lambda nuclease buffer Search Results


lambda phosphatase  (New England Biolabs)
99
New England Biolabs lambda phosphatase
(A) Illustration of wild-type precore protein (p25-WT) and mutant/HA-tagged p25 as well as its proteolytically processed products p22 and p17 that are expressed by pXF3H-derived plasmids (see for detailed description). Red arrow indicates the mutation of Cp starting codon (AUG) to AUA. The gray box indicates the insertion of HA tag at the immediate upstream of Cp starting codon. (B) HepG2 cells were transfected with pXF3H-p25-WT and derived plasmid expressing p25 with the indicated single amino acid substitution. The cells were harvested at 48 h post transfection. Intracellular p25-derived proteins were detected by Western blot assay with an antibody recognizing the last 14 amino acid residues at the C-terminus of precore protein and Cp (anti-HBc-170A). HBeAg in culture media was detected by CLIA and results (mean ± SD) from three independent experiments were analyzed by two-tailed Student’s t-test (unpaired), ***: P < 0.001. (C) HepG2 cells were transfected with a pXF3H-derived plasmid expressing the indicated p25 proteins or pCMV-HBc expressing Cp. Intracellular p25-derived proteins or Cp were detected by Western blot assay with an anti-HBc-170A as the primary antibody. The lysate from AML12HBVpolY63F cells was analyzed in parallel to serve as the control of hyper- and hypo-phosphorylated Cp. (D) HepG2 cells were transfected with pXF3H-p25HA, harvested at 48 h post transfection and lysed with <t>core</t> <t>DNA</t> lysis buffer. Aliquots of the cell lysate were mock-treated or treated with <t>Lambda</t> phosphatase at 30°C for 40 min. HBV p22 in the reactions were detected by Western blot assay with anti-HBc-170A. ( E ) HepG2 cells were transfected with a plasmid expressing the indicated precore protein and harvested at 48 h post transfection. The cells were lysed by 1× LDS lysis buffer (contained 2.5% B-ME) and the lysates were resolved by electrophoresis in NuPAGE 12% Bis-Tris Protein Gel (upper panel) and 12% phos-tag gel (lower panel). After blotting onto membranes, p22 were detected by anti-HBc-170A as primary antibody. β-actin served as a loading control.
Lambda Phosphatase, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 99 stars, based on 1 article reviews
lambda phosphatase - by Bioz Stars, 2026-03
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203te buffer  (Thermo Fisher)
99
Thermo Fisher 203te buffer
(A) Illustration of wild-type precore protein (p25-WT) and mutant/HA-tagged p25 as well as its proteolytically processed products p22 and p17 that are expressed by pXF3H-derived plasmids (see for detailed description). Red arrow indicates the mutation of Cp starting codon (AUG) to AUA. The gray box indicates the insertion of HA tag at the immediate upstream of Cp starting codon. (B) HepG2 cells were transfected with pXF3H-p25-WT and derived plasmid expressing p25 with the indicated single amino acid substitution. The cells were harvested at 48 h post transfection. Intracellular p25-derived proteins were detected by Western blot assay with an antibody recognizing the last 14 amino acid residues at the C-terminus of precore protein and Cp (anti-HBc-170A). HBeAg in culture media was detected by CLIA and results (mean ± SD) from three independent experiments were analyzed by two-tailed Student’s t-test (unpaired), ***: P < 0.001. (C) HepG2 cells were transfected with a pXF3H-derived plasmid expressing the indicated p25 proteins or pCMV-HBc expressing Cp. Intracellular p25-derived proteins or Cp were detected by Western blot assay with an anti-HBc-170A as the primary antibody. The lysate from AML12HBVpolY63F cells was analyzed in parallel to serve as the control of hyper- and hypo-phosphorylated Cp. (D) HepG2 cells were transfected with pXF3H-p25HA, harvested at 48 h post transfection and lysed with <t>core</t> <t>DNA</t> lysis buffer. Aliquots of the cell lysate were mock-treated or treated with <t>Lambda</t> phosphatase at 30°C for 40 min. HBV p22 in the reactions were detected by Western blot assay with anti-HBc-170A. ( E ) HepG2 cells were transfected with a plasmid expressing the indicated precore protein and harvested at 48 h post transfection. The cells were lysed by 1× LDS lysis buffer (contained 2.5% B-ME) and the lysates were resolved by electrophoresis in NuPAGE 12% Bis-Tris Protein Gel (upper panel) and 12% phos-tag gel (lower panel). After blotting onto membranes, p22 were detected by anti-HBc-170A as primary antibody. β-actin served as a loading control.
