bis tris sds page Search Results


tris  (Chem Impex International)
95
Chem Impex International tris
Tris, supplied by Chem Impex International, 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/result/tris/product/Chem Impex International
Average 95 stars, based on 1 article reviews
tris - by Bioz Stars, 2026-03
95/100 stars
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sds-page 4–20% bis-tris gels  (anamed Elektrophorese GmbH)
90
anamed Elektrophorese GmbH sds-page 4–20% bis-tris gels
Sds Page 4–20% Bis Tris Gels, supplied by anamed Elektrophorese GmbH, 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/sds-page 4–20% bis-tris gels/product/anamed Elektrophorese GmbH
Average 90 stars, based on 1 article reviews
sds-page 4–20% bis-tris gels - by Bioz Stars, 2026-03
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sds-page surepagetm, bis-tris  (GenScript corporation)
90
GenScript corporation sds-page surepagetm, bis-tris
Sds Page Surepagetm, Bis Tris, supplied by GenScript corporation, 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/sds-page surepagetm, bis-tris/product/GenScript corporation
Average 90 stars, based on 1 article reviews
sds-page surepagetm, bis-tris - by Bioz Stars, 2026-03
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4-12% bis-tris sds-page gel  (Sangon Biotech)
90
Sangon Biotech 4-12% bis-tris sds-page gel
4 12% Bis Tris Sds Page Gel, supplied by Sangon Biotech, 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/4-12% bis-tris sds-page gel/product/Sangon Biotech
Average 90 stars, based on 1 article reviews
4-12% bis-tris sds-page gel - by Bioz Stars, 2026-03
90/100 stars
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4–12 % bis tris nupage sds page  (Fisher Scientific)
90
Fisher Scientific 4–12 % bis tris nupage sds page
Antibodies of different clones, regardless of isotype, can fragment differently under the same conditions. (a) Reaction scheme for pepsin digestion. The pictured fragments are the most likely products for the bands observed at those molecular weights, for a canonical 150 kDa antibody. (b) Non-reducing <t>SDS</t> <t>PAGE</t> of antibodies digested at pH 4.4 with 125% Pepsin (%w/w) for 2h at 37°C. N=1 per condition and were ran in duplicate on gel (two lanes per condition). Lane contents are listed above each lane. Molecular weights (MW, kDa) of the ladder in Lane 1 are listed at the left. Note that for GK1.5, F(ab’)2 appears at a non-canonical weight of 80 kDa. (c) To quantify the fragmentation pattern, the relative mass % of all sample bands were quantified using a gel imager. (d) % yield, (e) digestion efficiency, and (f) the purity of F(ab’)2 produced the tested conditions.
4–12 % Bis Tris Nupage Sds Page, supplied by Fisher Scientific, 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/4–12 % bis tris nupage sds page/product/Fisher Scientific
Average 90 stars, based on 1 article reviews
4–12 % bis tris nupage sds page - by Bioz Stars, 2026-03
90/100 stars
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bis-tris sodium dodecyl sulfate-polyacrylamide electrophoresis gel sds-page  (Beyotime)
90
Beyotime bis-tris sodium dodecyl sulfate-polyacrylamide electrophoresis gel sds-page
Antibodies of different clones, regardless of isotype, can fragment differently under the same conditions. (a) Reaction scheme for pepsin digestion. The pictured fragments are the most likely products for the bands observed at those molecular weights, for a canonical 150 kDa antibody. (b) Non-reducing <t>SDS</t> <t>PAGE</t> of antibodies digested at pH 4.4 with 125% Pepsin (%w/w) for 2h at 37°C. N=1 per condition and were ran in duplicate on gel (two lanes per condition). Lane contents are listed above each lane. Molecular weights (MW, kDa) of the ladder in Lane 1 are listed at the left. Note that for GK1.5, F(ab’)2 appears at a non-canonical weight of 80 kDa. (c) To quantify the fragmentation pattern, the relative mass % of all sample bands were quantified using a gel imager. (d) % yield, (e) digestion efficiency, and (f) the purity of F(ab’)2 produced the tested conditions.
