TCI America Tris(hydroxymethyl)aminomethane [for Electrophoresis] T2516

Tris(hydroxymethyl)aminomethane [for Electrophoresis] / 2-Amino-2-(hydroxymethyl)-1,3-propanediol
In the field of biochemical research, buffering agents perform a very important function. The Tris buffers widely used today have a primary amino group and they are known to frequently cause inhibition problems in biological systems. Furthermore sufficient buffering power cannot be obtained under pH7.5.
Good and co-workers have developed buffers to overcome the above-noted defects and their superiority has been indicated by the Hill reactions. These buffers are referred to as Good's Buffers being named after the inventor.
[Characteristics]
1) Acid dissociation constant pKa is between 6~8.
2) High water solubility.
3) Low penetration through biomembranes.
4) Low base effect toward biological systems.
5) pKa is less affected by concentration, temperature and ion composition.
6) Low complexation ability with metal ions.
7) Chemically stable.
8) Low in absorption of visible and ultra-violet rays.
Composition and pH range

Tris(hydroxymethyl)aminomethane [for Electrophoresis] / 2-Amino-2-(hydroxymethyl)-1,3-propanediol
Electrophoresis is a technique which separates charged biomolecules based on the rate at which they migrate in an applied electrical field. In many cases, electrophoresis of proteins are performed using polyacrylamide gel electrophoresis (PAGE).1) For molecular weight estimation and purity determination of proteins, sodium dodecyl sulfate (SDS)-PAGE is frequently employed. SDS is a strong denaturant of proteins and is added to samples, gels, and buffer solutions for electrodes when proteins are separated with electrophoresis. As SDS not only denatures protein but also binds to the protein, when SDS is used in conjunction with a reducing reagent such as 2-mercaptoethanol to cleave disulfide bonds in the protein, and the protein is completely denatured, the amount of SDS bound is almost always proportional to the molecular weight of the protein. Resultantly, the protein is negatively charged. Therefore, the denatured protein can be separated by molecular weight independently of its structure and biological properties.
Laemmli's method is the most widely used system of SDS-PAGE.2) In this method, the separation and the stacking gel contain Tris-HCl and the upper and lower buffer reservoirs contain Tris-glycine. All components of the system contain SDS. The advantage of Laemmli's method is that it gives sharper bands in the final plate.1)