Human Trypsin

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	Proteins Synonyms: TRY, TRY2, Anionic trypsinogen, Serine protease 2, Trypsin II, PRSS2, TRYP2 Biological Activity: 2.5 units per mg protein Source: Human Pancreas Purity: ≥ 95% by SDS-PAGE. Physical State: Salt-free lyophilized from 2 mM HCl. Manufacturer:  Athens Research & Technology	Article No. Size Price   16-19-032000-100UG 100 µg 330 € 16-19-032000-1MG 1 mg 1.650 € 16-19-032000-5MG 5 mg 6.250 € Please inquire for other vial sizes and custom vialing.

 

 

Produktdetails

Synonyms

TRY, TRY2, Anionic trypsinogen, Serine protease 2, Trypsin II, PRSS2, TRYP2

 

Description of Human Trypsin

Human Trypsin is a 21000-23000 Da protein. Trypsin is a serine protease enzyme produced in the pancreas as the inactive precursor trypsinogen, which is activated in the small intestine. It plays a crucial role in protein digestion by hydrolyzing peptide, amide, and ester bonds specifically at the carboxyl side of the amino acids L-arginine and L-lysine, breaking dietary proteins into peptides and amino acids essential for growth, hormone production, and tissue repair. Three major isoforms of trypsinogen exist: cationic (trypsinogen-1), anionic (trypsinogen-2), and mesotrypsinogen (trypsinogen-3), each contributing differently to digestive processes. Clinically, abnormal trypsin or trypsinogen levels are significant in diagnosing diseases such as cystic fibrosis, where elevated serum values are observed, and acute pancreatitis, where premature activation leads to pancreatic inflammation and tissue damage. Deficient trypsin activity can cause malabsorption and nutritional deficiencies. Beyond digestion, trypsin is widely applied in biotechnology and medicine. It is essential for cell culture, enabling the detachment of adherent cells, and is used in proteomics for protein digestion prior to mass spectrometry analysis. Therapeutically, trypsin is employed in wound care to remove necrotic tissue and promote healing, as well as in the treatment of inflammation and as a component in enzyme therapy for various conditions. Its specificity and versatility make trypsin invaluable in research, diagnostics, and clinical applications.

 

Source

Prepared from pancrease shown to be non reactive for HBsAg, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA-required tests.

 

Biological Activity

2.5 units per mg protein. One unit is defined as the amount of enzyme that hydrolyzes one µmole of N-benzoyl-DL-arginine-pNA per minute at 25°C in 200 mM Tris-HCl, pH 7.8, with 20 mM CaCl₂.

 

Storage

For long term, store Human Trypsin at -20°C.

 

Applications

Assay Development, In Vitro Diagnostics, Inflammation, Cystic Fibrosis.

 

Citations/Publications

de Castro, S., et al., (2020), 'N-benzyl 4, 4-disubstituted piperidines as a potent class of influenza H1N1 virus inhibitors showing a novel mechanism of hemagglutinin fusion peptide interaction', European Journal of Medicinal Chemistry 194: pp 112223. Available at: https://doi.org/10.1016/j.ejmech.2020.112223
Miki, M., et al., (2019), 'Human airway trypsin-like protease enhances interleukin-8 synthesis in bronchial epithelial cells by activating protease-activated receptor 2', Archives of Biochemistry and Biophysics 664: pp 167–173. Available at: https://doi.org/10.1016/j.abb.2019.01.019
Garcia, G. M., et al., (2020), 'Generation and characterization of murine monoclonal antibodies against immunoreactive trypsinogen for newborn screening of cystic fibrosis', Analytical Biochemistry 591: pp 113569. Available at: https://doi.org/10.1016/j.ab.2019.113569
NCBI: https://www.ncbi.nlm.nih.gov/protein/P07478/

 

Shipped with ice packs

 

Gel Scan of Human Trypsin

Fig. 1: SDS-PAGE Gel

 

 

Download Datasheet

 

 

 

 

 

Usage: For research use only. Not for use in diagnostic or therapeutic procedures. Not for human use.

 

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