203te Buffer, supplied by Thermo Fisher, 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/result/203te buffer/product/Thermo Fisher
Average 99 stars, based on 1 article reviews
203te buffer - by Bioz Stars, 2026-03
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lambda protein phosphatase  (New England Biolabs)
96
New England Biolabs lambda protein phosphatase
(A) Illustration of wild-type precore protein (p25-WT) and mutant/HA-tagged p25 as well as its proteolytically processed products p22 and p17 that are expressed by pXF3H-derived plasmids (see for detailed description). Red arrow indicates the mutation of Cp starting codon (AUG) to AUA. The gray box indicates the insertion of HA tag at the immediate upstream of Cp starting codon. (B) HepG2 cells were transfected with pXF3H-p25-WT and derived plasmid expressing p25 with the indicated single amino acid substitution. The cells were harvested at 48 h post transfection. Intracellular p25-derived proteins were detected by Western blot assay with an antibody recognizing the last 14 amino acid residues at the C-terminus of precore protein and Cp (anti-HBc-170A). HBeAg in culture media was detected by CLIA and results (mean ± SD) from three independent experiments were analyzed by two-tailed Student’s t-test (unpaired), ***: P < 0.001. (C) HepG2 cells were transfected with a pXF3H-derived plasmid expressing the indicated p25 proteins or pCMV-HBc expressing Cp. Intracellular p25-derived proteins or Cp were detected by Western blot assay with an anti-HBc-170A as the primary antibody. The lysate from AML12HBVpolY63F cells was analyzed in parallel to serve as the control of hyper- and hypo-phosphorylated Cp. (D) HepG2 cells were transfected with pXF3H-p25HA, harvested at 48 h post transfection and lysed with <t>core</t> <t>DNA</t> lysis buffer. Aliquots of the cell lysate were mock-treated or treated with <t>Lambda</t> phosphatase at 30°C for 40 min. HBV p22 in the reactions were detected by Western blot assay with anti-HBc-170A. ( E ) HepG2 cells were transfected with a plasmid expressing the indicated precore protein and harvested at 48 h post transfection. The cells were lysed by 1× LDS lysis buffer (contained 2.5% B-ME) and the lysates were resolved by electrophoresis in NuPAGE 12% Bis-Tris Protein Gel (upper panel) and 12% phos-tag gel (lower panel). After blotting onto membranes, p22 were detected by anti-HBc-170A as primary antibody. β-actin served as a loading control.
Lambda Protein Phosphatase, supplied by New England Biolabs, 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/result/lambda protein phosphatase/product/New England Biolabs
Average 96 stars, based on 1 article reviews
lambda protein phosphatase - by Bioz Stars, 2026-03
96/100 stars
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lambda nuclease buffer  (New England Biolabs)
96
New England Biolabs lambda nuclease buffer
(A) Illustration of wild-type precore protein (p25-WT) and mutant/HA-tagged p25 as well as its proteolytically processed products p22 and p17 that are expressed by pXF3H-derived plasmids (see for detailed description). Red arrow indicates the mutation of Cp starting codon (AUG) to AUA. The gray box indicates the insertion of HA tag at the immediate upstream of Cp starting codon. (B) HepG2 cells were transfected with pXF3H-p25-WT and derived plasmid expressing p25 with the indicated single amino acid substitution. The cells were harvested at 48 h post transfection. Intracellular p25-derived proteins were detected by Western blot assay with an antibody recognizing the last 14 amino acid residues at the C-terminus of precore protein and Cp (anti-HBc-170A). HBeAg in culture media was detected by CLIA and results (mean ± SD) from three independent experiments were analyzed by two-tailed Student’s t-test (unpaired), ***: P < 0.001. (C) HepG2 cells were transfected with a pXF3H-derived plasmid expressing the indicated p25 proteins or pCMV-HBc expressing Cp. Intracellular p25-derived proteins or Cp were detected by Western blot assay with an anti-HBc-170A as the primary antibody. The lysate from AML12HBVpolY63F cells was analyzed in parallel to serve as the control of hyper- and hypo-phosphorylated Cp. (D) HepG2 cells were transfected with pXF3H-p25HA, harvested at 48 h post transfection and lysed with <t>core</t> <t>DNA</t> lysis buffer. Aliquots of the cell lysate were mock-treated or treated with <t>Lambda</t> phosphatase at 30°C for 40 min. HBV p22 in the reactions were detected by Western blot assay with anti-HBc-170A. ( E ) HepG2 cells were transfected with a plasmid expressing the indicated precore protein and harvested at 48 h post transfection. The cells were lysed by 1× LDS lysis buffer (contained 2.5% B-ME) and the lysates were resolved by electrophoresis in NuPAGE 12% Bis-Tris Protein Gel (upper panel) and 12% phos-tag gel (lower panel). After blotting onto membranes, p22 were detected by anti-HBc-170A as primary antibody. β-actin served as a loading control.