Bis Tris Sodium Dodecyl Sulfate Polyacrylamide Electrophoresis Gel Sds Page, supplied by Beyotime, 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/bis-tris sodium dodecyl sulfate-polyacrylamide electrophoresis gel sds-page/product/Beyotime
Average 90 stars, based on 1 article reviews
bis-tris sodium dodecyl sulfate-polyacrylamide electrophoresis gel sds-page - by Bioz Stars, 2026-03
90/100 stars
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bis-tris sds-page gels  (Beijing CWBio)
90
Beijing CWBio bis-tris sds-page gels
Antibodies of different clones, regardless of isotype, can fragment differently under the same conditions. (a) Reaction scheme for pepsin digestion. The pictured fragments are the most likely products for the bands observed at those molecular weights, for a canonical 150 kDa antibody. (b) Non-reducing <t>SDS</t> <t>PAGE</t> of antibodies digested at pH 4.4 with 125% Pepsin (%w/w) for 2h at 37°C. N=1 per condition and were ran in duplicate on gel (two lanes per condition). Lane contents are listed above each lane. Molecular weights (MW, kDa) of the ladder in Lane 1 are listed at the left. Note that for GK1.5, F(ab’)2 appears at a non-canonical weight of 80 kDa. (c) To quantify the fragmentation pattern, the relative mass % of all sample bands were quantified using a gel imager. (d) % yield, (e) digestion efficiency, and (f) the purity of F(ab’)2 produced the tested conditions.
Bis Tris Sds Page Gels, supplied by Beijing CWBio, 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/bis-tris sds-page gels/product/Beijing CWBio
Average 90 stars, based on 1 article reviews
bis-tris sds-page gels - by Bioz Stars, 2026-03
90/100 stars
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10% bis-tris sodium dodecyl sulfate-poly-acrylamide electrophoresis gel (sds-page)  (Beyotime)
90
Beyotime 10% bis-tris sodium dodecyl sulfate-poly-acrylamide electrophoresis gel (sds-page)
Antibodies of different clones, regardless of isotype, can fragment differently under the same conditions. (a) Reaction scheme for pepsin digestion. The pictured fragments are the most likely products for the bands observed at those molecular weights, for a canonical 150 kDa antibody. (b) Non-reducing <t>SDS</t> <t>PAGE</t> of antibodies digested at pH 4.4 with 125% Pepsin (%w/w) for 2h at 37°C. N=1 per condition and were ran in duplicate on gel (two lanes per condition). Lane contents are listed above each lane. Molecular weights (MW, kDa) of the ladder in Lane 1 are listed at the left. Note that for GK1.5, F(ab’)2 appears at a non-canonical weight of 80 kDa. (c) To quantify the fragmentation pattern, the relative mass % of all sample bands were quantified using a gel imager. (d) % yield, (e) digestion efficiency, and (f) the purity of F(ab’)2 produced the tested conditions.
10% Bis Tris Sodium Dodecyl Sulfate Poly Acrylamide Electrophoresis Gel (Sds Page), supplied by Beyotime, 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/10% bis-tris sodium dodecyl sulfate-poly-acrylamide electrophoresis gel (sds-page)/product/Beyotime
Average 90 stars, based on 1 article reviews
10% bis-tris sodium dodecyl sulfate-poly-acrylamide electrophoresis gel (sds-page) - by Bioz Stars, 2026-03
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4–20% gradient bis-tris sds-page  (Merck KGaA)
90
Merck KGaA 4–20% gradient bis-tris sds-page
Antibodies of different clones, regardless of isotype, can fragment differently under the same conditions. (a) Reaction scheme for pepsin digestion. The pictured fragments are the most likely products for the bands observed at those molecular weights, for a canonical 150 kDa antibody. (b) Non-reducing <t>SDS</t> <t>PAGE</t> of antibodies digested at pH 4.4 with 125% Pepsin (%w/w) for 2h at 37°C. N=1 per condition and were ran in duplicate on gel (two lanes per condition). Lane contents are listed above each lane. Molecular weights (MW, kDa) of the ladder in Lane 1 are listed at the left. Note that for GK1.5, F(ab’)2 appears at a non-canonical weight of 80 kDa. (c) To quantify the fragmentation pattern, the relative mass % of all sample bands were quantified using a gel imager. (d) % yield, (e) digestion efficiency, and (f) the purity of F(ab’)2 produced the tested conditions.
4–20% Gradient Bis Tris Sds Page, 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
