The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Approximately 5000 Units/mg material.
The spectrophotometric assay to determine the activity of trypsin measures the increase in absorbance at 253 nm due to N-a-benzoyl arginine as it is cleaved from N-a-benzoyl arginine ethyl ester, with the concomitant formation of ethanol.
Trypsin catalyzes the cleavage of peptide bonds in proteins at the carboxyl side of arginine and lysine residues, except when either is followed by a proline residue. Trypsin is commonly used to remove adherent cells during cell culture manipulations carried out in vitro.
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Shipped at 4°C. Store at -20ºC.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
复溶This product should ideally be re-desiccated under vacuum over silica gel.
Dissolves readily at 1mg/mL in 1 mM Hydrochloric acid, can be used in 67mM potassium phosphate buffer to assay for trypsin activity
Alpha-trypsin chain 2
Nonfunctional trypsin 1
Pancreatic trypsinogen III
Protease Serine 1
Protease serine 1 (trypsin 1)
Protease serine 2
Protease serine 2 (trypsin 2)
Protease serine 2 preproprotein
Protease serine 3
Protease serine 3 (mesotrypsin)
Protease serine 4 (trypsin 4 brain)
Serine protease 1
Serine protease 2
Serine protease 3
Serine protease 4
功能Has activity against the synthetic substrates Boc-Phe-Ser-Arg-Mec, Boc-Leu-Thr-Arg-Mec, Boc-Gln-Ala-Arg-Mec and Boc-Val-Pro-Arg-Mec. The single-chain form is more active than the two-chain form against all of these substrates.
疾病相关Defects in PRSS1 are a cause of hereditary pancreatitis (HPC) [MIM:167800]; also known as chronic pancreatitis (CP). HPC is an autosomal dominant disease characterized by the presence of calculi in pancreatic ducts. It causes severe abdominal pain attacks.
序列相似性Belongs to the peptidase S1 family. Contains 1 peptidase S1 domain.
翻译后修饰Occurs in a single-chain form and a two-chain form, produced by proteolytic cleavage after Arg-122.