polyacrylamide gradient gels Search Results


4%–20% gradient gels  (TEFCO Inc)
90
TEFCO Inc 4%–20% gradient gels
4%–20% Gradient Gels, supplied by TEFCO Inc, 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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4%–20% gradient gels - by Bioz Stars, 2026-09
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pre-cast gradient 4–20% tris-glycine gels  (anamed Elektrophorese GmbH)
90
anamed Elektrophorese GmbH pre-cast gradient 4–20% tris-glycine gels
Pre Cast Gradient 4–20% Tris Glycine 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
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pre-cast gradient 4–20% tris-glycine gels - by Bioz Stars, 2026-09
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polyacrylamide gradient gels  (Gradipore Inc)
90
Gradipore Inc polyacrylamide gradient gels
Polyacrylamide Gradient Gels, supplied by Gradipore 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/polyacrylamide+gradient+gels/nondenaturing+gradient+polyacrylamide+gels/10__1016_slash_s0021___9258_ascii40_17_ascii41_37724___4-60-3-7
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polyacrylamide gradient gels - by Bioz Stars, 2026-09
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sodium dodecyl sulphate-polyacrylamide gel electrophoresis gradient gels  (FUJIFILM)
90
FUJIFILM sodium dodecyl sulphate-polyacrylamide gel electrophoresis gradient gels
( a ) Intersubunit interaction around Arg243. Hydrogen bond and CH/ π stacking are indicated by dashed magenta and orange lines, respectively. ( b ) The ion bridge interaction of Lys249. Dashed cyan line represents ion bridges. ( c , d ) Mutational effect of the residues that participated in the interaction of Arg243 ( c ) and Lys249 ( d ) for the inactivation time constants. The inactivation time constants were measured from the current traces elicited by step pulses from holding potential at −140 mV. The time constant of NavSulP wild type (closed circle, n =8), R243E (open circle, n =4), Y242A (closed triangle, n =6), Y242F (open triangle, n =5), T239V (closed square, n =5) and R243A (open square, n =4) are represented in ( c ). The time constant of NavSulP wild type (closed circle, n =8), K249E (open circle, n =5), E251K (closed triangle, n =4), E254K (open triangle, n =4) and E251K/E254K (open square, n =4), are represented in ( d ). All values are presented as mean±standard error. ( e ) <t>Sodium</t> <t>dodecyl</t> <t>sulphate-polyacrylamide</t> <t>gel</t> <t>electrophoresis</t> analysis of tetramer and monomer fractions of NavSulP wild-type (WT) and mutants in size-exclusion chromatography. T and M indicate the tetramer and monomer fractions of NavSulP proteins in size-exclusion chromatography, respectively. To evaluate the amount of protein, proteins were denatured to monomers by sodium dodecyl sulphate treatment. The band intensities of the T and M lanes represent the amount of tetrameric channels and dissociated monomers, respectively. Most NavSulPΔC239 were dissociated to monomers and unable to form channel tetramers.
