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  2. Dithiothreitol - Wikipedia

    en.wikipedia.org/wiki/Dithiothreitol

    Dithiothreitol (DTT) is an organosulfur compound with the formula (CH(OH)CH 2 SH) 2. A colorless compound, it is classified as a dithiol and a diol . DTT is redox reagent also known as Cleland's reagent , after W. Wallace Cleland . [ 2 ]

  3. Western blot - Wikipedia

    en.wikipedia.org/wiki/Western_blot

    Western blot workflow. The western blot (sometimes called the protein immunoblot), or western blotting, is a widely used analytical technique in molecular biology and immunogenetics to detect specific proteins in a sample of tissue homogenate or extract. [1]

  4. Thermal shift assay - Wikipedia

    en.wikipedia.org/wiki/Thermal_Shift_Assay

    To reduce the workload, western blots could be replaced by SDS-PAGE gel polyhistidine-tag staining, provided that the protein has such a tag and is expressed in adequate amounts. FastPP can be used on unpurified, complex mixtures of proteins and proteins fused with other proteins, such as GST or GFP , as long as the sequence that is the target ...

  5. Lysis buffer - Wikipedia

    en.wikipedia.org/wiki/Lysis_buffer

    A lysis buffer is a buffer solution used for the purpose of breaking open cells for use in molecular biology experiments that analyze the labile macromolecules of the cells (e.g. western blot for protein, or for DNA extraction).

  6. Polyacrylamide gel electrophoresis - Wikipedia

    en.wikipedia.org/wiki/Polyacrylamide_gel...

    Western blotting is a process by which proteins separated in the acrylamide gel are electrophoretically transferred to a stable, manipulable membrane such as a nitrocellulose, nylon, or PVDF membrane. It is then possible to apply immunochemical techniques to visualise the transferred proteins, as well as accurately identify relative increases ...

  7. SDS-PAGE - Wikipedia

    en.wikipedia.org/wiki/SDS-PAGE

    Proteins of the erythrocyte membrane separated by SDS-PAGE according to their molecular masses. SDS-PAGE (sodium dodecyl sulfate–polyacrylamide gel electrophoresis) is a discontinuous electrophoretic system developed by Ulrich K. Laemmli which is commonly used as a method to separate proteins with molecular masses between 5 and 250 kDa.

  8. Bradford protein assay - Wikipedia

    en.wikipedia.org/wiki/Bradford_protein_assay

    Other interference may come from the buffer used when preparing the protein sample. A high concentration of buffer will cause an overestimated protein concentration due to depletion of free protons from the solution by conjugate base from the buffer. This will not be a problem if a low concentration of protein (subsequently the buffer) is used. [6]

  9. Immunoprecipitation - Wikipedia

    en.wikipedia.org/wiki/Immunoprecipitation

    Immunoprecipitation (IP) is the technique of precipitating a protein antigen out of solution using an antibody that specifically binds to that particular protein. This process can be used to isolate and concentrate a particular protein from a sample containing many thousands of different proteins.

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