Compare and contrast ELISA and western blotting (immunoblotting) by placing the phrases to the technique that they describe.If a phrase describes both ELISA and western blotting, place it under Both.ELISAcan be used to detect antibody in a sampleIncorrectrequires formation of anantigen-antibody complexWestern blot with SDS-PAGEproteins are in their native stateproteins have no higher order structureproteins transferred to a membrane or sheetAnswer BankBoth

Both ELISA & Western Blot are laboratory techniques which are used for the detection of specific…

Answered: Compare and contrast ELISA and western…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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29 of 41 In a western blot, the primary antibody binds to the while the secondary antibody binds to the O target protein; nitrocellulose membrane O Nitrocellulose membrane; target protein O target protein: primary antibody O secondary antibody; target protein
After the electrophoretic separation, the proteins are transferred to a nitrocellulose membrane prior to staining with antibodies specific for the protein understudy. Describe in detail how the primary and secondary antibodies could aid in the protein detection process.
To probe for presence tubulin in protein samples by western blot you use a anti tubulin monoclonal antibody. Which of the following secondary antibody should be used? one produced by a sheep immunized with goat antibodies. one produced by a donkey immunized with rabbit antibodies one produced by a goat immunized with mouse antibodies one produced by a frog immunized with hamster antibodies
类 Protein Specific competitor Mutant/non competitor Add reaction components + +. Probe Antibody Supershift 美美美 Shift Free Probe - Gel separation of complexes Detection of labeled probe Name the experiment shown above and briefly describe how it is set up as well as the role of each component in that setup. What is it used for?
Have a look at the results in this SDS-PAGE gel. A MW ladder is shown. In the "control" lane, a sample of recombinant protein "LBT3" was loaded. Lane A shows proteins that have been prepared from leukocytes from a normal, healthy individual. Lanes B, C, D, E and F show protein prepared from leukocytes from individuals with lymphoma. What is the best explanation for the result shown for patient D? 200 150 100 75 50 37 20 Weight, kDa MW ladder Control A
With regard to the experiment described in Figure shown, Explain why an antibody was used to remove the bacteria thatwere not transformed. What would the results look like, in allfive cases, if the antibody/centrifugation step had not beenincluded in the experimental procedure?
Why is it not advisable to use adhesive mixtures if protein histological inevstigations are contemplated.
The technique used to determine protein type or kind of protein in a membrane is called (type meaning for instance, peripheral or transmembrane protein, not a specific protein) thin layer chromatography with a protein specific antibody protein labeling with lactoperoxidase and radioactive iodine hydropathy with protein labeling SDS-PAGE with Western blot and protein specific antibody
This is an SDS-PAGE of an antibody purification sample with IgG seperated from a Bovine Calf serum. Would you be able to describe the bands that are appearing and why it appeared on the gel this way? As well, a western blot was done after the SDS-PAGE and the bands that appeared were at 50 kDa and 150 kDa for the IgG and two elution lanes. May you please explain?
Are the bands indicated in Step 6 (SDS-PAGE) likely visualized by western blot or by a general protein stain (such as Coomassie or silver)?
Cell line A was cultured in the absence and presence of KB9520 or PPT. You then lyse the cells and fractionate them, generating membrane, cytosolic and nuclear protein fractions of the whole cell lysate. Western blots were then run using antibodies against ER (alpha) and ER (beta) for each treatment, and include different lanes for the membrane, cytosolic and nuclear protein fractions. Draw the expected results for these western blots and briefly discuss the expected differences.
You have the following reagents available Rat anti-Keratin 8 antibody specific for mouse Keratin 8, Rabbit polyclonal antibody against mouse keratin 5 and antifade reagent with DAPI to stain DNA. Both primary antibodies work best at 1:500 dilution. A) What additional reagents would you need to perform immunostaining of frozen sections of mouse thymus tissue for Keratin 8 that is expressed in cortical thymic epithelial cells and Keratin 5 that is expressed in mouse medullary thymic epithelial cells? B) Create a staining protocol including all tubes and appropriate controls to stain 4 slides with frozen thymic sections. You will need 200ul of antibody staining solution for each slide.

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Compare and contrast ELISA and western blotting (immunoblotting) by placing the phrases to the technique that they describe. If a phrase describes both ELISA and western blotting, place it under Both.