. Huh7 cells expressing HBe or HBe3CA proteins were metabolically labeled for 30 min with 35 S, and then chased for 0.5, 1, and 4 h. At all time points, both cells and media were harvested and subjected to immunoprecipitation with anti-core antibody. Proteins were separated by SDS-PAGE and analyzed by autoradiography. ( E ) Comparison of HBe secretion by cells infected with wild type and mutant precore rcccDNA. HepG2-NTCP cells in 12-well plates were infected in triplicate with wild type rcccDNA (wt rcccDNA) and mutant precore rcccDNA (HBe3CA rcccDNA) with equal MOI of 2000 VGE/cell. Secretion of HBe in the culture supernatants was determined by ELISA at days 0, 3, 6, and 14. Data are plotted as mean ± SEM of three biological replicates.
1.4 Mg/Ml Purified Denatured (Boiling In 1% Sds, 0.1 M Dtt) Hbv Core Protein, supplied by Moravian Biotech, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 90 stars, based on 1 article reviews
1.4 mg/ml purified denatured (boiling in 1% sds, 0.1 m dtt) hbv core protein - by Bioz Stars, 2026-11
90/100 stars
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0.1 m dtt  (BIONOVAS Biotechnology Co Ltd)
90
BIONOVAS Biotechnology Co Ltd 0.1 m dtt
( A ) Huh7 cells expressing HBV precore precursor were metabolically labeled for 30 min with 35 S, lysed, and subjected to immunoprecipitation with anti-core antibody. Immunoprecipitated samples were untreated (−) or treated (+) with λ protein phosphatase and separated by <t>SDS-PAGE.</t> The electrophoretic mobility of precore related proteins was analyzed by autoradiography. The migration positions of the HBV precore forms p25 p , p25, and p22 are indicated. ( B ) Ratios of individual precore protein forms produced in the presence (+) or absence (−) of <t>dithiothreitol</t> <t>(DTT).</t> Huh7 cells expressing the precore precursor were metabolically labeled for 30 min with 35 S under standard or reducing (5 mM DTT) conditions. HBV precore-derived proteins were immunoprecipitated from the harvested cells with anti-core antibody, separated by SDS-PAGE, and analyzed by autoradiography. ( C ) Electrophoretic mobility comparison of HBe and the HBe3CA mutant. The experiment was performed as for , (+) phosphorylation of HBe3CA p25 protein was demonstrated by λ-PP treatment. ( D ) Pulse-chase analysis of precore protein processing and secretion. Huh7 cells expressing HBe or HBe3CA proteins were metabolically labeled for 30 min with 35 S, and then chased for 0.5, 1, and 4 h. At all time points, both cells and media were harvested and subjected to immunoprecipitation with anti-core antibody. Proteins were separated by SDS-PAGE and analyzed by autoradiography. ( E ) Comparison of HBe secretion by cells infected with wild type and mutant precore rcccDNA. HepG2-NTCP cells in 12-well plates were infected in triplicate with wild type rcccDNA (wt rcccDNA) and mutant precore rcccDNA (HBe3CA rcccDNA) with equal MOI of 2000 VGE/cell. Secretion of HBe in the culture supernatants was determined by ELISA at days 0, 3, 6, and 14. Data are plotted as mean ± SEM of three biological replicates.
0.1 M Dtt, supplied by BIONOVAS Biotechnology Co Ltd, 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/product/1+m+dtt/0+1+m+dtt/pm39322998-59-10-11
Average 90 stars, based on 1 article reviews
0.1 m dtt - by Bioz Stars, 2026-11
90/100 stars
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0.1 m tris-hcl buffer (ph 8.5) containing 2 mm dithiothreitol (dtt)  (BioSpec)
90
BioSpec 0.1 m tris-hcl buffer (ph 8.5) containing 2 mm dithiothreitol (dtt)
( A ) Huh7 cells expressing HBV precore precursor were metabolically labeled for 30 min with 35 S, lysed, and subjected to immunoprecipitation with anti-core antibody. Immunoprecipitated samples were untreated (−) or treated (+) with λ protein phosphatase and separated by <t>SDS-PAGE.</t> The electrophoretic mobility of precore related proteins was analyzed by autoradiography. The migration positions of the HBV precore forms p25 p , p25, and p22 are indicated. ( B ) Ratios of individual precore protein forms produced in the presence (+) or absence (−) of <t>dithiothreitol</t> <t>(DTT).</t> Huh7 cells expressing the precore precursor were metabolically labeled for 30 min with 35 S under standard or reducing (5 mM DTT) conditions. HBV precore-derived proteins were immunoprecipitated from the harvested cells with anti-core antibody, separated by SDS-PAGE, and analyzed by autoradiography. ( C ) Electrophoretic mobility comparison of HBe and the HBe3CA mutant. The experiment was performed as for , (+) phosphorylation of HBe3CA p25 protein was demonstrated by λ-PP treatment. ( D ) Pulse-chase analysis of precore protein processing and secretion. Huh7 cells expressing HBe or HBe3CA proteins were metabolically labeled for 30 min with 35 S, and then chased for 0.5, 1, and 4 h. At all time points, both cells and media were harvested and subjected to immunoprecipitation with anti-core antibody. Proteins were separated by SDS-PAGE and analyzed by autoradiography. ( E ) Comparison of HBe secretion by cells infected with wild type and mutant precore rcccDNA. HepG2-NTCP cells in 12-well plates were infected in triplicate with wild type rcccDNA (wt rcccDNA) and mutant precore rcccDNA (HBe3CA rcccDNA) with equal MOI of 2000 VGE/cell. Secretion of HBe in the culture supernatants was determined by ELISA at days 0, 3, 6, and 14. Data are plotted as mean ± SEM of three biological replicates.
0.1 M Tris Hcl Buffer (Ph 8.5) Containing 2 Mm Dithiothreitol (Dtt), supplied by BioSpec, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 90 stars, based on 1 article reviews
0.1 m tris-hcl buffer (ph 8.5) containing 2 mm dithiothreitol (dtt) - by Bioz Stars, 2026-11
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Image Search Results