Lambda Nuclease Buffer, supplied by New England Biolabs, 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/result/lambda nuclease buffer/product/New England Biolabs
Average 96 stars, based on 1 article reviews
lambda nuclease buffer - by Bioz Stars, 2026-03
96/100 stars
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b1500s bis tris buffer 1m  (New England Biolabs)
99
New England Biolabs b1500s bis tris buffer 1m
(A) Illustration of wild-type precore protein (p25-WT) and mutant/HA-tagged p25 as well as its proteolytically processed products p22 and p17 that are expressed by pXF3H-derived plasmids (see for detailed description). Red arrow indicates the mutation of Cp starting codon (AUG) to AUA. The gray box indicates the insertion of HA tag at the immediate upstream of Cp starting codon. (B) HepG2 cells were transfected with pXF3H-p25-WT and derived plasmid expressing p25 with the indicated single amino acid substitution. The cells were harvested at 48 h post transfection. Intracellular p25-derived proteins were detected by Western blot assay with an antibody recognizing the last 14 amino acid residues at the C-terminus of precore protein and Cp (anti-HBc-170A). HBeAg in culture media was detected by CLIA and results (mean ± SD) from three independent experiments were analyzed by two-tailed Student’s t-test (unpaired), ***: P < 0.001. (C) HepG2 cells were transfected with a pXF3H-derived plasmid expressing the indicated p25 proteins or pCMV-HBc expressing Cp. Intracellular p25-derived proteins or Cp were detected by Western blot assay with an anti-HBc-170A as the primary antibody. The lysate from AML12HBVpolY63F cells was analyzed in parallel to serve as the control of hyper- and hypo-phosphorylated Cp. (D) HepG2 cells were transfected with pXF3H-p25HA, harvested at 48 h post transfection and lysed with <t>core</t> <t>DNA</t> lysis buffer. Aliquots of the cell lysate were mock-treated or treated with <t>Lambda</t> phosphatase at 30°C for 40 min. HBV p22 in the reactions were detected by Western blot assay with anti-HBc-170A. ( E ) HepG2 cells were transfected with a plasmid expressing the indicated precore protein and harvested at 48 h post transfection. The cells were lysed by 1× LDS lysis buffer (contained 2.5% B-ME) and the lysates were resolved by electrophoresis in NuPAGE 12% Bis-Tris Protein Gel (upper panel) and 12% phos-tag gel (lower panel). After blotting onto membranes, p22 were detected by anti-HBc-170A as primary antibody. β-actin served as a loading control.
