SDS: Describe the procedure to use after the stacking gel has hardened and before you load...
SDS: Describe the procedure to use after the stacking gel has hardened and before you load your samples.
Homework Answers
After the stacking gel has hardened, remove the comb and the casting frame.
Place the plates with the gel in the electrophoresis apparatus and pour the tank buffer otherwise called as running buffer. immerse it completely in the running buffer. Both the upper and lower tank should be filled. Remove any bubbles present by using a syringe.
By the time prepare the sample according to your protocol, basically the samples are mixed with sample loading buffer and boiled for 5-10min according to the temperature you set.
Now you can load the samples inside the well and switch on the apparatus.
Add Answer to:
SDS: Describe the procedure to use after the stacking gel has
hardened and before you load...
parts a,b, c please 3. Sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis a. After pouring the...
parts a,b, c please
3. Sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis a. After pouring the SDS polyacrylamide gel, you realize that instead of 2 ml, you used 4 ml of 30% acrylamide/bisacrylamide solution for the preparation of the separating gel (in both cases for 5 ml, total gel volume). How would this affect the separation of your proteins during SDS PAGE? Explain your answer! b. You have to remake the gel and are now making sure just to add...
You start running an SDS-PAGE gel at 200V. After 10 minutes, you notice that the dye...
You start running an SDS-PAGE gel at 200V. After 10 minutes, you notice that the dye front has not moved very far and the current has dropped to almost zero. What's the most likely explanation for what has happened here?
1d. Finally, you run SDS-PAGE in the presence of 2-mercaptoet urun SDS-PAGE in the presence of...
1d. Finally, you run SDS-PAGE in the presence of 2-mercaptoet urun SDS-PAGE in the presence of 2.mernantoethanol on a subsample of each peak from each column in parts 1a and ic. The image below shows the migration of molecular weight markers and labels for each sample lane Indicate the location of protein band(s) for each of your samples. Identify the protein(s) in each band in each lane and explain your reasoning Anion Exchange 12 Gel Fitration 12 Gel filtation after...
what would happen to the proteins in your gel if you did not add SDS-PAGE?
what would happen to the proteins in your gel if you did not add SDS-PAGE?
12. In the gel electropboresis procedure we added ethidium bromide to the gel in order to...
12. In the gel electropboresis procedure we added ethidium bromide to the gel in order to Visualize the DNA. What specific health hazard is associated with this chemical? 13. Briefly describe one reason a non-biologist might want to identify a fungal sample to the species level. 14. After you weigh a fungal sample for DNA extraction; what is the first step towards isolating the DNA? 15. When handling a micropipet, why is it necessary to always hold it upright (tip...
Explanation of SDS-PAGE for Western blotting procedure, PLEASE answer the questions BELOW: 1. What does a...
Explanation of SDS-PAGE for Western blotting procedure, PLEASE answer the questions BELOW: 1. What does a gel electrophoresis allow you to do? 2. What is a gel? 3. How do you make the protein move, and why does this work? 4. Which protein fragments travel the furthest and why? 5. Name 3 materials used to make a gel. 6. What is polyacrylamide? 7. What is the purpose of the buffer? 8. What is the comb (in the gel) for? 9....
SDS Page Gel: The provided standard protein sample for electrophoresis consists of 9 polypeptides with molecular...
SDS Page Gel:
The provided standard protein sample for electrophoresis
consists of 9 polypeptides with molecular weights ranging from 250
to 15 KDa.
Sample 1: Protein A in a sample buffer with
B-Mercaptoethanol
Sample 2: Protein A in a sample buffer without
B-Mercaptoethanol
Sample 3: Protein B in a sample buffer with
B-Mercaptoethanol
Sample 4: Protein C in a sample buffer without
B-Mercaptoethanol
Use the picture below & the information about the proteins
above to answer the following questions.
1a....
You find yourself setting up another Western blot, however. today you are preparing the samples t...
