In this chapter, we described co-immunoprecipitation as a method for identifying binding partners to a protein of interest. Asimpler variation of this method can also be used to isolate proteins of low abundance in a complex mixture.Arrange the steps in sequential order to use this technique for this purpose.First stepLast stepAnswer BankThe protein mixture is centrifuged, the supernatant is removed, and the pellet is washed.The antibody binds to the protein of interest. The antibody-protein complexes become insoluble.An antibody against the protein of interest is added to the mixture.Protein A beads are added to the mixture.

Co-immunoprecipitation (Co-IP) is a laboratory technique used to identify and characterize…

Answered: In this chapter, we described…

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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Following is the data and notice that it is a terrible idea to culture hMSCs longer than 10 days. You’re strongly Days # cells0 50001 75002 125003 125004 218005 287006 530007 1143008 1653009 19200010 19200011 11680012 8950013 8830014 78300 Part1 You are working for a start-up that is pursuing a clinical trial. The trial involves grafting hMSCs intopatients suffering from interveterbral disc disease using a degradable polymer scaffold. You are going to 3Dprint a porous cylindrical scaffold that is 2 cm in radius and 1 cm in height (matching the dimensions of adegenerated disc). Assume a porosity of 50%. You will fill available volume of the scaffold with hMSCs at adensity of 1 million cells per cm3. Based on the data above, what starting number of cells will you use andhow long will it take you to get enough cells for the trial? Part2The trial is a failure (patients did not report any reduction in back pain). Your team wants to try againusing 85% hMSCs and 15% nucleus pulposus cells .…
hypothetically speaking, if a rapid test was being made to detect RSV (RSV antigen), the conjugate pad would contain the anti-RSV antibody conjugated with HRP. The test line would be the anti-RSV antibody. What would be a suitable control antibody to use?
The substrate For the secondary antibody used in the lab for western blothing is : TMB TritonX-100 tween BCIP/NBT
For an Immunoprecipitation experiment: What is the function of the IP-2 tube in this experiment?
Describe three examples of how antibodies are used as reagents in cell biology and molecular biology.
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).
1) SDS PAGE gels can be probed with NBT/BCIP to perform an immunoblot true/ false 2) the direction of migration of protiens through a matrix is due to most proteins in natur having a net negative charge true/false 3) PBST is a buffer that is used for blocking the membrane during immunoblotting. true/false 4) the buffer used during for transferring proteins to nitrocellulose methanol. true/false 7) The size of the pores of a polyacrylamide gel dcreases as concentrations of polyacrylamide increases. True or false 10) The secondary antibody used in laboratory for western blotting is conjugated to which enzyme A) Alkaline decarboxylase B) GAPDH C) Alkaline Phosphatase D) Horseeradish peroxide 13) In protien electrophroresis, what reagent present in the sample buffer is used to eliminate difference in the charge densities of protein A) SDS B) 2- mercaptoethanol C) Tris-HCL pH6.8 D) Tris- HCL PH 8.8
The substrate for the secondary antibody used in the lab for western blotting is: triton X-100 BCIP/NBT Tween TMB
Compared to an RNA Vaccine what additional steps does the information in DNA vaccine need to undergo before an antigenic protien is produced?
Answer question in the photo
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?
Why does the eliza with two antibodies incubate after adding the substrates?

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