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Human Chymotrypsin
Native whole molecule, biologically active
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Proteins Biological Activity: 40-70 units per mg protein Source: Human Pancreas Purity: ≥ 95% by SDS-PAGE; shows no trypsin activity when assayed against Nα-benzoyl-L-arginine-p-nitroanilide Physical State: Salt-free lyophilized solid Manufacturer: |
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Athens Research & Technology
Produktdetails
Description of Human Chymotrypsin
Human Chymotrypsin is a 25 kDa protein. Chymotrypsin is a serine protease synthesized in the pancreas as the inactive zymogen chymotrypsinogen. Upon secretion into the duodenum, trypsin cleaves chymotrypsinogen to activate it, enabling its role in digesting dietary proteins by hydrolyzing peptide bonds adjacent to aromatic (tryptophan, tyrosine, phenylalanine) and hydrophobic residues. Its catalytic mechanism relies on a triad of serine, histidine, and aspartate residues, with substrate specificity dictated by a hydrophobic binding pocket. Pancreatic duct obstruction in Cystic Fibrosis leads to elevated serum levels of chymotrypsinogen due to impaired secretion, while fecal chymotrypsin decreases, reflecting exocrine insufficiency. This dichotomy aids diagnosis, as low fecal levels (<120 µg/g) correlate with fat malabsorption and pancreatic dysfunction. Reduced chymotrypsin activity in stool serves as a biomarker for progressive pancreatic damage and insufficiency. Genetic mutations in CTRC, encoding chymotrypsin C, heighten chronic pancreatitis risk by disrupting trypsin regulation. In pancreatic cancer, elevated serum chymotrypsinogen levels may indicate ductal obstruction or tumor-related inflammation. Chymotrypsin quantification in stool remains a non-invasive diagnostic tool for pancreatic insufficiency, particularly in CF and chronic pancreatitis. Clinically, chymotrypsin supplements are used in enzyme replacement therapy to mitigate malabsorption in pancreatic disorders. Experimental therapies targeting chymotrypsin’s regulatory role in trypsin activation show promise for pancreatitis management. Additionally, its proteolytic properties are leveraged in wound debridement and cataract surgery, though evidence for efficacy in other conditions (e.g., burns, ulcers) remains limited.
Source
Prepared from pancreas shown to be non reactive for HBsAg, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA-required tests.
Biological Activity
40-70 units per mg protein. One unit is defined as the amount of enzyme that hydrolyzes one umole of Suc-Ala-Ala-Pro-Phe-pNA per minute at 21°C, pH 8.0
Storage
For long term, store Human Chymotrypsin at ≤ -20°C.
Applications
Cystic Fibrosis, Pancreatic Cancer, Pancreatic Damage, In Vitro Diagnostic, SARS-CoV-2.
Citations/Publications
Zhao, P., et al., (2020), 'Virus-Receptor Interactions of Glycosylated SARS-CoV-2 Spike and Human ACE2 Receptor', Cell Host & Microbe 28: pp 586–601. Available at: https://doi.org/10.1016/j.chom.2020.08.004
Chmielewski, D., et al., (2023), 'Structural insights into the modulation of coronavirus spike tilting and infectivity by hinge glycans', Nature Communications, 14: pp 7175. Available at: https://doi.org/10.1038/s41467-023-42836-9
Rosenbalm, K. E., et al., (2020), 'Glycomics-informed glycoproteomic analysis of sitespecific glycosylation for SARS-CoV-2 spike protein', STAR Protocols, 1: 100214. Available at: https://doi.org/10.1016/j.xpro.2020.100214
Shipped with ice packs
Gel Scan of Human Chymotrypsin
| Fig. 1: SDS-PAGE Gel |
Usage: For research use only. Not for use in diagnostic or therapeutic procedures. Not for human use.
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Payment Methods
Paying by bank transfer
