USP grade Trypsin source from Swine / Bovine pancreas
Trypsin is a kind of serine proteolytic enzyme, with molecular weight of 23300 dalton, and is a single peptide chain composed of 223 amino acid residues. With rigorous specificity, the trypsin specifically acts on the peptide linkage constituted by the basic amino acid arginine and leucine. Enzyme easily autolyzes by itself, and its activation also reduces or loses gradually. It is easily soluble in the water, but insoluble in trichloromethane, ethanol, ether and glycerin, and the optimum PH is 8.0~9.0. When the PH is 1.8, it is hardly deactivated when boiled for a short time; if the salt is added into the hot solution, the protein will precipitate, and the enzyme action of filtrate cannot be seen, and Ca2+ plays the role in protecting and activating the trypsin. The high purity Trypsin is purified by re-crystallization, and then by Ion Exchange chromatography and ultra-filtration.
For cell culture, hydrolyze the proteins between cells and disperse them.
Activity ≥ 2500 USP U/mg
Source: Bovine Pancreas
|White or almost white lyophilized powder
|500,000USP Trypsin Units is soluble in 10ml of water and in 10ml of saline TS.
|Loss on drying
|No more than 5.0%
|Residue on Ignition
|No more than 2.5%
|No more than 50 USP units/mg powder
|Trypsin ≥ 2500USP units/mg powder
|white crystalline powder
|A) A purple color develops within 3 minutes
B) No purple color develops with in 3 minutes
|Appearance of solution
|Solution S is not more opalescent than reference suspension Ⅲ
|1) 280nm : 13.5 ~ 16.5
2) 250nm : not more than 7.0
|Not more than 1µg/0.2µkatal
|Loss on drying
|Not more than 5%
|Limit of Chymotrypsin
|Not more than 1%
|Total viable aerobic count
|Not less than 0.5µkatal /mg, calculated on the dried basis.
Store in an airtight container, at a temperature of 2°C to 8°C.
|Specification Activity:Trypsin>=2500U/mg, Chymotrypsin<=2%; Standard USP43; CAS NO. 9002-07-7