https://www.bioz.com/result/4–20% gradient bis-tris sds-page/product/Merck KGaA
Average 90 stars, based on 1 article reviews
4–20% gradient bis-tris sds-page - by Bioz Stars, 2026-03
90/100 stars
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bis-tris 10% sds-page  (Beyotime)
90
Beyotime bis-tris 10% sds-page
Antibodies of different clones, regardless of isotype, can fragment differently under the same conditions. (a) Reaction scheme for pepsin digestion. The pictured fragments are the most likely products for the bands observed at those molecular weights, for a canonical 150 kDa antibody. (b) Non-reducing <t>SDS</t> <t>PAGE</t> of antibodies digested at pH 4.4 with 125% Pepsin (%w/w) for 2h at 37°C. N=1 per condition and were ran in duplicate on gel (two lanes per condition). Lane contents are listed above each lane. Molecular weights (MW, kDa) of the ladder in Lane 1 are listed at the left. Note that for GK1.5, F(ab’)2 appears at a non-canonical weight of 80 kDa. (c) To quantify the fragmentation pattern, the relative mass % of all sample bands were quantified using a gel imager. (d) % yield, (e) digestion efficiency, and (f) the purity of F(ab’)2 produced the tested conditions.
Bis Tris 10% Sds Page, supplied by Beyotime, 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/bis-tris 10% sds-page/product/Beyotime
Average 90 stars, based on 1 article reviews
bis-tris 10% sds-page - by Bioz Stars, 2026-03
90/100 stars
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4%–12% bis-tris sds-page gels  (LuBioScience GmbH)
90
LuBioScience GmbH 4%–12% bis-tris sds-page gels
Antibodies of different clones, regardless of isotype, can fragment differently under the same conditions. (a) Reaction scheme for pepsin digestion. The pictured fragments are the most likely products for the bands observed at those molecular weights, for a canonical 150 kDa antibody. (b) Non-reducing <t>SDS</t> <t>PAGE</t> of antibodies digested at pH 4.4 with 125% Pepsin (%w/w) for 2h at 37°C. N=1 per condition and were ran in duplicate on gel (two lanes per condition). Lane contents are listed above each lane. Molecular weights (MW, kDa) of the ladder in Lane 1 are listed at the left. Note that for GK1.5, F(ab’)2 appears at a non-canonical weight of 80 kDa. (c) To quantify the fragmentation pattern, the relative mass % of all sample bands were quantified using a gel imager. (d) % yield, (e) digestion efficiency, and (f) the purity of F(ab’)2 produced the tested conditions.
4%–12% Bis Tris Sds Page Gels, supplied by LuBioScience GmbH, 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/4%–12% bis-tris sds-page gels/product/LuBioScience GmbH
Average 90 stars, based on 1 article reviews
4%–12% bis-tris sds-page gels - by Bioz Stars, 2026-03
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4-12% bis-tris sds-page gels  (Amersham Life Sciences Inc)
90
Amersham Life Sciences Inc 4-12% bis-tris sds-page gels
Antibodies of different clones, regardless of isotype, can fragment differently under the same conditions. (a) Reaction scheme for pepsin digestion. The pictured fragments are the most likely products for the bands observed at those molecular weights, for a canonical 150 kDa antibody. (b) Non-reducing <t>SDS</t> <t>PAGE</t> of antibodies digested at pH 4.4 with 125% Pepsin (%w/w) for 2h at 37°C. N=1 per condition and were ran in duplicate on gel (two lanes per condition). Lane contents are listed above each lane. Molecular weights (MW, kDa) of the ladder in Lane 1 are listed at the left. Note that for GK1.5, F(ab’)2 appears at a non-canonical weight of 80 kDa. (c) To quantify the fragmentation pattern, the relative mass % of all sample bands were quantified using a gel imager. (d) % yield, (e) digestion efficiency, and (f) the purity of F(ab’)2 produced the tested conditions.
4 12% Bis Tris Sds Page Gels, supplied by Amersham Life Sciences 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/4-12% bis-tris sds-page gels/product/Amersham Life Sciences Inc
Average 90 stars, based on 1 article reviews
4-12% bis-tris sds-page gels - by Bioz Stars, 2026-03
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Image Search Results