Sodium Dodecyl Sulphate Polyacrylamide Gel Electrophoresis Gradient Gels, supplied by FUJIFILM, 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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sodium dodecyl sulphate-polyacrylamide gel electrophoresis gradient gels - by Bioz Stars, 2026-09
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nondenaturing polyacrylamide 2–16% gradient slab gels  (Alamo Gels Inc)
90
Alamo Gels Inc nondenaturing polyacrylamide 2–16% gradient slab gels
( a ) Intersubunit interaction around Arg243. Hydrogen bond and CH/ π stacking are indicated by dashed magenta and orange lines, respectively. ( b ) The ion bridge interaction of Lys249. Dashed cyan line represents ion bridges. ( c , d ) Mutational effect of the residues that participated in the interaction of Arg243 ( c ) and Lys249 ( d ) for the inactivation time constants. The inactivation time constants were measured from the current traces elicited by step pulses from holding potential at −140 mV. The time constant of NavSulP wild type (closed circle, n =8), R243E (open circle, n =4), Y242A (closed triangle, n =6), Y242F (open triangle, n =5), T239V (closed square, n =5) and R243A (open square, n =4) are represented in ( c ). The time constant of NavSulP wild type (closed circle, n =8), K249E (open circle, n =5), E251K (closed triangle, n =4), E254K (open triangle, n =4) and E251K/E254K (open square, n =4), are represented in ( d ). All values are presented as mean±standard error. ( e ) <t>Sodium</t> <t>dodecyl</t> <t>sulphate-polyacrylamide</t> <t>gel</t> <t>electrophoresis</t> analysis of tetramer and monomer fractions of NavSulP wild-type (WT) and mutants in size-exclusion chromatography. T and M indicate the tetramer and monomer fractions of NavSulP proteins in size-exclusion chromatography, respectively. To evaluate the amount of protein, proteins were denatured to monomers by sodium dodecyl sulphate treatment. The band intensities of the T and M lanes represent the amount of tetrameric channels and dissociated monomers, respectively. Most NavSulPΔC239 were dissociated to monomers and unable to form channel tetramers.
Nondenaturing Polyacrylamide 2–16% Gradient Slab Gels, supplied by Alamo Gels Inc, 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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excelgel (12 to 14% gradient) sodium dodecyl sulfate (sds)-polyacrylamide gels  (Pharmacia LKB Biotechnology Inc)
90
Pharmacia LKB Biotechnology Inc excelgel (12 to 14% gradient) sodium dodecyl sulfate (sds)-polyacrylamide gels
( a ) Intersubunit interaction around Arg243. Hydrogen bond and CH/ π stacking are indicated by dashed magenta and orange lines, respectively. ( b ) The ion bridge interaction of Lys249. Dashed cyan line represents ion bridges. ( c , d ) Mutational effect of the residues that participated in the interaction of Arg243 ( c ) and Lys249 ( d ) for the inactivation time constants. The inactivation time constants were measured from the current traces elicited by step pulses from holding potential at −140 mV. The time constant of NavSulP wild type (closed circle, n =8), R243E (open circle, n =4), Y242A (closed triangle, n =6), Y242F (open triangle, n =5), T239V (closed square, n =5) and R243A (open square, n =4) are represented in ( c ). The time constant of NavSulP wild type (closed circle, n =8), K249E (open circle, n =5), E251K (closed triangle, n =4), E254K (open triangle, n =4) and E251K/E254K (open square, n =4), are represented in ( d ). All values are presented as mean±standard error. ( e ) <t>Sodium</t> <t>dodecyl</t> <t>sulphate-polyacrylamide</t> <t>gel</t> <t>electrophoresis</t> analysis of tetramer and monomer fractions of NavSulP wild-type (WT) and mutants in size-exclusion chromatography. T and M indicate the tetramer and monomer fractions of NavSulP proteins in size-exclusion chromatography, respectively. To evaluate the amount of protein, proteins were denatured to monomers by sodium dodecyl sulphate treatment. The band intensities of the T and M lanes represent the amount of tetrameric channels and dissociated monomers, respectively. Most NavSulPΔC239 were dissociated to monomers and unable to form channel tetramers.
