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A general dot blot protocol involves spotting 1–2 microliters of a samples onto a nitrocellulose or PVDF membrane and letting it air dry. Samples can be in the form of tissue culture supernatants, blood serum, cell extracts, or other preparations. [4]
A reverse phase protein lysate microarray (RPMA) is a protein microarray designed as a dot-blot platform that allows measurement of protein expression levels in a large number of biological samples simultaneously in a quantitative manner when high-quality antibodies are available. [1]
Protein:protein interaction studies; Colony blot, dot blot, Western blot and ELISA; Screening for positive expression clones; Immunocytochemistry and Immunohistochemistry; Protein localization and targeting studies; Because the Strep-tag is capable of isolating protein complexes, strategies for the study of protein-protein interactions can also ...
In a dot blot, macromolecules are applied directly to the matrix. Macromolecules can also be separated and transferred via gel electrophoresis. [1] One of the most common blotting matrices for protein analysis is nitrocellulose, which has a high affinity for proteins due to hydrophobic interactions. However, proteins with low molecular weight ...
Former protocols were hampered by the need for large amounts of proteins and their susceptibility to degradation while being isolated. Southwestern blotting was first described by Brian Bowen, Jay Steinberg, U.K. Laemmli, and Harold Weintraub in 1979. [2] During the time the technique was originally called "protein blotting".
A southwestern blot is based on Southern blot and is used to identify and characterize DNA-binding proteins by their ability to bind to specific oligonucleotide probes. [2] The proteins are separated by gel electrophoresis and are subsequently transferred to nitrocellulose membranes similar to other types of blotting.
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