You find yourself setting up another Western blot, however. today you are preparing the samples to load onto the SDS-PAGE gel. You are using a 4-20%SDS-PAGE gel that can hold a maximum of 30 μしper 1 You remember from you so decided to prepare each sample with a final volume of 25 uL. However, no one is perfect at pipetting, so make sure each sample is made at 1.5X the total volume needed per well. The protein you are interested...
Carl has just finished purifying a protein and analysis by gel filtration indicated that the molecular...
Carl has just finished purifying a protein and analysis by gel filtration indicated that the molecular weight of the native (undenatured) protein was 130,000 dalton. His advisor wanted him to determine whether this protein had quaternary structure using gel electrophoresis. He wants to be able to describe the molecular weight of each of the subunits and the forces involved in linking these subunits together (disulfide linkages and/or electrostatic, hydrogen bonding and hydrophobic interactions). Carl first analyzed his pure protein sample...
Not sure how to figure out what formulas to use here esolving gel with DI water,...
Not sure how to figure out what formulas to use here
esolving gel with DI water, and blot dry with a paper towel. (demo) a small flask (clean and reuse the old flask), mix com , swirl to mix and add the mixture (with a Pasteur pipet) to the gel ur ponents of the s dly in sert the comb. Some acrylamide may spill out of the gel. Repeat erize at room temperature for 45 min. below should be drawn,...
parts a,b, c please
3. Sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis a. After pouring the SDS polyacrylamide gel, you realize that instead of 2 ml, you used 4 ml of 30% acrylamide/bisacrylamide solution for the preparation of the separating gel (in both cases for 5 ml, total gel volume). How would this affect the separation of your proteins during SDS PAGE? Explain your answer! b. You have to remake the gel and are now making sure just to add...
1d. Finally, you run SDS-PAGE in the presence of 2-mercaptoet urun SDS-PAGE in the presence of 2.mernantoethanol on a subsample of each peak from each column in parts 1a and ic. The image below shows the migration of molecular weight markers and labels for each sample lane Indicate the location of protein band(s) for each of your samples. Identify the protein(s) in each band in each lane and explain your reasoning Anion Exchange 12 Gel Fitration 12 Gel filtation after...
12. In the gel electropboresis procedure we added ethidium bromide to the gel in order to Visualize the DNA. What specific health hazard is associated with this chemical? 13. Briefly describe one reason a non-biologist might want to identify a fungal sample to the species level. 14. After you weigh a fungal sample for DNA extraction; what is the first step towards isolating the DNA? 15. When handling a micropipet, why is it necessary to always hold it upright (tip...
SDS Page Gel:
The provided standard protein sample for electrophoresis
consists of 9 polypeptides with molecular weights ranging from 250
to 15 KDa.
Sample 1: Protein A in a sample buffer with
B-Mercaptoethanol
Sample 2: Protein A in a sample buffer without
B-Mercaptoethanol
Sample 3: Protein B in a sample buffer with
B-Mercaptoethanol
Sample 4: Protein C in a sample buffer without
B-Mercaptoethanol
Use the picture below & the information about the proteins
above to answer the following questions.
1a....
You find yourself setting up another Western blot, however. today you are preparing the samples to load onto the SDS-PAGE gel. You are using a 4-20%SDS-PAGE gel that can hold a maximum of 30 μしper 1 You remember from you so decided to prepare each sample with a final volume of 25 uL. However, no one is perfect at pipetting, so make sure each sample is made at 1.5X the total volume needed per well. The protein you are interested...
Not sure how to figure out what formulas to use here
esolving gel with DI water, and blot dry with a paper towel. (demo) a small flask (clean and reuse the old flask), mix com , swirl to mix and add the mixture (with a Pasteur pipet) to the gel ur ponents of the s dly in sert the comb. Some acrylamide may spill out of the gel. Repeat erize at room temperature for 45 min. below should be drawn,...
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