Excelgel (12 To 14% Gradient) Sodium Dodecyl Sulfate (Sds) Polyacrylamide Gels, supplied by Pharmacia LKB Biotechnology Inc, 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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sds-polyacrylamide gels 4-20% gradient  (Promega)
90
Promega sds-polyacrylamide gels 4-20% gradient
( a ) Intersubunit interaction around Arg243. Hydrogen bond and CH/ π stacking are indicated by dashed magenta and orange lines, respectively. ( b ) The ion bridge interaction of Lys249. Dashed cyan line represents ion bridges. ( c , d ) Mutational effect of the residues that participated in the interaction of Arg243 ( c ) and Lys249 ( d ) for the inactivation time constants. The inactivation time constants were measured from the current traces elicited by step pulses from holding potential at −140 mV. The time constant of NavSulP wild type (closed circle, n =8), R243E (open circle, n =4), Y242A (closed triangle, n =6), Y242F (open triangle, n =5), T239V (closed square, n =5) and R243A (open square, n =4) are represented in ( c ). The time constant of NavSulP wild type (closed circle, n =8), K249E (open circle, n =5), E251K (closed triangle, n =4), E254K (open triangle, n =4) and E251K/E254K (open square, n =4), are represented in ( d ). All values are presented as mean±standard error. ( e ) <t>Sodium</t> <t>dodecyl</t> <t>sulphate-polyacrylamide</t> <t>gel</t> <t>electrophoresis</t> analysis of tetramer and monomer fractions of NavSulP wild-type (WT) and mutants in size-exclusion chromatography. T and M indicate the tetramer and monomer fractions of NavSulP proteins in size-exclusion chromatography, respectively. To evaluate the amount of protein, proteins were denatured to monomers by sodium dodecyl sulphate treatment. The band intensities of the T and M lanes represent the amount of tetrameric channels and dissociated monomers, respectively. Most NavSulPΔC239 were dissociated to monomers and unable to form channel tetramers.
Sds Polyacrylamide Gels 4 20% Gradient, 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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sds-polyacrylamide gels 4-20% gradient - by Bioz Stars, 2026-09
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gradient gels polyacrylamid (pa) provided by carl  (Carl Roth GmbH)
90
Carl Roth GmbH gradient gels polyacrylamid (pa) provided by carl
( a ) Intersubunit interaction around Arg243. Hydrogen bond and CH/ π stacking are indicated by dashed magenta and orange lines, respectively. ( b ) The ion bridge interaction of Lys249. Dashed cyan line represents ion bridges. ( c , d ) Mutational effect of the residues that participated in the interaction of Arg243 ( c ) and Lys249 ( d ) for the inactivation time constants. The inactivation time constants were measured from the current traces elicited by step pulses from holding potential at −140 mV. The time constant of NavSulP wild type (closed circle, n =8), R243E (open circle, n =4), Y242A (closed triangle, n =6), Y242F (open triangle, n =5), T239V (closed square, n =5) and R243A (open square, n =4) are represented in ( c ). The time constant of NavSulP wild type (closed circle, n =8), K249E (open circle, n =5), E251K (closed triangle, n =4), E254K (open triangle, n =4) and E251K/E254K (open square, n =4), are represented in ( d ). All values are presented as mean±standard error. ( e ) <t>Sodium</t> <t>dodecyl</t> <t>sulphate-polyacrylamide</t> <t>gel</t> <t>electrophoresis</t> analysis of tetramer and monomer fractions of NavSulP wild-type (WT) and mutants in size-exclusion chromatography. T and M indicate the tetramer and monomer fractions of NavSulP proteins in size-exclusion chromatography, respectively. To evaluate the amount of protein, proteins were denatured to monomers by sodium dodecyl sulphate treatment. The band intensities of the T and M lanes represent the amount of tetrameric channels and dissociated monomers, respectively. Most NavSulPΔC239 were dissociated to monomers and unable to form channel tetramers.
