In urea assay (Catalog #K375-100) what is the nmol (range) it can detect?
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) In urea assay (Catalog #K375-100) what is the nmol (range) it can detect?
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- (MB = methylene blue) What is the concentration of the sample of the substance with the reporter absorbance of 0.40 at 595 nm?Gel-filtration chromatography is a useful method for removing salts, such as ammonium sulfate, from protein solutions. Describe how such a separation is accomplished.In a mixture of five proteins listed, draw an elution profile (Absorbance vs. mL eluted, arbitrary) for the purification of the listed proteins on a gel filtration chromatography resin: cytochrome c (pI = 5.4; Mr = 13,000), immunoglobulin G (pI = 7.3; Mr = 145,000), ribonuclease A (pI = 9.6; Mr = 13,700), RNA polymerase (pI = 6.3; Mr = 450,000), human serum albumin (pI = 5.4; Mr = 68,500). Label your elution peaks. Draw a sketch of an SDS-PAGE, reflecting the mobility of the above mixture as they elute from the column. Label you protein bands.
- A number of techniques can separate proteins on the basis of their differences in mass. Describe the use of two of these techniques, centrifugation and gel electrophoresis. The blood proteins transferrin (MW 76 kDa) and lysozyme (MW 15 kDa) can be separated by rate zonal centrifugation or SDS-polyacrylamide gel electrophoresis. Which of the two proteins will sediment faster during centrifugation? Which will migrate faster during electrophoresis?Can we purify mCherry protein (His-tag attached) with immobilised metal ions affinity chromatography (Ni-IDA)? If so, how can we confirm whether the protein is purified and how to increase its purity?In nickel column affinity chromatography,how does the protein binds to column?How is the protein eluted from the column?
- A vial of Doxorubicin reads 0•5g per vial. Instructions say to reconstitute each 12mg with 2•5ml of NS. How many ml of NS will be needed to reconstitute the vial of the recommended concentration? please show workingIn a gel filtration chromatography, what type of gel must be used when the protein size is 2500 Da? Explain.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.
- Design an assay with purified phycocyanin to test protein stability using 500ml of 95% ethanol. Then do the same with 2 M sodium chloride. Make each step clear.If 1ml of an unknown sample of protein is diluted to 10ml, and a 0.5ml portion of the diluted sample is found to contain 50ug of protein when assayed for protein using the lowry method. If you mix two unknown samples and repeat the lowry assay, is the absorbance equivalent to the sum of the two individual unknown samples that is used?G418 disulfate (FW 692.7) is an antibiotic used to select transfected mammalian cells in tissue culture. The standard working concentration for selection is 400 µg/mL of active ingredient in culture medium. The bottle states that it contains 71% active ingredient. You need to make a 100x stock in medium and adjust the pH before you apply it to cells. How much powder should be added to make 10 mL of stock solution? How much do you add to a 2 mL culture dish?