Antibodies of different clones, regardless of isotype, can fragment differently under the same conditions. (a) Reaction scheme for pepsin digestion. The pictured fragments are the most likely products for the bands observed at those molecular weights, for a canonical 150 kDa antibody. (b) Non-reducing SDS PAGE of antibodies digested at pH 4.4 with 125% Pepsin (%w/w) for 2h at 37°C. N=1 per condition and were ran in duplicate on gel (two lanes per condition). Lane contents are listed above each lane. Molecular weights (MW, kDa) of the ladder in Lane 1 are listed at the left. Note that for GK1.5, F(ab’)2 appears at a non-canonical weight of 80 kDa. (c) To quantify the fragmentation pattern, the relative mass % of all sample bands were quantified using a gel imager. (d) % yield, (e) digestion efficiency, and (f) the purity of F(ab’)2 produced the tested conditions.

Journal: Bioconjugate chemistry

Article Title: Optimization of Enzymatic Antibody Fragmentation for Yield, Efficiency, and Binding Affinity

doi: 10.1021/acs.bioconjchem.8b00912

Figure Lengend Snippet: Antibodies of different clones, regardless of isotype, can fragment differently under the same conditions. (a) Reaction scheme for pepsin digestion. The pictured fragments are the most likely products for the bands observed at those molecular weights, for a canonical 150 kDa antibody. (b) Non-reducing SDS PAGE of antibodies digested at pH 4.4 with 125% Pepsin (%w/w) for 2h at 37°C. N=1 per condition and were ran in duplicate on gel (two lanes per condition). Lane contents are listed above each lane. Molecular weights (MW, kDa) of the ladder in Lane 1 are listed at the left. Note that for GK1.5, F(ab’)2 appears at a non-canonical weight of 80 kDa. (c) To quantify the fragmentation pattern, the relative mass % of all sample bands were quantified using a gel imager. (d) % yield, (e) digestion efficiency, and (f) the purity of F(ab’)2 produced the tested conditions.

Article Snippet: Antibody fragmentation samples were analyzed using 4–12 % Bis Tris NuPAGE SDS PAGE (Fisher Scientific) with MOPS buffer (Fisher Scientific).

Techniques: Clone Assay, SDS Page, Produced

A change in pH had the greatest effect on yield and efficiency of F(ab)2 production by pepsin. Rat IgG1 clone HRPN was fragmented under 23 = 8 conditions of pH, % pepsin (% w/w), and time. (a) % molar yield of F(ab’)2 produced in each condition. (b) The change in yield as a result of increasing pH, % pepsin, or time. (c) % efficiency of reaction in each condition. (b) The change in efficiency as a result of increase pH, % Pepsin, or time. N=1 for each reaction condition. Conditions were measured twice on SDS PAGE.

Journal: Bioconjugate chemistry

Article Title: Optimization of Enzymatic Antibody Fragmentation for Yield, Efficiency, and Binding Affinity

doi: 10.1021/acs.bioconjchem.8b00912

Figure Lengend Snippet: A change in pH had the greatest effect on yield and efficiency of F(ab)2 production by pepsin. Rat IgG1 clone HRPN was fragmented under 23 = 8 conditions of pH, % pepsin (% w/w), and time. (a) % molar yield of F(ab’)2 produced in each condition. (b) The change in yield as a result of increasing pH, % pepsin, or time. (c) % efficiency of reaction in each condition. (b) The change in efficiency as a result of increase pH, % Pepsin, or time. N=1 for each reaction condition. Conditions were measured twice on SDS PAGE.

Article Snippet: Antibody fragmentation samples were analyzed using 4–12 % Bis Tris NuPAGE SDS PAGE (Fisher Scientific) with MOPS buffer (Fisher Scientific).

Techniques: Produced, SDS Page

Case study 3: Yield and efficiency can vary with pH. Digestion of anti-IFN-γ clone: XMG1.2 at pH 2.8 and pH 4.4 has (a) % molar yield and (b) efficiency of F(ab’)2 produced (* aggregation/ unable to be quantified). (c) affinity ELISA of best condition (marked with blue square). IC50: F(ab’)2 - 0.25 nM; Whole - 20.4 nM. Digestion at pH 5.0 shows increased (d) yield and (e) efficiency of F(ab’)2 produced, and has maintained affinity as measured by (f) affinity ELISA (tested condition marked with red square). IC50: F(ab’)2 - 0.41 nM; Whole - 23.0 nM. N=1 per fragmentation condition and ran in duplicate on SDS PAGE. N=3 per indirect ELISA condition, data was fit with 4 parameter curve in GraphPad Prism.

Journal: Bioconjugate chemistry

Article Title: Optimization of Enzymatic Antibody Fragmentation for Yield, Efficiency, and Binding Affinity

doi: 10.1021/acs.bioconjchem.8b00912

Figure Lengend Snippet: Case study 3: Yield and efficiency can vary with pH. Digestion of anti-IFN-γ clone: XMG1.2 at pH 2.8 and pH 4.4 has (a) % molar yield and (b) efficiency of F(ab’)2 produced (* aggregation/ unable to be quantified). (c) affinity ELISA of best condition (marked with blue square). IC50: F(ab’)2 - 0.25 nM; Whole - 20.4 nM. Digestion at pH 5.0 shows increased (d) yield and (e) efficiency of F(ab’)2 produced, and has maintained affinity as measured by (f) affinity ELISA (tested condition marked with red square). IC50: F(ab’)2 - 0.41 nM; Whole - 23.0 nM. N=1 per fragmentation condition and ran in duplicate on SDS PAGE. N=3 per indirect ELISA condition, data was fit with 4 parameter curve in GraphPad Prism.

Article Snippet: Antibody fragmentation samples were analyzed using 4–12 % Bis Tris NuPAGE SDS PAGE (Fisher Scientific) with MOPS buffer (Fisher Scientific).

Techniques: Produced, Enzyme-linked Immunosorbent Assay, SDS Page, Indirect ELISA