Gradient Gels Polyacrylamid (Pa) Provided By Carl, supplied by Carl Roth 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/product/polyacrylamide+gradient+gels/gradient+gels+polyacrylamid++pa++provided+by+carl/pm36302750-68-3-17
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gradient gels polyacrylamid (pa) provided by carl - by Bioz Stars, 2026-09
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pagel c520l  (ATTO Corp)
90
ATTO Corp pagel c520l
( a ) Intersubunit interaction around Arg243. Hydrogen bond and CH/ π stacking are indicated by dashed magenta and orange lines, respectively. ( b ) The ion bridge interaction of Lys249. Dashed cyan line represents ion bridges. ( c , d ) Mutational effect of the residues that participated in the interaction of Arg243 ( c ) and Lys249 ( d ) for the inactivation time constants. The inactivation time constants were measured from the current traces elicited by step pulses from holding potential at −140 mV. The time constant of NavSulP wild type (closed circle, n =8), R243E (open circle, n =4), Y242A (closed triangle, n =6), Y242F (open triangle, n =5), T239V (closed square, n =5) and R243A (open square, n =4) are represented in ( c ). The time constant of NavSulP wild type (closed circle, n =8), K249E (open circle, n =5), E251K (closed triangle, n =4), E254K (open triangle, n =4) and E251K/E254K (open square, n =4), are represented in ( d ). All values are presented as mean±standard error. ( e ) <t>Sodium</t> <t>dodecyl</t> <t>sulphate-polyacrylamide</t> <t>gel</t> <t>electrophoresis</t> analysis of tetramer and monomer fractions of NavSulP wild-type (WT) and mutants in size-exclusion chromatography. T and M indicate the tetramer and monomer fractions of NavSulP proteins in size-exclusion chromatography, respectively. To evaluate the amount of protein, proteins were denatured to monomers by sodium dodecyl sulphate treatment. The band intensities of the T and M lanes represent the amount of tetrameric channels and dissociated monomers, respectively. Most NavSulPΔC239 were dissociated to monomers and unable to form channel tetramers.
Pagel C520l, supplied by ATTO Corp, 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/polyacrylamide+gradient+gels/5+20++gradient+polyacrylamide+gels+c520l/us11236342-399-25-27
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pagel c520l - by Bioz Stars, 2026-09
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polyacrylamide gradient gel  (Alamo Gels Inc)
90
Alamo Gels Inc polyacrylamide gradient gel
( a ) Intersubunit interaction around Arg243. Hydrogen bond and CH/ π stacking are indicated by dashed magenta and orange lines, respectively. ( b ) The ion bridge interaction of Lys249. Dashed cyan line represents ion bridges. ( c , d ) Mutational effect of the residues that participated in the interaction of Arg243 ( c ) and Lys249 ( d ) for the inactivation time constants. The inactivation time constants were measured from the current traces elicited by step pulses from holding potential at −140 mV. The time constant of NavSulP wild type (closed circle, n =8), R243E (open circle, n =4), Y242A (closed triangle, n =6), Y242F (open triangle, n =5), T239V (closed square, n =5) and R243A (open square, n =4) are represented in ( c ). The time constant of NavSulP wild type (closed circle, n =8), K249E (open circle, n =5), E251K (closed triangle, n =4), E254K (open triangle, n =4) and E251K/E254K (open square, n =4), are represented in ( d ). All values are presented as mean±standard error. ( e ) <t>Sodium</t> <t>dodecyl</t> <t>sulphate-polyacrylamide</t> <t>gel</t> <t>electrophoresis</t> analysis of tetramer and monomer fractions of NavSulP wild-type (WT) and mutants in size-exclusion chromatography. T and M indicate the tetramer and monomer fractions of NavSulP proteins in size-exclusion chromatography, respectively. To evaluate the amount of protein, proteins were denatured to monomers by sodium dodecyl sulphate treatment. The band intensities of the T and M lanes represent the amount of tetrameric channels and dissociated monomers, respectively. Most NavSulPΔC239 were dissociated to monomers and unable to form channel tetramers.
