Technology
Affinity Chromatography
A chromatographic separation technique based on the ability of proteins to bind specific ligands reversibly.
Loading
Loading
Search products, companies, tests, and guides — go from query to quote request in one place.
Technology
A chromatographic separation technique based on the ability of proteins to bind specific ligands reversibly.
Technology
An electrophoresis procedure, in which a sample is introduced into a capillary tube and the components are separated by the application of high voltage. Due to the large surface to volume ratio, cooling is more efficient, allowing use of higher voltages. As a result, separation occurs more quickly and sensitivity is increased. The technique allows for separation of proteins, nucleic acids, and carbohydrates.
Technology
A molecular genetic technique that combines chromatin immunoprecipitation (ChIP) with massively parallel DNA sequencing to map the binding sites of DNA-associated proteins in a sample of cells. First, crosslinked protein-DNA complexes are isolated using ChIP. Next, the crosslinks are broken, the proteins are removed and the purified DNA is modified with adaptor oligonucleotides to facilitate massively parallel DNA sequencing. Following sequencing, the DNA sequences that are obtained can be mapped to their genomic locations.
Technology
A technique that utilizes immunoprecipitation to find protein-DNA interactions in a biological sample. First, the sample is treated causing the formation of protein-chromatin crosslinks. Then, the sample is sheared to separate individual protein-DNA complexes. Finally, an antibody directed against a protein of interest is applied and the protein-DNA complexes are immunoprecipitated.
Technology
A molecular biology technique used to detect the interaction of a DNA binding protein with its cognate binding sequence. Labeled DNAs were reacted with crude cell extracts and the complexes are run through a non-denaturing polyacrylamide gel. The migration of the labeled DNA through the gel will be slower by being bound. This shift in electrophoretic mobility indicates functional binding between the protein and the DNA.
Technology
Gel electrophoresis is a method of separating large molecules (such as DNA fragments or proteins) from a mixture of similar molecules by electrophoretic filtration through a gelatinous matrix. Subject to an electric field, each molecule in the sample mixture migrates through the matrix at a different rate, depending mainly on electrical charge and size, resulting in spatial separation within the matrix of each molecular species in the sample mixture. Agarose and acrylamide in a cylindrical tube or slab gel are commonly used media for electrophoresis of proteins and nucleic acids.
Technology
A method for the detection of proteins or antigens on samples of cells that are grown in monolayers or in suspension and deposited on slides using antibodies or other biomolecules that bind the target and can be visualized through a chemical process.
Technology
An enhancement of immunoelectrophoresis in which a series of post-electrophoretic gel slabs are layered with cellulose-acetate gels saturated with specific antibodies. The resulting antigen-antibody complexes fixed on the second gel may then be stained, allowing sensitive and specific qualitative visual identification of paraproteins by electrophoretic position. It can be used to identify specific proteins in the blood or urine. It has greatest application in the identification and monitoring of monoclonal proteins that are produced in conditions like Waldenstom's macroglobulinaemia and multiple myeloma.
Technology
An analysis of DNA or protein to detect the presence and/or location of methyl groups.
Technology
Analysis using microarray technology (e.g., cDNA arrays to see gene expression or protein microarrays to profile the pattern of proteins).
Technology
Analytical and separative procedures in which molecules, particularly proteins or nucleic acids, are separated by their different electrophoretic mobilities in a hydrated gel. The gel suppresses convective mixing of the fluid phase through which the electrophoresis takes place and contributes molecular sieving. For proteins, commonly carried out in the presence of the anionic detergent sodium dodecylsulphate (SDS). SDS denatures proteins so that noncovalently associating sub unit polypeptides migrate independently and by binding to the proteins confers a net negative charge roughly proportional to the chain weight.
Technology
Separation of protein fractions by precipitation, chromatography, or other methods.