Results 211 to 220 of about 684,938 (261)
Advanced Science, EarlyView.Neuronal PKM2‐driven glycolysis generates excess lactate that triggers histone H3K18 lactylation (H3K18la), establishing a pathogenic metabolic‐epigenetic axis in epilepsy. Elevated H3K18la enriches the Cop1 promoter, transcriptionally upregulating the E3 ubiquitin ligase COP1, which subsequently drives proteasomal degradation of GABAARβ2 and impairs ...
Yuan Meng +8 more
wiley +1 more source
Advanced Science, EarlyView.ABSTRACT Diabetes mellitus‐induced erectile dysfunction (DMED) is a highly prevalent complication among diabetic patients; however, its underlying pathogenic mechanisms remain incompletely understood. Metabolic disorder is a hallmark of diabetes, yet its precise contribution to DMED progression is not well defined.
Wanyang Guo +14 more
wiley +1 more source
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Proteomics, 2011
AbstractSDS normally is strictly avoided during Blue native (BN) PAGE because it leads to disassembly of protein complexes and unfolding of proteins. Here, we report a modified BN‐PAGE procedure, which is based on low‐SDS treatment of biological samples prior to native gel electrophoresis.
Jennifer Senkler, Hans-Peter Braun
exaly +3 more sources
AbstractSDS normally is strictly avoided during Blue native (BN) PAGE because it leads to disassembly of protein complexes and unfolding of proteins. Here, we report a modified BN‐PAGE procedure, which is based on low‐SDS treatment of biological samples prior to native gel electrophoresis.
Jennifer Senkler, Hans-Peter Braun
exaly +3 more sources
2012
Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis (tricine-SDS-PAGE) is an efficient way of separating low molecular mass proteins. However, the standard system is quite complicated and specifically may not be useful when the separated proteins are to be recovered from the gel for quantitative analysis.
Syed R, Haider +2 more
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Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis (tricine-SDS-PAGE) is an efficient way of separating low molecular mass proteins. However, the standard system is quite complicated and specifically may not be useful when the separated proteins are to be recovered from the gel for quantitative analysis.
Syed R, Haider +2 more
openaire +3 more sources
2018
The discontinuous polyacrylamide gel electrophoresis system devised by Laemmli (Nature 227:680-685, 1970) has not only been used in numerous laboratories but has also been modified in several ways since its birth. In our laboratories, we use a modified Laemmli SDS-PAGE system for following protein purification as well as for analysis of certain protein-
Lars, Backman, Karina, Persson
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The discontinuous polyacrylamide gel electrophoresis system devised by Laemmli (Nature 227:680-685, 1970) has not only been used in numerous laboratories but has also been modified in several ways since its birth. In our laboratories, we use a modified Laemmli SDS-PAGE system for following protein purification as well as for analysis of certain protein-
Lars, Backman, Karina, Persson
openaire +2 more sources
SDS-PAGE Focusing: Preparative Aspects
Analytical Chemistry, 2007As a followup of our previous report (Zilberstein, G.; Korol, L.; Antonioli, P.; Righetti, P. G.; Bukshpan, S. Anal. Chem. 2007, 79, 821-827) on analytical SDS-PAGE focusing, a novel method is here reported for small-scale prefractionation of complex protein mixtures, for subsequent proteome analysis, based on mass separation of SDS-protein micelles ...
G. Zilberstein +3 more
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Nature Protocols, 2006
Tricine-SDS-PAGE is commonly used to separate proteins in the mass range 1-100 kDa. It is the preferred electrophoretic system for the resolution of proteins smaller than 30 kDa. The concentrations of acrylamide used in the gels are lower than in other electrophoretic systems. These lower concentrations facilitate electroblotting, which is particularly
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Tricine-SDS-PAGE is commonly used to separate proteins in the mass range 1-100 kDa. It is the preferred electrophoretic system for the resolution of proteins smaller than 30 kDa. The concentrations of acrylamide used in the gels are lower than in other electrophoretic systems. These lower concentrations facilitate electroblotting, which is particularly
openaire +2 more sources
Cold Spring Harbor Protocols, 2006
INTRODUCTION Initial heating of a protein sample at 95°C in the presence of excess SDS and a thiol reagent denatures the protein mixture and disrupts disulfide bonds. Under these conditions, all reduced polypeptides bind the same amount of SDS (1.4 g of SDS per gram of polypeptide) independent of amino acid composition and sequence. The resolving power
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INTRODUCTION Initial heating of a protein sample at 95°C in the presence of excess SDS and a thiol reagent denatures the protein mixture and disrupts disulfide bonds. Under these conditions, all reduced polypeptides bind the same amount of SDS (1.4 g of SDS per gram of polypeptide) independent of amino acid composition and sequence. The resolving power
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SDS‐Polyacrylamide Gel Electrophoresis (SDS‐PAGE)
Current Protocols Essential Laboratory Techniques, 2008AbstractElectrophoresis is used to separate complex mixtures of proteins (e.g., from cells, subcellular fractions, column fractions, or immunoprecipitates), investigate subunit compositions, verify homogeneity of protein samples, and purify proteins for use in further applications.
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