Polyacrylamide Gradient Gel, supplied by Alamo Gels 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/polyacrylamide+gradient+gels/2++to+16++polyacrylamide+gradient+gels/10__1016_slash_s0022___2275_ascii40_20_ascii41_33373___3-116-13-16
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polyacrylamide gradient gel - by Bioz Stars, 2026-09
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10% polyacrylamide/bis (37.5 : 1) gels with denaturing gradients from 30– 60  (Severn Biotech Limited)
90
Severn Biotech Limited 10% polyacrylamide/bis (37.5 : 1) gels with denaturing gradients from 30– 60
( a ) Intersubunit interaction around Arg243. Hydrogen bond and CH/ π stacking are indicated by dashed magenta and orange lines, respectively. ( b ) The ion bridge interaction of Lys249. Dashed cyan line represents ion bridges. ( c , d ) Mutational effect of the residues that participated in the interaction of Arg243 ( c ) and Lys249 ( d ) for the inactivation time constants. The inactivation time constants were measured from the current traces elicited by step pulses from holding potential at −140 mV. The time constant of NavSulP wild type (closed circle, n =8), R243E (open circle, n =4), Y242A (closed triangle, n =6), Y242F (open triangle, n =5), T239V (closed square, n =5) and R243A (open square, n =4) are represented in ( c ). The time constant of NavSulP wild type (closed circle, n =8), K249E (open circle, n =5), E251K (closed triangle, n =4), E254K (open triangle, n =4) and E251K/E254K (open square, n =4), are represented in ( d ). All values are presented as mean±standard error. ( e ) <t>Sodium</t> <t>dodecyl</t> <t>sulphate-polyacrylamide</t> <t>gel</t> <t>electrophoresis</t> analysis of tetramer and monomer fractions of NavSulP wild-type (WT) and mutants in size-exclusion chromatography. T and M indicate the tetramer and monomer fractions of NavSulP proteins in size-exclusion chromatography, respectively. To evaluate the amount of protein, proteins were denatured to monomers by sodium dodecyl sulphate treatment. The band intensities of the T and M lanes represent the amount of tetrameric channels and dissociated monomers, respectively. Most NavSulPΔC239 were dissociated to monomers and unable to form channel tetramers.
10% Polyacrylamide/Bis (37.5 : 1) Gels With Denaturing Gradients From 30– 60, supplied by Severn Biotech Limited, 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/polyacrylamide+gradient+gels/10++polyacrylamide+bis++37+5+++1++gels+with+denaturing+gradients+from+30++60/pm16014426-43-7-33
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10% polyacrylamide/bis (37.5 : 1) gels with denaturing gradients from 30– 60 - by Bioz Stars, 2026-09
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nondenaturing polyacrylamide gradient gels  (Alamo Gels Inc)
90
Alamo Gels Inc nondenaturing polyacrylamide gradient gels
( a ) Intersubunit interaction around Arg243. Hydrogen bond and CH/ π stacking are indicated by dashed magenta and orange lines, respectively. ( b ) The ion bridge interaction of Lys249. Dashed cyan line represents ion bridges. ( c , d ) Mutational effect of the residues that participated in the interaction of Arg243 ( c ) and Lys249 ( d ) for the inactivation time constants. The inactivation time constants were measured from the current traces elicited by step pulses from holding potential at −140 mV. The time constant of NavSulP wild type (closed circle, n =8), R243E (open circle, n =4), Y242A (closed triangle, n =6), Y242F (open triangle, n =5), T239V (closed square, n =5) and R243A (open square, n =4) are represented in ( c ). The time constant of NavSulP wild type (closed circle, n =8), K249E (open circle, n =5), E251K (closed triangle, n =4), E254K (open triangle, n =4) and E251K/E254K (open square, n =4), are represented in ( d ). All values are presented as mean±standard error. ( e ) <t>Sodium</t> <t>dodecyl</t> <t>sulphate-polyacrylamide</t> <t>gel</t> <t>electrophoresis</t> analysis of tetramer and monomer fractions of NavSulP wild-type (WT) and mutants in size-exclusion chromatography. T and M indicate the tetramer and monomer fractions of NavSulP proteins in size-exclusion chromatography, respectively. To evaluate the amount of protein, proteins were denatured to monomers by sodium dodecyl sulphate treatment. The band intensities of the T and M lanes represent the amount of tetrameric channels and dissociated monomers, respectively. Most NavSulPΔC239 were dissociated to monomers and unable to form channel tetramers.
