Recombinant Dog Anionic Trypsin protein (His tag) is a Dog Full Length protein, in the 24 to 247 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
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| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Anionic trypsin
Recombinant Dog Anionic Trypsin protein (His tag) is a Dog Full Length protein, in the 24 to 247 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
pH: 7.2 - 7.4
Constituents: Tris buffer, 50% Glycerol (glycerin, glycerine)
Belongs to the peptidase S1 family.
Anionic Trypsin also known as Trypsin-2 or PRSS2 is a serine protease with a molecular mass of approximately 25 kDa. It finds expression mainly in the pancreas. This protease functions by breaking down proteins into smaller peptides through cleaving peptide bonds at the carboxyl side of lysine and arginine residues. It plays an essential role in digestion being activated from its inactive precursor trypsinogen in the small intestine.
Anionic trypsin participates in protein digestion within the digestive system. It is part of the pancreatic enzyme complex that includes other proteases like chymotrypsin and elastase. This complex activity ensures the effective breakdown of dietary proteins which is vital for nutrient absorption and utilization. Anionic trypsin further regulates itself through feedback inhibition managing its own activity to prevent damage to pancreatic tissues.
Anionic trypsin plays a role in the proteolytic pathway important for nutrient assimilation. It operates alongside related enzymes such as chymotrypsin aiding the coordinated breakdown of proteins. Anionic trypsin is integral to the zymogen activation pathway where it converts trypsinogen to active trypsin ensuring digestive enzymes remain inactive until they reach the intestine where their function is most needed.
Anionic trypsin relates significantly to pancreatitis and cystic fibrosis. Mutations affecting its activity can lead to improper protein digestion contributing to inflammation in the pancreas as seen in pancreatitis. Anionic trypsin also interacts with CFTR protein influencing the pancreatic complications observed in cystic fibrosis. Understanding these interactions provides insights into treatment strategies for these conditions.
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