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Affinity chromatography is a method of separating a biomolecule from a mixture, based on a highly specific macromolecular binding interaction between the biomolecule and another substance.
IMAC resins typically retain several prominent endogenous proteins as impurities. In E. coli for instance, a prominent example is FKBP-type peptidyl prolyl isomerase, which appears around 25 kDa on SDS-PAGE. These impurities can be eliminated using additional purification steps or by expressing the recombinant protein in a deficient strain of ...
An immunoassay (IA) is a biochemical test that measures the presence or concentration of a macromolecule or a small molecule in a solution through the use of an antibody (usually) or an antigen (sometimes).
In biology, the extracellular matrix (ECM), [1] [2] also called intercellular matrix (ICM), is a network consisting of extracellular macromolecules and minerals, such as collagen, enzymes, glycoproteins and hydroxyapatite that provide structural and biochemical support to surrounding cells.
Developmental psychobiology posed this question since the lack of knowledge about the precise coordination of all cells, even those not related anatomically, in space and time during the embryonic period does not allow us to understand what forces at the cellular level coordinate four very general classes of tissue deformation, namely: tissue ...
Fast protein liquid chromatography (FPLC) is a form of liquid chromatography that is often used to analyze or purify mixtures of proteins. As in other forms of chromatography, separation is possible because the different components of a mixture have different affinities for two materials, a moving fluid (the mobile phase) and a porous solid (the stationary phase).
The class I amidotransferase domain is made of the N terminal 206 residues of the enzyme, and consists of 12 beta strands and 5 alpha helices; the core of this domain is an open 7-stranded mixed beta sheet. Its catalytic triad includes Cys86, His181 and Glu183.
iCLIP [1] [2] [3] (individual-nucleotide resolution crossLinking and immunoprecipitation) is a variant of the original CLIP method used for identifying protein-RNA interactions, [4] which uses UV light to covalently bind proteins and RNA molecules to identify RNA binding sites of proteins.