Immunostaining was used to investigate the expression of the Fibrillin 1 gene in muscle fibres. Twoantibodies were used, Antibody A binds to a muscle membrane protein that is unrelated to Fibrillin.Antibody B binds to the N terminus of Fibrillin 1, whilst Antibody C binds to the C terminus of Fibrillin 1.What is the best explanation for the staining pattern see in the following figureAntibody BAntibody AAntibody C A point mutation in the fibrillin gene introduced a stop codon in the proteinA gene translocation has removed the N terminus of the proteinA gene translocation has removed the chromosome encoding the fibrillin geneA tuncation mutation has removed the central region of the proteinThe C and N termini of the Fibrillin protein are unchanged by the mutationA point mutation in the fibrillin gene has changed an amino acid in the proteinA point mutation in the fibrillin gene has introduced a start codon in the proteinA truncation mutation has removed the N terminus of the proteinA point mutation in the fibrillin gene has resulted in the removal of a stop codonBoth the N and C termini regions of the protein have been deleted by a mutationA point mutation in the fibillingene has led to it not being expressed

Immunostaining is a process of staining proteins by antibodies that are covalently linked to an…

Answered: Immunostaining was used to investigate…

Curren'S Math For Meds: Dosages & Sol

11th Edition

ISBN:9781305143531

Author:CURREN

Publisher:CURREN

Chapter16: Adult And Pediatric Dosages Based On Body Surface Area

Section: Chapter Questions

Problem 7.2P

See similar textbooks

Similar questions

Protein analysis by gel electrophoresis a). Using the gel image provided to calculate the electrophoretic relative mobility as a ratio of the distance of protein migration to the distance of the tracking dye migration (See Appendix B). If your dye front is not visible, measure the mobility relative to the bottom edge of the resolving gel. Include a labeled print-out of your gel image with your report. b). Plot log MW of the protein markers and commercial myoglobin vs. mobility. Determine the molecular weight of myoglobin obtained after the final purification step (Sample E) from the equation of the line. Submit a copy of your graph along with the gel image. c). Compare your sample E and commercial myoglobin with the ladder. Summary your results. order of sample (left to right) is : A B C D blank E blank Commercial Myoglobin Molecular Ladder
A variety of organic chelating ligands have been synthesized to tightly coordinate radioactive metal cations to identify and treat malig- nancies by coupling the metal complex to a polypeptide linker attached to a monoclonal antibody that binds specifically to a cell surface re- ceptor. One such metal complex is illustrated in the diagram on the right. The radioactive Cu-64 cation is tightly coordinated by the che- lating ligand that is, in turn, conjugated to a peptide linker attached to a monoclonal antibody. (The antibody is not shown in this diagram.) When coupled to a specifically designed monoclonal antibody, the complex binds specifically to somatostatin receptors that are ex- pressed on the surface of neuroendocrine tumors. Subsequently the entire complex with the receptor is internalized, i.e., passed into the cytoplasm, where the radioactive metal cation kills the malignant cell. 1. CH3 HN NHNH HN NHNH HN Но НО NH HN S-S HN Но NH NH HN -NH HN- H2N OH NH ) Write the three…
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.
Fluorescence-activated cell sorting (FACS) is a powerful technique for separating cells according to their content of particular molecules. For example, a fluorescence-labeled antibody specific for a cell-surface protein can be used to detect cells containing such a molecule. Suppose that you want to isolate cells that possess a receptor enabling them to detect bacterial degradation products. However, you do not yet have an antibody directed against this receptor. Which fluorescence-labeled molecule would you prepare to identify such cells?
Which of the following statements best describes the function of SDS in western blotting? Select one: A. It gives proteins a net positive charge. B. It can solidify polyacrylamide gel. C. It can form a colored product with proteins. D. It allows the transfer of proteins from polyacrylamide gel to nitrocellulose membrane. E. It can linearize protein molecules.
Which of the following statements best describes the function of SDS in western blotting? Select one: A. It can solidify polyacrylamide gel. B. It allows the transfer of proteins from polyacrylamide gel to nitrocellulose membrane. C. It can form a colored product with proteins. D. It can linearize protein molecules. E. It gives proteins a net positive charge. O O O O
In a particular species, the gene for the kappa light chain has 200 V segments and 4 J segments. In the gene for the lambda light chain, this species has 300 V segments and 6 J segments. If only the antibody diversity arising from somatic recombination is taken into consideration, how many different types of light chains are possible?
A chain of biochemical events is responsible for Aequorea victoria turning green. Firstly, the protein aequorin converts chemical energy into blue light. A second protein, known as GFP (green fluorescent protein), absorbs the light. Aequorin is a 21 kDa protein with a pI of 4.5 that generates blue light from an attached non-protein chromophore. GFP is a 27 kDa protein with a pI of 6.2. In order for it to fluoresce, 3 amino acids undergo a remarkable reaction when they are folded in the right way. Aequorin does not absorb light in the visible range, and GFP absorbs light at 395 nm and 475 nm. 1. Sketch what you would see if you ran a mixture of aequorin and GFP over a size-exclusion column. In your sketch, include absorbance data at 280, 395, and 475 nm.
Briefly compare the composition of DNA versus that of RNA. Answer the following questions pertaining to the experimental use of green fluorescent protein (GFP). What is the main advantage of GFP in terms of protein visualization in cells/organisms? Which microscope technique is used to visualize GFP-tagged proteins?
An important mechanism for generating diversity in immunoglobulin light chain V-region sequences is based on the fact that the RAG recombinase generates hairpin structures, rather than blunt ends, at the cleavage sites between the recombination signal sequences and the coding sequences. Explain how this mechanism generates diversity at the junctions.
Cre-Lox system is used for site-specific modification of DNA for genetic engineering applications. The reporter gene construct shown below is used to test the Cre-Lox system. Cells are transfected with the construct shown below and the activity of the constructs is determined by visualizing the cells with a fluorescence microscope. Match the following conditions with the expected cell observations. Hint: Make sure you note the position of the Start and Stop. The GFP and RFP genes shown do not have start codons. Cre/Lox Reporter Gene ATG LoxP CMV-Pro A. No Expression GFP Stop B. GFP Only LoxP Absence of Cre Cells treated with drug that induces expression of Cre RFP C. RFP Only A. Image A B. Image B C. Image C D Image D express ? D. RFP and GFP
Consider the leucine transporter. Would Vmax and/or Kt change if you added a Na+ ionophore to the assay solution containing Na+? Explain.

SEE MORE QUESTIONS

Recommended textbooks for you

Curren'S Math For Meds: Dosages & Sol

Nursing

ISBN:

9781305143531

Author:

CURREN

Publisher:

Cengage

Basic Clinical Laboratory Techniques 6E

Biology

ISBN:

9781133893943

Author:

ESTRIDGE

Publisher:

Cengage

Curren'S Math For Meds: Dosages & Sol

Nursing

ISBN:

9781305143531

Author:

CURREN

Publisher:

Cengage

Basic Clinical Laboratory Techniques 6E

Biology

ISBN:

9781133893943

Author:

ESTRIDGE

Publisher:

Cengage

SEE MORE TEXTBOOKS