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The concentration of a purified monoclonal antibody was measured using UV280 nm. The sample was diluted (200 μL of purified antibody in 800 μL buffer) prior to analysis using a spectrophotometer. Calculate the concentration of antibody in the purified fraction if the Abs=0.95 of the diluted antibody. The molar absorptivity is known to be 191,411.6 M-1cm-1 and the molecular weight is 150 kDa. The pathlength for the cuvette is 1 cm.
Monoclonal antibodies are laboratory-produced molecules that are engineered to mimic the immune system's ability to fight off harmful pathogens. They are made from identical immune cells that are all clones of a unique parent cell, hence the name "monoclonal." These antibodies can be designed to target specific proteins or cells, making them useful for treating a variety of diseases, including cancer, autoimmune disorders, and infectious diseases.
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- Suppose that you are tasked to determine the protein concentration of an unknown protein solution via Bradford assay. You prepared six solutions of bovine serum albumin (BSA) with different concentrations. The initial concentration of the BSA stock solution is 7.50 mg/mL. Approximately 200 µL of Bradford Reagent was added to each of these solutions and the absorbance at 595 nm was taken after 5 minutes. See the table below for data on the standard solutions. Standard # A595 BSA conc (mg/mL) 0.000 0.158 2 1.125 0.291 2.250 0.372 4 3.375 0.503 5 4.500 6 5.625 0.675 Determine the protein concentration, in mg/mL, of the unknown solution if its absorbance at 595 nm was 0.248. Note: Final answer format must be x.xx (two decimal places). Round off only in the final answer. Do not round off in the middle of calculation.arrow_forward8L.Part Iarrow_forwardYou perform a Bradford assay. You obtain the absorbance values listed below from the BSA samples; your protein sample yields an absorbance of 1.3; what is the protein concentration of your sample? How did you determine that? BSA (ug/ml) Absorbance @ 595 nm. 25 0.15 50 0.30 75 0.45 100 0.60 150 0.90 200 1.25arrow_forward
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- Please dont provide handwrittin solution.../.arrow_forward(b) Both laboratories used 10 micrograms of protein each in their kinetic assays. Protein concentrations weredetermined by the Bradford protein assay. Assay conditions employed in the two labs (pH, temperature,etc.) were also identical. What would be the most plausible cause for the discrepancy in the Vmax valuesfor the compound I? Explain.Recall that the Bradford assay measures total protein amounts in sample solution based on complexformation between a dye and proteins. Also, the assay solution used in both labs does not contain anyinhibitors.arrow_forwardMatch the types of data to the example. Precise measurements Assay standard Positive control Quantitative results Negative control Qualitative results Standard curve…arrow_forward
- With an accompanying brief narrative, write a short lab report (brieflydescribing what you did) and in a results section, show your standard curve andtabulate the concentration of the unknown protein samples provided using thethe Bradford Assay and UV absorbance)arrow_forwardUsing the SDS-PAGE and the calibration curve given, calculate the size of the lysozyme and ovalbumin bands from this lysozyme purification. Lysozyme is the bottom band in the samples, ovalbumin is the most intense band in the first three samples, and the first and last lanes are molecular mass standards.arrow_forwardV2arrow_forward
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