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In Western Blots and ELISAS, the following molecules are used:
Tween-20
SDS
Goat anti-rabbit IgG (whole molecule) – HRP
Rabbit anti-egg albumin
Bovine IgG
Rabbit anti-bovine IgG – HRP
Egg albumin (globular protein – what is Molecular weight?)
Milk protein (globular protein – what is Molecular weight?)
TMB
Beta-mercaptoethanol
Methanol
HCl
May you explain the reasons why they are used?
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- antibodies were produced in a rabbit against a 25 KDa human soluble protien. when the rabbit antiserum was used in a western blot of human soluble protiens, it detected 25-KDa protien,but also bound to protiens of 65KDa and 39 KDa.assuming that a pure protien was used to make the antibodies,how do yuo explain the results of the western blot?What is the purpose of Southern's blotting technique? Explain in detail the biochemical principle that underpin each step of the method.A Western blot is seen in the picture above. Sodium dodecyl sulfate gel polyacrylamide gel electrophoresis was used to isolate the proteins (SDS-PAGE).1. Since gel electrophoresis has isolated individual proteins, what kind of molecule is used to detect them? 2. On the right side of this Western blot, three molecules are identified. One of the bands corresponds to the smallest molecule?
- At higher amounts of protein, the Bradford assay is not linear. Consider the plot to the right: what is the maximum amount of protein a sample could contain and still fall within a standard curve? Briefly explain your reasoning.why are lysozyme and ovoalbumin the recommended standards used in the Bradford protein assay and why would they be preferred over BSA being this widely used but not recommended? Justify the answerHow would you determine the concentration of a protein that falls outside (above or below) the linear range of this assay? asap
- If a student uses a monoclonal antibody to detect a protein using a direct Western-blotting protocol after running an SDS PAGE, the student can detect a 50kd protein. However, if the student tries to use this antibody to immunoprecipitate the 50 kd protein and then Western -blot the immunoprecipitated samples, the student found that there is no band at all at 50kd region in the Western blot. How do you explain these results based on what you know about protein structure and antigen-antibody recognition? (Hint: Western blot analysis explores an SDS-containing buffer, whereas the immunoprecipitation buffer uses a NP40-containing buffer to maintain proteins in their native form).In the Western blot shown here, proteins were isolated from redblood cells and muscle cells from two different individuals. Oneindividual was unaffected, and the other suffered from a diseaseknown as thalassemia, which involves a defect in hemoglobin. Theblot was exposed to an antibody that recognizes β globin, whichis one of the polypeptides that constitute hemoglobin. Equal totalamounts of cellular proteins were added to each lane. Explain these results.There are three names that often get used when discussing the Lowry assay. Those names are: Lowry, Folin-Ciocalteu, and Biuret. Are those names interchangeable when discussing the assay or do those names describe the same thing(s)? Significant differences? What is the relationship between those names?
- Why is the bradford assay method using BSA sensitive ? and how does it compare to the amino acid analysis methodDraw a gel to represent the band shift assay result for testing the following mixtures: (1) Eukaryotic DNA along(2) Eukaryotic DNA + TFs(3) Eukaryotic DNA + RNA polymerase II(4) Eukaryotic DNA + TFs + RNA polymerase II(5) Eukaryotic DNA + TFs + RNA polymerase II + nucleotidesBands for smaller molecules can be ignoredHow is the Bicinchoninic acid assay used in protein quantification?