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The Principle Of Western Blot

Western blotting was performed by Towbin et al. 1979, a widely used method for protein analysis. It can be used for both qualitative and semi-quantitative protein analysis.

To achieve the western blot, there are three elements that separate the proteins based on their size, transfer the proteins to a solid buffer, and label the proteins of the primary and secondary antibodies for visualization. You can visit some companies like bosterbio to get more information and services of western blot.

The Principle of Western Blot

Western blotting was performed using polypropylene gel electrophoresis. With SDS-PAGE, protein samples can be separated and transferred to a solid buffer such as a nitrocellulose (NC) membrane or polyvinylidene difluoride (PVDF).

The solid support can absorb protein and leave its biological activity unchanged. The solid support membrane that is transferred is called a stain and is treated with a protein solution to block the hydrophobic binding site on the membrane.

The membrane is treated with antibodies (primary antibodies) to the target protein. Only the protein tested can specifically bind to primary antibodies to form antigen-antibody complexes.

After the primary antibody is washed and removed, only the position of the target protein will bind to the primary antibody. The membranes treated with primary antibodies were treated with labeled secondary antibodies after washing. After treatment, labeled secondary antibodies that bind to the primary antibody form an antibody complex that can indicate the location of the primary antibody as well as the location of the protein to be tested.