Trypsin, 100 mg
Storage temp. -20 °C
Transport temp. ambient temp.
CAS No. [9002-07-7]
excl. VAT. | 100 mg per Pack Qty.
Art. No. 5455.1
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A pancreatic serine protease with a specificity for peptide bonds between basic amino acids arginine or lysine and another non-specific amino acid.
Trypsin is frequently used to suspend cells which grow as monolayers on surfaces. Longer exposure to trypsin can damage cells, so that an inhibitor (serum or trypsin inhibitor from soya beans) should be added upon completion.
Trypsin ≥2500 USP-U/mg, cryst.
pH optimum 7.2-8.5.
One USP Unit will cause an increase in absorption (253 nm) per minute of 0.003 at 25 °C and pH 7.6 using BAEE as substrate.
One (international) Unit (U, 255 nm, BAEE, pH 8) is approx. 90 USP U.
One TAME Unit is approx. 20 USP Units.
One NF Unit is one USP Unit.
Ten „BAEE Units“ are approx. 3.3 USP Units.
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Enzyme: a neoclassical, Greek artificial word ενζυμου, énzymon, derived from εν-, en- (in-) and ζυμη, zýmé (yeast, sourdough, archaic)
Ferments: comes from the Latin fermentum (ferments, sourdough)
There are six classes in which all enzymes are classified according to the particular reaction they catalyse:
• Oxidoreductases (catalyse redox reactions)
• Transferases (transfer functional groups among substrates)
• Hydrolases (cleave bonds via addition of water)
• Lyases/Synthases (cleave or synthesise complex products out of basic substrates without cleavage of ATP)
• Isomerases (transform chemical isomers)
• Ligases/Synthetases (cleave or synthesise complex products out of basic substrates via cleavage of ATP)
|Appearance||beige to light brown hygroscopic powder|
|Activity||≥2500 USP-U/mg Trypsin|
|Residue on ignition||≤3,0 %|
|Loss on drying (60 °C)||<5 %|