Question

In: Biology

This is a question about the SDS - PAGE method, one of the protein analysis methods....

This is a question about the SDS - PAGE method, one of the protein analysis methods.

1. I would like to know the functions of resolving gel and stacking gel in SDS - PAGE analysis.

2. I would like to know the various reagents used in manufacturing resolving gel and stacking gel in SDS - PAGE analysis and their role. ( Please tell us in detail the role of each reagent. )

We would appreciate your detailed explanation of each question.

Solutions

Expert Solution


Related Solutions

This is a question about the SDS - PAGE method, one of the protein analysis methods....
This is a question about the SDS - PAGE method, one of the protein analysis methods. I would like to know the various reagents used in manufacturing resolving gel and stacking gel in SDS - PAGE analysis and their role. ( Please tell us in detail the role of each reagent. ) 30% Acrylamide/bis 0.5M Tris-HCl, pH 6.8 1.5M Tris-HCl, pH 8.8 10% SDS diH2O TEMED 10% APS We would appreciate your detailed explanation. Please typing.
This is a question about the SDS - PAGE method, one of the protein analysis methods....
This is a question about the SDS - PAGE method, one of the protein analysis methods. 1. I would like to know the functions of resolving gel and stacking gel in SDS - PAGE analysis. 2. I would like to know the various reagents used in manufacturing resolving gel and stacking gel in SDS - PAGE analysis and their role. ( Please tell us in detail the role of each reagent. ) We would appreciate your detailed explanation of each...
Compare and contrast protein (SDS-PAGE) and DNA (agarose) gel electrophoresis.
Compare and contrast protein (SDS-PAGE) and DNA (agarose) gel electrophoresis.
Explain how the same protein can migrate differently on SDS page
Explain how the same protein can migrate differently on SDS page
How do we visualize the protein profile of the sample after SDS-PAGE?
Reagents, Supplies and Equipment Laemmli sample buffer containing Dithiothreitol (DTT) at 10 mg/mL 10X tris-glycine-SDS (TGS) electrophoresis buffer Bio-Safe Coomassie stain for proteins Actin and myosin standard Precision Plus Protein Kaleidoscope pre-stained standard Mini-PROTEAN pre-cast polyacrylamide gels Mini-PROTEAN Tetra gel electrophoresis system Microcentrifuge tubes and microcentrifuge tube rack Heat block at 95oC Pipets and pipet tips Procedure Part A – Protein Extraction Using a spatula, put a small amount of fish or meat into a microtube. Weight the tube to...
what information give SDS-PAGE about the proteins that are being analysed ?
what information give SDS-PAGE about the proteins that are being analysed ?
SDS-PAGE separates proteins by:
  SDS-PAGE separates proteins by:   Question 1 options:   Size   Structure   Viscosity   Function       Intercomplementarity occurs when the primer forms structure as a hairpin loop Question 3 options: True False     Which component is not required in the first round of RT reaction? Question 5 options:   reverse transcripatase enzyme   buffer   DNA polymarese   mRNA template       If you want to clone your PCR product your primer should have...
You are given 5mL of 3mg/mL protein solution. You are asked to prepare samples for SDS-PAGE...
You are given 5mL of 3mg/mL protein solution. You are asked to prepare samples for SDS-PAGE containing 250ng, 500ng, 750ng, and 1000ng. Your pipettes are calibrated to 2uL at the lower limit. Your total volume is 20uL, with 5uL being your loading buffer. How would you prepare these samples?
You are given 5mL of 3mg/mL protein solution. You are asked to prepare samples for SDS-PAGE...
You are given 5mL of 3mg/mL protein solution. You are asked to prepare samples for SDS-PAGE containing 250ng, 500ng, 750ng, and 1000ng. Your pipettes are calibrated to 2uL at the lower limit. Your total volume is 20uL, with 5uL being your loading buffer. How would you prepare these samples?
Biochemistry: I am doing a lab report on protein quaternary structures using a SDS-PAGE. We used...
Biochemistry: I am doing a lab report on protein quaternary structures using a SDS-PAGE. We used denaturants such as BME and urea to see which proteins were held by disulfide bonds. The proteins that we used were Carbonic anyhydrase (CA), glyceraldehyde 3-phosphate dehydrogenase (GPD), hemoglobin (Hb), and superoxide dismutase (SOD). We had a set that was treated with BME and Urea. The other set was plain. Well, results were just awful. No I do not have the gel results on...
ADVERTISEMENT
ADVERTISEMENT
ADVERTISEMENT