The protein concentration of a known standard is 100mg/mL If you prepared a serial dilution, mixing 10μL of protein with 40μL of water what would be concentrations of the first 3 dilutions?
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The protein concentration of a known standard is 100mg/mL If you prepared a serial dilution, mixing 10μL of protein with 40μL of water what would be concentrations of the first 3 dilutions?
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- To prepare a gel sample, you want to load 50 ng total of protein/well. You have added 200 μL of protein in 800 µL reagent and measured your sample by Bradford A595 to be 0.7 mg/mL - your dilution is unaccounted for at this point. Assuming a total final volume of 20 μL, what volume of protein sample, buffer and 4X SDS PAGE Loading Dye needs to be mixed to create a final sample of 50 ng protein in 20 μL?You will be given 1 mL of a 2.0 mg/mL solution of bovine serum albumin (BSA) and 1 mL of a 2.0 mg/mL solution of bovine gamma globulin (BGG). From these solutions, you will need to make 100 μL of each of the following standards using 1x MBP purification buffer as the diluent for preparation of a standard curve: 1000 μg/mL, 750 μg/mL, 500 μg/mL, 250 μg/mL, 125 μg/mL, and 0 μg/mL.The A280 of a protein sample loaded onto a gel was determined to be 0.767 (1.00 cm path length, after subtracting the blank). The total volume of this sample was 428 µL. 19.0 µL of this protein sample was mixed with 19.0 µL of 2X laemalli sample buffer and then 12.0 µL of the entire sample was loaded into the gel and electrophoresed. Calculate the amount of protein that was loaded into the gel (in µg).
- Consider a mixture of two proteins with molecular weights of 20,000 and 200,000. For simplicity of calculation, both may be approximated as unhydrated spheres with VB 0.740 mL g1. a. Calculate the ratio of the sedimentation coefficients of the proteins in the same medium (density=1.05 g mL¯1) at the same temperature.You perform a Bradford assay to determine the concentration of isolated α-lactalbumin. You use 50 μL of a two-fold diluted solution of α-lactalbumin in the assay. You generate a standard curve with the following equation for the line: y = 0.163x + 0.082. The absorbance of your sample was 0.674 AU. What is the concentration of α-lactalbumin, in mg/mL, in your sample? Give your answer to three significant figures.The following stock solutions are available to make a protein extraction buffer: 100% Nonidet P-40, 1 M Tris-Cl, and 0.5 M EDTA. What quantity of the original stocks will be needed to make 250 ml of buffer with the following final concentrations: 0.5% Nonidet, 150 mM Tris-Cl, and 10 mM EDTA?
- The calibration curve shown below was used to analyze an unknown protein solution. What is the concentration of the unknown solution, if the absorbance of the unknown is 0.505? Answer in ug/mL. 1.2 y%3D0.005x+0.061 R=0.992 0.8 0.6 0.4 0.2 50 100 150 200 250 Concentration ug/ml AbsorbanceCalculate the volume of BSA stock that will be required to make the standard solutions needed to create the BSA standard curve. Be sure to show your work and include the volume of 0.02 M phosphate buffer required to reach a final volume of 1 mL. From a 2,000 μg/mL BSA stock, create 1 mL of each of the following stock solutions in 0.02 M phosphate buffer using individual microcentrifuge tubes: 50 μg/mL, 250 μg/mL, 500 μg/mL, 1,000 μg/mL, 1,250 μg/mL, 1,500 μg/mL. Be sure to properly label all the microcentrifuge tubes before creating the standards.1) You have been asked to make up four 1.5% agarose gels at 30 ml each. Ethidium Bromide is to be added at 0.5 ug/ml and you have a bottle at 10ug/ml. Write down step-by-step protocol of how to proceed. 2. How would you make up one liter of 1X TAE buffer using a 25X stock?
- Calculate the appropriate volume (in µL) of 3X loading buffer that should be added to 24.0 µL of a sample prior to loading the sample on an agarose gel.A solution containing egg albumin (pl=4.6), B-lactoglobulin (pl=5.2), and chymotrypsinogen (pl=9.5) was loaded onto a column of diethylaminoethyl cellulose (DEAE-cellulose) at pH 5.4.The column was then eluted with a pH 5.4 buffer, with an increasing salt concentration. Predict the elution pattern.The diffusivity of amino acids in polyacrylamide gel is approximately 1x10^-9 cm2./s calculate the initial flux of amino acids, give an instantaneous gradient of (20g/cm 3 )/8cm Why is polyacrylamide gel is used in electrophoresis?