Answer:
C.The added epitope disrupts the function of the tagged protein
Explanation:
When an additional sequence is tagged to a protein to use comercial antibodies, there are several reasons why this procedure wouldn't work as expected (note that we're assuming the protein is being expressed but it's not possible to detect it).
For example, the sequence of nucleotide added to codify for the tagged epitope are removed during the RNA processing. In that case, the protein would be expressed without the epitope, so it would be impossible to localize it with the antibodies.
Also, it could be that the new epitope is affecting some way the protein folding, making it not functional. This way, it would be degraded by the cell so it wouldn't be detected.
Another possibility is that the epitope doesn't affects the protein folding nor its function, but during the folding ends up in a conformation that makes it inaccesible for the antibody.
In summary, the way as the possible answers to this question are shown, the correct option seems to be C:<em> The added epitope disrupts the function of the target protein.</em>
Answer: They have a backbone
Explanation: Humans and fish are both vertebrates. Vertebrates are organisms with a backbone.
The relative time of divergence from a common ancestor can be estimated by comparing the nucleotide/protein sequence.
<h3>What is sequence homo-logy?</h3>
In molecular biology, sequence homo-logy means the degree of similarity between sequences due to a common ancestor.
A sequence is a given fragment of a single DNA strand where nucleotides are arranged in a specific linear order.
Divergence or separation between lineages is directly proportional to the level of sequence homo-logy.
In conclusion, the relative time of divergence from a common ancestor can be estimated by comparing the nucleotide/protein sequence.
Learn more about sequence homo-logy here:
brainly.com/question/9640986
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