AG Scientific
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AG Scientific specializes in secondary metabolites derived from fermentation. Most of their products are antibiotics for gene selection, but the catalog also includes antimicrobial, antifungal, anti-cancer, antiviral, antiparasitic and immunosuppressive reagents.
Antibiotics:
AG Scientific, Inc. has developed a series of antibiotic screening agents, including Blasticidin S, G-418, Puromycin, Gentamycin, Kanamycin, Ampicillin, Streptomycin, Carbenicillin.
More recently, AG Scientific has partnered with pharmaceutical customers using CRISPR technology.
Anti-cancer:
The catalog includes secondary metabolites in the field of cancer such as rapamycin, FK-506, cyclosporine A.
Website : www.agscientific.com
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![Maltosides](https://www.clinisciences.com/en/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.
![](/upload/glucosides-xwk3jjbj-zSHx5CCk.jpg)
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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