( A ) Huh7 cells expressing HBV precore precursor were metabolically labeled for 30 min with 35 S, lysed, and subjected to immunoprecipitation with anti-core antibody. Immunoprecipitated samples were untreated (−) or treated (+) with λ protein phosphatase and separated by SDS-PAGE. The electrophoretic mobility of precore related proteins was analyzed by autoradiography. The migration positions of the HBV precore forms p25 p , p25, and p22 are indicated. ( B ) Ratios of individual precore protein forms produced in the presence (+) or absence (−) of dithiothreitol (DTT). Huh7 cells expressing the precore precursor were metabolically labeled for 30 min with 35 S under standard or reducing (5 mM DTT) conditions. HBV precore-derived proteins were immunoprecipitated from the harvested cells with anti-core antibody, separated by SDS-PAGE, and analyzed by autoradiography. ( C ) Electrophoretic mobility comparison of HBe and the HBe3CA mutant. The experiment was performed as for , (+) phosphorylation of HBe3CA p25 protein was demonstrated by λ-PP treatment. ( D ) Pulse-chase analysis of precore protein processing and secretion. Huh7 cells expressing HBe or HBe3CA proteins were metabolically labeled for 30 min with 35 S, and then chased for 0.5, 1, and 4 h. At all time points, both cells and media were harvested and subjected to immunoprecipitation with anti-core antibody. Proteins were separated by SDS-PAGE and analyzed by autoradiography. ( E ) Comparison of HBe secretion by cells infected with wild type and mutant precore rcccDNA. HepG2-NTCP cells in 12-well plates were infected in triplicate with wild type rcccDNA (wt rcccDNA) and mutant precore rcccDNA (HBe3CA rcccDNA) with equal MOI of 2000 VGE/cell. Secretion of HBe in the culture supernatants was determined by ELISA at days 0, 3, 6, and 14. Data are plotted as mean ± SEM of three biological replicates.

Journal: bioRxiv

Article Title: Biogenesis of hepatitis B virus e antigen is driven by translocon-associated protein complex and regulated by conserved cysteines in signal peptide

doi: 10.1101/2021.06.17.448870

Figure Lengend Snippet: ( A ) Huh7 cells expressing HBV precore precursor were metabolically labeled for 30 min with 35 S, lysed, and subjected to immunoprecipitation with anti-core antibody. Immunoprecipitated samples were untreated (−) or treated (+) with λ protein phosphatase and separated by SDS-PAGE. The electrophoretic mobility of precore related proteins was analyzed by autoradiography. The migration positions of the HBV precore forms p25 p , p25, and p22 are indicated. ( B ) Ratios of individual precore protein forms produced in the presence (+) or absence (−) of dithiothreitol (DTT). Huh7 cells expressing the precore precursor were metabolically labeled for 30 min with 35 S under standard or reducing (5 mM DTT) conditions. HBV precore-derived proteins were immunoprecipitated from the harvested cells with anti-core antibody, separated by SDS-PAGE, and analyzed by autoradiography. ( C ) Electrophoretic mobility comparison of HBe and the HBe3CA mutant. The experiment was performed as for , (+) phosphorylation of HBe3CA p25 protein was demonstrated by λ-PP treatment. ( D ) Pulse-chase analysis of precore protein processing and secretion. Huh7 cells expressing HBe or HBe3CA proteins were metabolically labeled for 30 min with 35 S, and then chased for 0.5, 1, and 4 h. At all time points, both cells and media were harvested and subjected to immunoprecipitation with anti-core antibody. Proteins were separated by SDS-PAGE and analyzed by autoradiography. ( E ) Comparison of HBe secretion by cells infected with wild type and mutant precore rcccDNA. HepG2-NTCP cells in 12-well plates were infected in triplicate with wild type rcccDNA (wt rcccDNA) and mutant precore rcccDNA (HBe3CA rcccDNA) with equal MOI of 2000 VGE/cell. Secretion of HBe in the culture supernatants was determined by ELISA at days 0, 3, 6, and 14. Data are plotted as mean ± SEM of three biological replicates.

Article Snippet: Rabbit polyclonal anti-HBV core protein antiserum was obtained after immunization of three animals with 1.4 mg/ml purified denatured (boiling in 1% SDS, 0.1 M DTT) HBV core protein produced in E. coli (Moravian Biotech).

Techniques: Expressing, Metabolic Labelling, Labeling, Immunoprecipitation, SDS Page, Autoradiography, Migration, Produced, Derivative Assay, Mutagenesis, Pulse Chase, Infection, Enzyme-linked Immunosorbent Assay