B1500s Bis Tris Buffer 1m, supplied by New England Biolabs, 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/result/b1500s bis tris buffer 1m/product/New England Biolabs
Average 99 stars, based on 1 article reviews
b1500s bis tris buffer 1m - by Bioz Stars, 2026-03
99/100 stars
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nuclease buffer  (New England Biolabs)
96
New England Biolabs nuclease buffer
(A) Illustration of wild-type precore protein (p25-WT) and mutant/HA-tagged p25 as well as its proteolytically processed products p22 and p17 that are expressed by pXF3H-derived plasmids (see for detailed description). Red arrow indicates the mutation of Cp starting codon (AUG) to AUA. The gray box indicates the insertion of HA tag at the immediate upstream of Cp starting codon. (B) HepG2 cells were transfected with pXF3H-p25-WT and derived plasmid expressing p25 with the indicated single amino acid substitution. The cells were harvested at 48 h post transfection. Intracellular p25-derived proteins were detected by Western blot assay with an antibody recognizing the last 14 amino acid residues at the C-terminus of precore protein and Cp (anti-HBc-170A). HBeAg in culture media was detected by CLIA and results (mean ± SD) from three independent experiments were analyzed by two-tailed Student’s t-test (unpaired), ***: P < 0.001. (C) HepG2 cells were transfected with a pXF3H-derived plasmid expressing the indicated p25 proteins or pCMV-HBc expressing Cp. Intracellular p25-derived proteins or Cp were detected by Western blot assay with an anti-HBc-170A as the primary antibody. The lysate from AML12HBVpolY63F cells was analyzed in parallel to serve as the control of hyper- and hypo-phosphorylated Cp. (D) HepG2 cells were transfected with pXF3H-p25HA, harvested at 48 h post transfection and lysed with <t>core</t> <t>DNA</t> lysis buffer. Aliquots of the cell lysate were mock-treated or treated with <t>Lambda</t> phosphatase at 30°C for 40 min. HBV p22 in the reactions were detected by Western blot assay with anti-HBc-170A. ( E ) HepG2 cells were transfected with a plasmid expressing the indicated precore protein and harvested at 48 h post transfection. The cells were lysed by 1× LDS lysis buffer (contained 2.5% B-ME) and the lysates were resolved by electrophoresis in NuPAGE 12% Bis-Tris Protein Gel (upper panel) and 12% phos-tag gel (lower panel). After blotting onto membranes, p22 were detected by anti-HBc-170A as primary antibody. β-actin served as a loading control.
Nuclease Buffer, supplied by New England Biolabs, 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/result/nuclease buffer/product/New England Biolabs
Average 96 stars, based on 1 article reviews
nuclease buffer - by Bioz Stars, 2026-03
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rnase  (Thermo Fisher)
99
Thermo Fisher rnase
(A) Illustration of wild-type precore protein (p25-WT) and mutant/HA-tagged p25 as well as its proteolytically processed products p22 and p17 that are expressed by pXF3H-derived plasmids (see for detailed description). Red arrow indicates the mutation of Cp starting codon (AUG) to AUA. The gray box indicates the insertion of HA tag at the immediate upstream of Cp starting codon. (B) HepG2 cells were transfected with pXF3H-p25-WT and derived plasmid expressing p25 with the indicated single amino acid substitution. The cells were harvested at 48 h post transfection. Intracellular p25-derived proteins were detected by Western blot assay with an antibody recognizing the last 14 amino acid residues at the C-terminus of precore protein and Cp (anti-HBc-170A). HBeAg in culture media was detected by CLIA and results (mean ± SD) from three independent experiments were analyzed by two-tailed Student’s t-test (unpaired), ***: P < 0.001. (C) HepG2 cells were transfected with a pXF3H-derived plasmid expressing the indicated p25 proteins or pCMV-HBc expressing Cp. Intracellular p25-derived proteins or Cp were detected by Western blot assay with an anti-HBc-170A as the primary antibody. The lysate from AML12HBVpolY63F cells was analyzed in parallel to serve as the control of hyper- and hypo-phosphorylated Cp. (D) HepG2 cells were transfected with pXF3H-p25HA, harvested at 48 h post transfection and lysed with <t>core</t> <t>DNA</t> lysis buffer. Aliquots of the cell lysate were mock-treated or treated with <t>Lambda</t> phosphatase at 30°C for 40 min. HBV p22 in the reactions were detected by Western blot assay with anti-HBc-170A. ( E ) HepG2 cells were transfected with a plasmid expressing the indicated precore protein and harvested at 48 h post transfection. The cells were lysed by 1× LDS lysis buffer (contained 2.5% B-ME) and the lysates were resolved by electrophoresis in NuPAGE 12% Bis-Tris Protein Gel (upper panel) and 12% phos-tag gel (lower panel). After blotting onto membranes, p22 were detected by anti-HBc-170A as primary antibody. β-actin served as a loading control.
