No image available
No image available
Your request is being processed.
Register Forgot Password?
Home
Products
Applications
Contact Us

Protein Sample Preparation

Protein Sample Preparation

Initial protein extraction is often based on buffers containing mild non-ionic detergents, various salts, stabilizing agents, chelating agents, reducing agents, and protease inhibitors.

The choice of protease inhibitor may be critical to maintaining yield, structure, and function. Nucleases can be used to remove nucleic acids, and care should be taken to remove contaminants, including detergents that might interfere with downstream applications.

The preparation of protein samples is critical to the success of analytical methods such as mass spectrometry, 2-D gel electrophoresis, 1-D SDS-PAGE, trypsin digestion, and chromatography.

 

Cell Lysis and Protein Extraction

In general, gentle methods are employed when the sample consists of easily lysed, cultured cells or blood cells, whereas more vigorous methods are employed for the disruption of more robust bacterial or plant cells, or mammalian cells embedded in connective tissue.

Protein Enrichment and Sample Concentration

Capture and enrichment of a specific target protein helps to enhance detection signal strength. This strategy is effective both for proteins from natural sources as well as recombinant proteins.

Sample Clean-Up

Compounds such as nucleic acids, polysaccharides, and salts may interfere with electrophoretic separation. Sample cleanup may thus improve the quality of Western blotting.

Protein Quantitation

Quantitative analysis requires that all lanes in a gel are loaded with the same amount of total protein.




Feedback Form