Not available outside of the UK & Ireland.

Application

Use Papain for the complete proteolytic cleavage of proteins, limited hydrolysis of native immunoglobulins, and tissue dissociation (together with collagenase, esterase, and trypsin). The enzyme solubilizes integral membrane proteins and produces glycopeptides from purified proteoglycans. The addition of cysteine (approximately 0.5% [w/v]) is essential for enzyme activity.

Papain has been used in the digestion of various brain cells.

Biochem/physiol Actions

Papain exhibits proteolytic activity against amide links, amino acid esters, peptides, proteins. It mainly cleaves peptide bonds containing amino acids such as lysine, arginine and residues succeeding phenylalanine. It can catalyze several reactions, such as hydrolysis, transferase action, specificity and acyl-enzyme intermediate.

Features and Benefits

Inhibitors: SH-blocking reagents, iodoacetic acid, iodoacetamide, TPCK, TLCK, leupeptin, a2-macroglobulin, E-64, PMSF, and antipain, Hg2+, and other heavy metals

General description

Papain is a cysteine protease of the papain family. It is a single chain protein. The molecular weight of papain is 23 kDa. Papain is composed of two structural domains and a cleft between them, which consists of the active site.

Other Notes

For life science research only. Not for use in diagnostic procedures.

Physical form

Suspension, crystalline, nonsterile

Preparation Note

Working concentration: 0.05 to 0.5 mg/ml

Storage and Stability

Store at 2 to 8 °C. (a decrease in activity of 20% may occur within 6 months)