Rnase, supplied by Thermo Fisher, 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/result/rnase/product/Thermo Fisher
Average 99 stars, based on 1 article reviews
rnase - by Bioz Stars, 2026-03
99/100 stars
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Image Search Results


(A) Illustration of wild-type precore protein (p25-WT) and mutant/HA-tagged p25 as well as its proteolytically processed products p22 and p17 that are expressed by pXF3H-derived plasmids (see for detailed description). Red arrow indicates the mutation of Cp starting codon (AUG) to AUA. The gray box indicates the insertion of HA tag at the immediate upstream of Cp starting codon. (B) HepG2 cells were transfected with pXF3H-p25-WT and derived plasmid expressing p25 with the indicated single amino acid substitution. The cells were harvested at 48 h post transfection. Intracellular p25-derived proteins were detected by Western blot assay with an antibody recognizing the last 14 amino acid residues at the C-terminus of precore protein and Cp (anti-HBc-170A). HBeAg in culture media was detected by CLIA and results (mean ± SD) from three independent experiments were analyzed by two-tailed Student’s t-test (unpaired), ***: P < 0.001. (C) HepG2 cells were transfected with a pXF3H-derived plasmid expressing the indicated p25 proteins or pCMV-HBc expressing Cp. Intracellular p25-derived proteins or Cp were detected by Western blot assay with an anti-HBc-170A as the primary antibody. The lysate from AML12HBVpolY63F cells was analyzed in parallel to serve as the control of hyper- and hypo-phosphorylated Cp. (D) HepG2 cells were transfected with pXF3H-p25HA, harvested at 48 h post transfection and lysed with core DNA lysis buffer. Aliquots of the cell lysate were mock-treated or treated with Lambda phosphatase at 30°C for 40 min. HBV p22 in the reactions were detected by Western blot assay with anti-HBc-170A. ( E ) HepG2 cells were transfected with a plasmid expressing the indicated precore protein and harvested at 48 h post transfection. The cells were lysed by 1× LDS lysis buffer (contained 2.5% B-ME) and the lysates were resolved by electrophoresis in NuPAGE 12% Bis-Tris Protein Gel (upper panel) and 12% phos-tag gel (lower panel). After blotting onto membranes, p22 were detected by anti-HBc-170A as primary antibody. β-actin served as a loading control.

Journal: PLoS Pathogens

Article Title: Amino acid residues at core protein dimer-dimer interface modulate multiple steps of hepatitis B virus replication and HBeAg biogenesis

doi: 10.1371/journal.ppat.1010057

Figure Lengend Snippet: (A) Illustration of wild-type precore protein (p25-WT) and mutant/HA-tagged p25 as well as its proteolytically processed products p22 and p17 that are expressed by pXF3H-derived plasmids (see for detailed description). Red arrow indicates the mutation of Cp starting codon (AUG) to AUA. The gray box indicates the insertion of HA tag at the immediate upstream of Cp starting codon. (B) HepG2 cells were transfected with pXF3H-p25-WT and derived plasmid expressing p25 with the indicated single amino acid substitution. The cells were harvested at 48 h post transfection. Intracellular p25-derived proteins were detected by Western blot assay with an antibody recognizing the last 14 amino acid residues at the C-terminus of precore protein and Cp (anti-HBc-170A). HBeAg in culture media was detected by CLIA and results (mean ± SD) from three independent experiments were analyzed by two-tailed Student’s t-test (unpaired), ***: P < 0.001. (C) HepG2 cells were transfected with a pXF3H-derived plasmid expressing the indicated p25 proteins or pCMV-HBc expressing Cp. Intracellular p25-derived proteins or Cp were detected by Western blot assay with an anti-HBc-170A as the primary antibody. The lysate from AML12HBVpolY63F cells was analyzed in parallel to serve as the control of hyper- and hypo-phosphorylated Cp. (D) HepG2 cells were transfected with pXF3H-p25HA, harvested at 48 h post transfection and lysed with core DNA lysis buffer. Aliquots of the cell lysate were mock-treated or treated with Lambda phosphatase at 30°C for 40 min. HBV p22 in the reactions were detected by Western blot assay with anti-HBc-170A. ( E ) HepG2 cells were transfected with a plasmid expressing the indicated precore protein and harvested at 48 h post transfection. The cells were lysed by 1× LDS lysis buffer (contained 2.5% B-ME) and the lysates were resolved by electrophoresis in NuPAGE 12% Bis-Tris Protein Gel (upper panel) and 12% phos-tag gel (lower panel). After blotting onto membranes, p22 were detected by anti-HBc-170A as primary antibody. β-actin served as a loading control.

Article Snippet: HepG2 cells transfected with desired plasmids were lysed by core DNA lysis buffer, 40 μl lysed samples were incubated with 1μl Lambda phosphatase (NEB, MA, USA), 5 μl 10 ×NEB buffer 3.1 and 4 μl nuclease-free water for 40 min at 30°C.

Techniques: Mutagenesis, Derivative Assay, Transfection, Plasmid Preparation, Expressing, Western Blot, Two Tailed Test, Lysis, Electrophoresis