Nondenaturing Polyacrylamide Gradient Gels, supplied by Alamo Gels Inc, 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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Image Search Results


( a ) Intersubunit interaction around Arg243. Hydrogen bond and CH/ π stacking are indicated by dashed magenta and orange lines, respectively. ( b ) The ion bridge interaction of Lys249. Dashed cyan line represents ion bridges. ( c , d ) Mutational effect of the residues that participated in the interaction of Arg243 ( c ) and Lys249 ( d ) for the inactivation time constants. The inactivation time constants were measured from the current traces elicited by step pulses from holding potential at −140 mV. The time constant of NavSulP wild type (closed circle, n =8), R243E (open circle, n =4), Y242A (closed triangle, n =6), Y242F (open triangle, n =5), T239V (closed square, n =5) and R243A (open square, n =4) are represented in ( c ). The time constant of NavSulP wild type (closed circle, n =8), K249E (open circle, n =5), E251K (closed triangle, n =4), E254K (open triangle, n =4) and E251K/E254K (open square, n =4), are represented in ( d ). All values are presented as mean±standard error. ( e ) Sodium dodecyl sulphate-polyacrylamide gel electrophoresis analysis of tetramer and monomer fractions of NavSulP wild-type (WT) and mutants in size-exclusion chromatography. T and M indicate the tetramer and monomer fractions of NavSulP proteins in size-exclusion chromatography, respectively. To evaluate the amount of protein, proteins were denatured to monomers by sodium dodecyl sulphate treatment. The band intensities of the T and M lanes represent the amount of tetrameric channels and dissociated monomers, respectively. Most NavSulPΔC239 were dissociated to monomers and unable to form channel tetramers.

Journal: Nature Communications

Article Title: The C-terminal helical bundle of the tetrameric prokaryotic sodium channel accelerates the inactivation rate

doi: 10.1038/ncomms1797

Figure Lengend Snippet: ( a ) Intersubunit interaction around Arg243. Hydrogen bond and CH/ π stacking are indicated by dashed magenta and orange lines, respectively. ( b ) The ion bridge interaction of Lys249. Dashed cyan line represents ion bridges. ( c , d ) Mutational effect of the residues that participated in the interaction of Arg243 ( c ) and Lys249 ( d ) for the inactivation time constants. The inactivation time constants were measured from the current traces elicited by step pulses from holding potential at −140 mV. The time constant of NavSulP wild type (closed circle, n =8), R243E (open circle, n =4), Y242A (closed triangle, n =6), Y242F (open triangle, n =5), T239V (closed square, n =5) and R243A (open square, n =4) are represented in ( c ). The time constant of NavSulP wild type (closed circle, n =8), K249E (open circle, n =5), E251K (closed triangle, n =4), E254K (open triangle, n =4) and E251K/E254K (open square, n =4), are represented in ( d ). All values are presented as mean±standard error. ( e ) Sodium dodecyl sulphate-polyacrylamide gel electrophoresis analysis of tetramer and monomer fractions of NavSulP wild-type (WT) and mutants in size-exclusion chromatography. T and M indicate the tetramer and monomer fractions of NavSulP proteins in size-exclusion chromatography, respectively. To evaluate the amount of protein, proteins were denatured to monomers by sodium dodecyl sulphate treatment. The band intensities of the T and M lanes represent the amount of tetrameric channels and dissociated monomers, respectively. Most NavSulPΔC239 were dissociated to monomers and unable to form channel tetramers.

Article Snippet: Purified proteins were resolved on 7.5–20% sodium dodecyl sulphate-polyacrylamide gel electrophoresis gradient gels (Wako) and stained with silver staining.

Techniques: Polyacrylamide Gel Electrophoresis, Size-exclusion Chromatography