SERVA Electrophoresis
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50 years of experience in the supply of quality reagents at SERVA provides expertise in manufacture, development and distribution of products worldwide. This know-how is the platform for outstanding customer service - all you need to succeed. Our mission is to bring innovative products to the life sciences market, meeting our customers needs. Technical competence and total quality management are the basis for continuous improvement. We pursue the highest standards in product quality, workplace safety and responsibility for the environment we live in. We dedicate our capacity and integrity to guarantee consistent product performance and continuity of supply. We are certified for ISO 9001:2000.
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![Maltosides](https://www.clinisciences.com/es/upload/thumbs/bandeau3-wns9m7yn-fkHjf5F3-c5db53.png)
Maltosides
Dodecyl Maltoside is usually the first choice for working with membrane proteins and G protein-coupled receptors (GPCRs). Otherwise known as DDM, the detergent is part of the most popular family of detergents.
Alkyl glycoside detergents are mostly derived from maltose or glucose. These detergents are mild and non-denaturing because they disrupt protein-lipid and lipid-lipid interactions rather than protein-protein interactions. The sugar serves as a polar head group with a non-polar alkyl chain attached. The hydrophilic head groups offer ample strength to extract proteins while still providing the capability to stabilize proteins in solution and promote crystal growth. These detergents are also well chronicled for their ability to stabilize other large macromolecules as well.
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These micelle-producing detergents are perfect for both protein extraction and maintaining solubility and stability in aqueous environments. Glucoside detergents have a long track record of crystallizing membrane proteins for x-ray crystallization studies or creating the necessary stable tertiary structure for NMR work. Anatrace detergents are the most cited detergents in journal articles pertaining to structure and function of membrane proteins.
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