Extract

Bovine Factor XIa is an enzyme, which is involved in the intrinsic pathway of blood coagulation. Bovine Factor XIa is highly selective and exhibits a minimal extended substrate recognition site of at least five residues long. Bovine Factor XIa is reactive as Bovine Factor IXa (HY-E70393I) does, that it cleaves all the peptides bearing factor IX activation site sequences.

Bovine Factor IXa Beta is an inactive and highly specific enzyme, with a minimal extended substrate recognition site and a preference for particular amino acid residues at specific subsites. Bovine Factor IXa Beta plays a role in the blood coagulation cascade.

Human Kallikrein is a serine protease that can be found in plasma and tissue. Human Kallikrein has the potential for the research of blood pressure, complement activation, and mediation and maintenance of inflammatory responses.

α-Glucosidase, rice is a GH31 glycoside hydrolase in rice seeds, with high selectivity for α-1,4-glycosidic bonds. α-Glucosidase, rice can be inhibited by rice husk extracts (IC₅₀ = 1.25 μg/mL) and steroidal components (IC₅₀ = 1.83 μg/mL). α-Glucosidase, rice exists in two major isoforms, among which isoform II is more sensitive to inhibitors. α-Glucosidase, rice can directly bind to and degrade starch granules in rice seeds. α-Glucosidase, rice can form ONG2-I and ONG2-II via post-translational proteolysis. α-Glucosidase, rice can be used in type 2 diabetes research.

Shrimp Alkaline Phosphatase (SAP), a nucleotide phosphatase, can catalyze the removal of 5′ phosphates from nucleic acid templates. Shrimp Alkaline Phosphatase is readily inactivated in the absence of chelators and is widely used phosphatases in molecular cloning.

α-Amylase, Human Pancreas (Amylase) is a hydrolase enzyme that can be isolated from human pancreas. α-Amylase, Human Pancreas catalyses the hydrolysis of internal α-1, 4-glycosidic linkages in starch to yield products like glucose and maltose. α-Amylase, Human Pancreas can be used in life science research.

Trypsin-Chymotrypsin 1:250 is a biocatalyst and a key enzyme in new biocatalyst technology. Enzyme engineering focuses on enhancing enzyme reaction kinetics, substrate selectivity, and activity under harsh conditions such as low or high pH. By introducing stimulus responsiveness to these enzyme modifications, dynamic control of activity is also possible.

Trypsin-Chymotrypsin 1:1 is a biocatalyst and a key enzyme in new biocatalyst technology. Enzyme engineering focuses on enhancing enzyme reaction kinetics, substrate selectivity, and activity under harsh conditions such as low or high pH. By introducing stimulus responsiveness to these enzyme modifications, dynamic control of activity is also possible.

Aminopeptidase catalyzes the cleavage of amino acids from the amino terminus of protein or peptide substrates.

1,3-β-Glucanase is one of the primary components in C. albicans biofilm extrapolymeric substance (EPS). 1,3-β-Glucanase can degrade β-1,3-glucan so as to disrupt the Candida biofilm matrix and increase the effect of the antimicrobial agent. 1,3-β-Glucanase can be used as an antibiofilm agent.

L-Lysine α-oxidase is a potent anticancer agent. L-Lysine α-oxidase also a L-amino acid oxidase, deaminates L-lysine with the yield of H2O2, ammonia, and α-keto-ε-aminocaproate. L-Lysine α-oxidase shows cytotoxicity and anticancer activity.

Phenylalanine ammonia-lyase is a non-mammalian enzyme converting phenylalanine into trans-cinnamic acid and ammonia. Phenylalanine ammonia-lyase can be used in the research of phenylketonuria.

Thioglucosidase is a S-glycosidic bond hydrolase. Thioglucosidase is promising for research of plant defense metabolites (e.g., glucosinolates).

Phosphatidylinositol phosphodiesterase hydrolyzes phosphatidylinositol to diacylglycerols and a mixture of myoinositol 1- and 1, 2-cyclic phosphates.

Agarase is a glycosidase that catalyzes the hydrolysis of agar into oligosaccharides.

Tryptophanase is a zymogen-converting enzyme and inducible enzyme that can convert its inactive precursor form into an active enzyme without additional polypeptide synthesis. In Escherichia coli K12, tryptophanase functions as an inducible enzyme, and its induction kinetics are similar to those of β-galactosidase. Tryptophanase catalyzes the conversion of L-tryptophan to indole.

Sutilains is a proteolytic enzyme that dissolves necrotic tissue and hyaluronidase. Sutilains can be used as a topical debriding agent in burns.