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the quantity of precipitate, which forms after the reagent antibody (precipitin) has incubated with the sample and reacted with its respective antigen to form an insoluble aggregate.

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What are the differences between immunoprecipitation and western blot techniques in protein analysis?

Immunoprecipitation is a method used to isolate a specific protein from a mixture, while western blot is a technique used to detect and analyze proteins based on their size and abundance. Immunoprecipitation involves using antibodies to pull out a specific protein, while western blot involves separating proteins by size and then detecting them with antibodies.


What are the differences between western blot and immunoprecipitation techniques in protein analysis?

Western blot and immunoprecipitation are both techniques used in protein analysis, but they have some key differences. In western blotting, proteins are separated by size using gel electrophoresis and then transferred to a membrane for detection with specific antibodies. This technique is used to detect and quantify a specific protein in a sample. On the other hand, immunoprecipitation involves using antibodies to pull down a specific protein from a complex mixture. This technique is used to isolate and purify a specific protein or protein complex from a sample for further analysis. Overall, western blotting is used to detect and quantify proteins, while immunoprecipitation is used to isolate and purify specific proteins for further study.


What has the author Philippe Collas written?

Philippe Collas has written: 'Chromatin immunoprecipitation assays' -- subject(s): Chromatin, Laboratory manuals


How much SUMO1-Antibody should be used in immunoprecipitation using Protein AG to collect sumoylated proteins?

You should start with 1 or 3 micrograms of antibody.


What is the definition of the term immuniprecipitation?

The term immunoprecipitation refers to the technique of precipitating protein antigens out of a solution using an antibody that is designed to bind itself to that particular protein.


How does chromatin immunoprecipitation work to identify protein-DNA interactions?

Chromatin immunoprecipitation (ChIP) is a technique used to study protein-DNA interactions. It involves cross-linking proteins to DNA, breaking the DNA into small fragments, and then using an antibody to pull down the protein of interest along with any DNA it is bound to. The DNA fragments can then be analyzed to identify the specific regions of the genome where the protein is interacting with DNA.


What are some alternative methods to western blot for protein analysis?

Some alternative methods to western blot for protein analysis include enzyme-linked immunosorbent assay (ELISA), mass spectrometry, immunoprecipitation, and protein microarrays. These techniques offer different advantages and may be more suitable for specific research needs.


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In this parallelogram the measure of b is twice the measure of a what is the measure of B is twice the measure of A What is the measure of A?

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