Papain is a cysteine protease, found in Carica papaya. It is composed of a single polypeptide chain containing three disulfide bridges and a sulfhydryl group.
Papain from papaya latex has been used:
- to digest carotid artery smooth muscle cells
- in dissecting solutions
- to produce Fab fragments of antibodies
- for cell dissociation since it has been shown to be more effective and less damaging with certain tissues
- in the enzyme cocktail for dissociating human fetal retinal tissue
- to digest chondrocytes/scaffold cultures for total DNA quantification for cell proliferation
- as a supplement in neurobasal medium to produce retinal cell suspensions
Used to produce Fab fragments of antibodies. Also used for cell dissociation since it has been shown to be more effective and less damaging with certain tissues.
25 mg in poly bottle
50, 100, 500 mg in glass bottle
1, 5 g in glass bottle
Package size based on protein content
Papain with wide specificity, cleaves peptide bonds of basic amino acids, leucine or glycine. It also hydrolyzes esters and amides. Papain is considered to digest protein substrates more broadly than the pancreatic proteases. Papain is commonly used in cell isolation procedures as it is highly efficient and less harmful than other proteases on certain tissues. The use of papain is known to yield more viable smooth muscle cells, retaining the cell′s sensitivity to stimulants. Papain papaya latex has antifungal activity against C. albicans and is a cysteine protease.
- The pH optimum is 6.0-7.0
- Papain hydrolyzes esters and amides
A cysteine protease that cleaves peptide bonds of basic amino acids, leucine, or glycine.
pH optimum 6.0-7.0
Also hydrolyzes esters and amides.
One unit will hydrolyze 1.0 micromole of N-alpha-benzoyl-L-arginine ethyl ester (BAEE) per minute at pH 6.2 at 25 deg C.
Lyophilized powder containing sodium acetate