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Isoelectric point. The isoelectric point (pI, pH (I), IEP), is the pH at which a molecule carries no net electrical charge or is electrically neutral in the statistical mean. The standard nomenclature to represent the isoelectric point is pH (I). [1] However, pI is also used. [2] For brevity, this article uses pI.
Protein precipitation. Protein precipitation is widely used in downstream processing of biological products in order to concentrate proteins and purify them from various contaminants. For example, in the biotechnology industry protein precipitation is used to eliminate contaminants commonly contained in blood. [1]
The two dimensions that proteins are separated into using this technique can be isoelectric point, protein complex mass in the native state, or protein mass. [citation needed] The separation by isoelectric point is called isoelectric focusing. Thereby, a pH gradient is applied to a gel and an electric potential is applied across the gel, making ...
Isoelectric focusing (IEF), also known as electrofocusing, is a technique for separating different molecules by differences in their isoelectric point (pI). [1][2] It is a type of zone electrophoresis usually performed on proteins in a gel that takes advantage of the fact that overall charge on the molecule of interest is a function of the pH ...
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 ] Besides detecting the proteins, this technique is also utilized to visualize, distinguish, and quantify the ...
The isoelectric point is the pH at which a compound - in this case a protein - has no net charge. A protein's isoelectric point or PI can be determined using the pKa of the side chains, if the amino (positive chain) is able to cancel out the carboxyl (negative) chain, the protein would be at its PI.
Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. [1] Although over 500 amino acids exist in nature, by far the most important are the 22 α-amino acids incorporated into proteins. [2] Only these 22 appear in the genetic code of life. [3][4]
Ubiquitin is a small (8.6 kDa) regulatory protein found in most tissues of eukaryotic organisms, i.e., it is found ubiquitously. It was discovered in 1975 [1] by Gideon Goldstein and further characterized throughout the late 1970s and 1980s. [2] Four genes in the human genome code for ubiquitin: UBB, UBC, UBA52 and RPS27A.