Western Blotting and SDS-PAGE are techniques used to identify proteins. These experiments were combined in order to find specific protein inside an antibody. The techniques are aiming to accomplish the separation of protein in a given sample through SDS-PAGE (also known as electrophoresis), and identification of different proteins in a specific organism by the use of antigens through Western Blotting (or protein immunoblot). In general, these experiments are used to localize the protein of interest by antibonding specificity and molecular mass. For this laboratory experiment in particular, students conducted the experiment properly by following the precautions and steps correctly. The group tracked a variety of stages in order to achieve the main …show more content…
From the results that were obtained, it shows how C (shrimp) has a higher concentration of myosin than A (Tuna) and B (Mahi). Tuna and Mahi muscle proteins are more closely related to each other than that of the shrimp. The bands are to keep track of the proteins, but since they are naked to the human eye, they need to be stained. They represent the concentration of myosin in each protein. The darker the bar the less concentration of myosin it contains. Each lane in the gel represents different proteins of animal species, the two that are the most similar to each other in this gel are A and B, where A represents Tuna and B represents Mahi. In the SDS-PAGE gel can be seen how A and B have more concentration of myosin in a certain area of the gel, as how C which represents shrimp has higher concentration in various places of the gel. Electrophoresis is the indicator of the protein’s size, to make the proteins transferable to a Western blotting membrane. Which makes the charged molecules migrate in an electric field to the opposite charge electrode. Molecules separate when they migrate through the gel for the reason that they travel at different