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Results for "

autolysis

" in MedChemExpress (MCE) Product Catalog:

By Targets:	Biochemical Assay Reagents (2) Endogenous Metabolite (1)

Inhibitors & Agonists

Biochemical Assay Reagents

Cat. No.	Product Name	Target	Research Areas	Chemical Structure

HY-129047C

TPCK-treated Trypsin	Biochemical Assay Reagents	Others
TPCK-treated Trypsin is a trypsin whose activity is inhibited by tosyl phenylalanyl chloromethyl ketone. TPCK-treated Trypsin reduces autolysis and nonspecific proteolysis during experiments, exhibits stability in storage and handling. TPCK-treated trypsin can be used in proteomics research .

HY-P2823

Trypsinogen	Endogenous Metabolite Biochemical Assay Reagents	Others
Trypsinogen, a proenzyme synthesized in the pancreas, is activated to form trypsin by enterokinase upon reaching the small intestine lumen, where it opens a hexapeptide bond at the Lys6 - Ile7 junction, leading to the production of the active enzyme. This single polypeptide chain, composed of 229 amino acids and stabilized by six disulfide bridges, further autocatalytically converts additional trypsinogen into trypsin, which is initially present as β-trypsin before undergoing autolysis at the Lys131 - Ser132 site to form α-trypsin. As a serine protease, trypsin features His46 and Ser183 at its active site and exhibits optimal enzymatic activity at a pH range of 7 to 9.

Cat. No.	Product Name	Type

HY-P2823

Trypsinogen	Biochemical Assay Reagents
Trypsinogen, a proenzyme synthesized in the pancreas, is activated to form trypsin by enterokinase upon reaching the small intestine lumen, where it opens a hexapeptide bond at the Lys6 - Ile7 junction, leading to the production of the active enzyme. This single polypeptide chain, composed of 229 amino acids and stabilized by six disulfide bridges, further autocatalytically converts additional trypsinogen into trypsin, which is initially present as β-trypsin before undergoing autolysis at the Lys131 - Ser132 site to form α-trypsin. As a serine protease, trypsin features His46 and Ser183 at its active site and exhibits optimal enzymatic activity at a pH range of 7 to 9.

Trypsinogen

Biochemical Assay Reagents

Trypsinogen, a proenzyme synthesized in the pancreas, is activated to form trypsin by enterokinase upon reaching the small intestine lumen, where it opens a hexapeptide bond at the Lys6 - Ile7 junction, leading to the production of the active enzyme. This single polypeptide chain, composed of 229 amino acids and stabilized by six disulfide bridges, further autocatalytically converts additional trypsinogen into trypsin, which is initially present as β-trypsin before undergoing autolysis at the Lys131 - Ser132 site to form α-trypsin. As a serine protease, trypsin features His46 and Ser183 at its active site and exhibits optimal enzymatic activity at a pH range of 7 to 9.

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