Trypsin is a serine protease in the digestive system of human and animals. The main function of this enzyme is to hydrolyze proteins into smaller peptides or even amino acids. Trypsin cleaves peptides on the C-terminal side of lysine and arginine residues. The rate of hydrolysis of this reaction is slowed if an acidic residue is on either side of the cleavage site and hydrolysis is stopped if a proline residue is on the carboxyl side of the cleavage site. The optimal pH for trypsin activity is 7-9. Trypsin can also act to cleave ester and amide linkages of synthetic derivatives of amino acids. EDTA is added to trypsin solutions as a chelating agent that neutralizes calcium and magnesium ions that obscure the peptide bonds on which trypsin acts. Removing these ions increases the enzymatic activity.
Front Cell Neurosci. 2021 Oct 1;15:735723.
The Expression and Roles of the Super Elongation Complex in Mouse Cochlear Lgr5+ Progenitor Cells
Trypsin (porcine pancreas) purchased from AbMole
|Solubility (25°C)||Soluble in water (10 mg/ml)
Soluble in phosphate buffers (10 mg/ml)
|Storage||2-8°C, dry, sealed|
|Body Surface Area (m2)||0.007||0.025||0.15||0.05||0.02||0.5|
|Animal A (mg/kg) = Animal B (mg/kg) multiplied by||Animal B Km|
|Animal A Km|
For example, to modify the dose of Compound A used for a mouse (20 mg/kg) to a dose based on the BSA for a rat, multiply 20 mg/kg by the Km factor for a mouse and then divide by the Km factor for a rat. This calculation results in a rat equivalent dose for Compound A of 10 mg/kg.
|Related Enzymes & Coenzymes Products|
Cipaglucosidase alfa is a unique human recombinant acidic alpha-glucosidase (GAA) that can be used in studies related to Pompe disease.
PreScission Protease is a recombinantly expressed 3C protease of human rhinovirus type 14 with a GST tag in Escherichia coli that specifically recognizes the octapeptide sequence Leu-Glu-Val-Leu-Phe-Gln-Gly-Pro or the core pentapeptide sequence Leu-Phe-Gln-Gly-Pro at low temperature (4°C) and cleaves between Gln and Gly amino acid residues. Pro and enzymatically cleaves between Gln and Gly amino acid residues, commonly used to remove Glutathione S-transferase (GST), His, or other tags from fusion proteins.
|DNase I (Bovine Pancreas)
DNase I (Bovine Pancreas) is a bovine pancreas-derived DNase I that plays a key role in the cleavage of extracellular DNA, degrading double-stranded DNA into oligodeoxyribonucleotides with a 5ˊ-phosphate and 3ˊ-OH terminus. It can also degrade single-stranded DNA in the presence of monovalent manganese ions, and can be used in molecular biology research.
Lactate oxidase (LOX) is a group of flavin mononucleotide (FMN)-dependent enzymes that catalyze the oxidation of l-lactate using oxygen as the primary electron acceptor, as well as converting lactate to pyruvate and releasing hydrogen peroxide.
|Angiotensin Converting Enzyme (from porcine kidney)
The angiotensin-converting enzyme (ACE) is a dipeptidyl-carboxypeptidase which exists in somatic and testicular isoforms with zinc binding motif HEXXH in their active site. ACE regulates blood pressure through renin-angiotensin system.
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