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Why dont you use ethidium bromide staining for non denaturing PAGE gels?
Tanuat
Because PAGE gels are used to look a protein and ethidium bromide only stains double stranded nucleic acids.
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What is denaturing sds page?
Sodium dodecyl sulphate (SDS) is an anionic detergent which denatures proteins by "wrapping around" the polypeptide backbone - and SDS binds to proteins fairly specifically in a mass ratio of 1.4:1. In so doing, SDS confers a negative charge to the polypeptide in proportion to its length - ie: the denatured polypeptides become "rods" of negative charge cloud with equal charge or charge densities per unit length. It is usually necessary to reduce disulphide bridges in proteins before they adopt the random-coil configuration necessary for separation by size: this is done with 2- mercaptoethanol or dithiothreitol. In denaturing SDS-PAGE separations therefore, migration is determined not by intrinsic electrical charge of the polypeptide, but by molecular weightAnd for the actual experiment beyond the denaturing: PAGE stands for polyacylamide gel electrophoresis. This is a procedure that separates proteins by size by running them through a gel "matrix" so that the smaller ones travel faster that the larger ones. This is achieved by creating an electric field with the sds-protein complex traveling toward the positively charged end of the gel. Once the smallest proteins have traveled most of the way across the gel the current is turned of and the gel is removed and stained with dye that binds protein so that you can see where it is in the gel.
What is the minimum amount of protein that can appear in SDS PAGE gel?
Although this would in part depend the size of the protein being separated and stained (for some staining methods), the largest factor that determines sensitivity of SDS-PAGE is the type of staining method used: - If staining is done with coomassie brilliant blue, the limit of detection claimed by most suppliers is 50 ng. In my experience, 100-1000 ng is more accurate for proteins of 20-30 kDa. - If staining is done with silver stain, the limit of detection is much lower (or higher sensitivity). Manufacturers usually claim that 5-50 ng of protein can be visualized, but in my experience 50 ng is the lower limit for average sized proteins (20-30 kDa). - If visualization is accomplished with an enzyme immunoassay, the limit of detection is lower still, as low as 0.1-1 ng (100-1000 pg). - If visualization is accomplished with radio immunoassay the limit of detection becomes much lower again, easily to the picogram level (0.001 ng).
Purpose of gel electrophoresis?
Polyacrylamide gel electrophoresis (PAGE) is used to separate large biomolecules, such as RNA, DNA and proteins, by their size, shape and charge. Proteins can be separated based on their size alone if the sample is treated with a denaturing agent first, such as sodium dodecyl sulfate (SDS). Nucleic acid samples can be separated on size alone through the use of an agarose gel.
What is the first part of the geography book called?
The title page is the first page of a book.
What is the nema of the Right hand page of a book?
The right-hand page of a book is called the recto.
Why is denaturing sds-page used for running sds-page electrophoresis of egg-white lysozyme and not non-denaturing page?
may be because of toomany disulfide linkages
What is Permanent unfolding of normal protein?
its like the denaturation of proteins so just look up denaturation of proteins on google and there should be an animation on it on the first page. it explains everything
Why two stains required in SDS PAGE- bromophenol blue and coomassie blue?
bromophenol blue is used as the tracking dye while coomassie brilliant blue is the staining dye.
How separated bands of human serum in a sds page can be recognised?
it could be recognized using a staining day that used to stain proteins in the sample it will separate several band according to molecular weight
Do you know of a website that will help me pick out a local painting contractor?
Here's a site that can help you: http://www.servicemagic.com/category.Painting-Staining.10215.html . Note that this is the "main" painting contractor page. You'll need to enter your zipcode to narrow the search.
What is the minimum amount of protein that can appear in SDS PAGE gel?
Although this would in part depend the size of the protein being separated and stained (for some staining methods), the largest factor that determines sensitivity of SDS-PAGE is the type of staining method used: - If staining is done with coomassie brilliant blue, the limit of detection claimed by most suppliers is 50 ng. In my experience, 100-1000 ng is more accurate for proteins of 20-30 kDa. - If staining is done with silver stain, the limit of detection is much lower (or higher sensitivity). Manufacturers usually claim that 5-50 ng of protein can be visualized, but in my experience 50 ng is the lower limit for average sized proteins (20-30 kDa). - If visualization is accomplished with an enzyme immunoassay, the limit of detection is lower still, as low as 0.1-1 ng (100-1000 pg). - If visualization is accomplished with radio immunoassay the limit of detection becomes much lower again, easily to the picogram level (0.001 ng).
What is denaturing sds page?
Sodium dodecyl sulphate (SDS) is an anionic detergent which denatures proteins by "wrapping around" the polypeptide backbone - and SDS binds to proteins fairly specifically in a mass ratio of 1.4:1. In so doing, SDS confers a negative charge to the polypeptide in proportion to its length - ie: the denatured polypeptides become "rods" of negative charge cloud with equal charge or charge densities per unit length. It is usually necessary to reduce disulphide bridges in proteins before they adopt the random-coil configuration necessary for separation by size: this is done with 2- mercaptoethanol or dithiothreitol. In denaturing SDS-PAGE separations therefore, migration is determined not by intrinsic electrical charge of the polypeptide, but by molecular weightAnd for the actual experiment beyond the denaturing: PAGE stands for polyacylamide gel electrophoresis. This is a procedure that separates proteins by size by running them through a gel "matrix" so that the smaller ones travel faster that the larger ones. This is achieved by creating an electric field with the sds-protein complex traveling toward the positively charged end of the gel. Once the smallest proteins have traveled most of the way across the gel the current is turned of and the gel is removed and stained with dye that binds protein so that you can see where it is in the gel.
Purpose of gel electrophoresis?
Polyacrylamide gel electrophoresis (PAGE) is used to separate large biomolecules, such as RNA, DNA and proteins, by their size, shape and charge. Proteins can be separated based on their size alone if the sample is treated with a denaturing agent first, such as sodium dodecyl sulfate (SDS). Nucleic acid samples can be separated on size alone through the use of an agarose gel.
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page 9,sometimes page 35,misses page 38,scavenger page 40,examples page 62,picture page 63,how page 64,fishing page 65,storage page 71,seats page 71,musical page 73,search page 75,tossing page 77,buying page 101,donated page 117,jerseys page 118,squads page 140,breeze page 141,conbined page 143,secret page 154,aren page 155,queen page 156,small page 169,start page 171,annual page 175,crown page 176,item page 179,penguins page 182,actions
What keyboard command moves to the next worksheet in a workbook?
Ctrl - Page Up and Ctrl - Page Down.Ctrl - Page Up and Ctrl - Page Down.Ctrl - Page Up and Ctrl - Page Down.Ctrl - Page Up and Ctrl - Page Down.Ctrl - Page Up and Ctrl - Page Down.Ctrl - Page Up and Ctrl - Page Down.Ctrl - Page Up and Ctrl - Page Down.Ctrl - Page Up and Ctrl - Page Down.Ctrl - Page Up and Ctrl - Page Down.Ctrl - Page Up and Ctrl - Page Down.Ctrl - Page Up and Ctrl - Page Down.
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