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Proteinase K is a highly reactive nonspecific serine protease that belongs to the subtilisin family of proteins. It cleaves at the carboxylic acid side of aliphatic, aromatic, or hydrophobic amino acids. Proteinase K is capable of inactivating RNases and DNases and is used in the isolation or preparation of high molecular weight nucleic acids. Proteinase K is also useful for helping to characterize enzymes, due to its cleavage specificity. This enzyme was designated proteinase K because of its ability to hydrolyze keratin. Proteinase K is stable in a wide variety of detergents and buffer salts and at various temperatures and pH. The isoelectric point of proteinase K is 8.9.

Proteinase K is a highly reactive nonspecific serine protease that belongs to the subtilisin family of proteins. It cleaves at the carboxylic acid side of aliphatic, aromatic, or hydrophobic amino acids. Proteinase K is capable of inactivating RNases and DNases and is used in the isolation or preparation of high molecular weight nucleic acids. Proteinase K is also useful for helping to characterize enzymes, due to its cleavage specificity. This enzyme was designated proteinase K because of its ability to hydrolyze keratin. Proteinase K is stable in a wide variety of detergents and buffer salts and at various temperatures and pH. The isoelectric point of proteinase K is 8.9.

TCEP-HCl is an odorless reducing agent suitable for protein applications and in the preparation for electrophoresis. TCEP is water soluble, is stable in a variety of solutions and is particularly useful in the labeling of cysteine residues with maleimides, preventing the cysteines from forming disulfide bonds. As a reducing agent, TCEP has many other desirable features.

GoldBio Tris has the highest purity available on the market. Short for Tris (hydroxymethyl) aminomethane (THAM), Tris is an organic compound often used in buffer solutions such as TAE or TBE for electrophoresis gels. Tris is highly soluble in water and is useful in the pH range 7.0-9.0 and is also used in the preparation of Laemmli buffer, one of the most common SDS-PAGE buffers. In addition, it can also be used for many custom running and loading buffers, most often with glycine and SDS.

Vancomycin hydrochloride is a member of the glycopeptide antibiotic class derived from Streptomyces orientalis. It is effective against gram-positive bacteria and used in studies of antibiotic resistance bacteria and nanoparticle transport studies. Exhibiting low toxicity to plants, vancomycin is suitable for plant selection and prevention of bacterial contamination in plant cell culture applications.

5-Bromo-4-chloro-3-indolyl β-D-galactopyranoside is most commonly known as X-Gal. X-gal is a histochemical substrate for β-galactosidase which cleaves X-Gal to yield an insoluble blue precipitate.

X-Gal is a mainstay in molecular biology cloning applications in which it is used to detect the activity of β-galactosidase. X-Gal is used to detect the insertion of foreign DNA into the lacZ region of a plasmid DNA. Insertion of DNA into the lacZ region results in the loss of β-galactosidase activity. Bacteria cells that retain active β-galactosidase will result in characteristic blue colonies. Successful disruption of the lacZα gene disrupts the α-complementation of the β-galactosidase gene and the precipitate does not form, resulting in white colonies.

Many other applications also use X-Gal as a substrate to detect β-galactosidase activity. These include β-galactosidase -antibody linked immunoassays and immunohistochemistry, coliphage detection based on β-galactosidase induction and the detection of micrometastasis formation during tumor progession.