Extract

Phenylalanine dehydrogenase is an NAD⁺-dependent oxidoreductase targeting L-phenylalanine. Phenylalanine dehydrogenase catalyzes deamination to phenylpyruvate and NADH as part of amino acid metabolism regulation. Phenylalanine dehydrogenase is promising for research of phenylketonuria (PKU).

Glutamate carboxypeptidase is an endo/exopeptidase targeting folate and antifolate agents. Glutamate carboxypeptidase regulates intracellular folate homeostasis by hydrolyzing γ-polyglutamate chains. Glutamate carboxypeptidase is promising for research of antifolate agents and cancers.

Rennet is is a mixture of the proteolytic enzymes pepsin and chymosin (rennin), which is found in the fourth stomach of young ruminants. Rennet is promising for research of allergies (e.g., asthma, rhinitis).

(R)-Mandelonitrile lyase (Mandelonitrile Lyase) is an enzyme that can be isolated from Prunus species.

Fructosyl amino acid oxidase can be used to measure glycosylated protein. Glycosylated protein, especially glycosylated hemoglobin A1c, is an important marker to evaluate the efficacy of diabetes treatment.

β-Lactamase is the enzyme produced by bacteria. β-Lactamase mediates β-lactam resistance.

Sphingomyelin phosphodiesterase, Streptomyces sp. is a sphingomyelin phosphodiesterase derived from the genus Streptomyces, which cleaves the phosphodiester bond of sphingomyelin. Sphingomyelin phosphodiesterase, Streptomyces sp. catalyzes the hydrolysis of sphingomyelin in micelles, synthetic substrates, erythrocyte ghost membranes and liposomes, as well as the hydrolysis of the substrate HNP. In the presence of Mg²⁺ or Mn²⁺ , Sphingomyelin phosphodiesterase, Streptomyces sp. induces hemolysis of bovine erythrocytes through the hydrolysis of membrane sphingomyelin.

Lipoxygenase, general (LOX) is a dioxygenase, is often used in biochemical studies. Lipoxygenase, general catalyzes the formation of corresponding hydroperoxides from polyunsaturated fatty acids such as linoleic acid and arachidonic acid.

Tannase is a tannin acyl hydrolase. Tannase catalyzes the hydrolysis of ester bonds in gallotannins, complex tannins and gallic acid esters to release gallic acid. Tannase plays a role in industrial production, including the manufacture of instant tea, beer, fruit juice, some wines, and the production of gallic acid.

Phosphodiesterase II (EC 3.1.16.1), namely phosphodiesterase 2, is mainly involved in the hydrolysis of the important second messengers cyclic adenosine monophosphate (cAMP) and cyclic guanosine monophosphate (cGMP), and is often used in biochemical research. Phosphodiesterase II is expressed in a variety of tissues, such as the adrenal medulla, brain, heart, platelets, macrophages and endothelial cells, and is involved in the regulation of many different intracellular processes.

Phosphorylase b is one of the two forms of phosphorylase present in skeletal muscle. The other is Phosphorylase a, which can be transformed into one another. The conversion process requires the addition of divalent metal ions and ATP.

Peptidase (IMPa) (Erepsin) is catalytically active enzyme that cleaves peptide bonds in proteins and peptides by hydrolysis.

Penicillinase is an enzyme capable of hydrolyzing penicillin. Penicillinase converts penicillin into penicilloic acid, which has no antigenicity, and destroys the antibacterial, antigenic and epileptogenic properties of penicillin. Penicillinase shortens the duration of penicillin-induced seizures and neutralizes the ability of penicillin to form epileptogenic foci. Penicillinase can be used in research related to penicillin hypersensitivity and penicillin-induced encephalopathy.

β-Amylase, Bacilus subtilis has abundant starch degrading activities. β-Amylase can be used for various biochemical studies.

Rabbit Factor X is a vitamin K-dependent plasma serine protease that is activated to generate Factor Xa. Rabbit Factor X mediates the common coagulation pathway and catalyzes the conversion of prothrombin to thrombin. Rabbit Factor X is the first enzyme to act in the common pathway of thrombosis in the coagulation cascade. Rabbit Factor X can be used in studies related to Factor X deficiency.

Collagenase (Type C, filtered, animal free) is a microbial collagenolytic enzyme that can be found in Clostridium histolyticum, leeches, or Paralithodes camtschaticus (Kamchatka crab). The activity of Collagenase (Type C, filtered, animal free) is completely inhibited by tea catechins, especially (-)-epicatechin gallate (ECg) (HY-N0356) and (-)-epigallocatechin gallate (EGCg). Collagenase (Type C, filtered, animal free) is used in research related to Peyronie's disease.

Collagenase (Type B, animal free) does not contain animal-related components, and is sterilized by filtration using a 0.22 μm filter membrane. Collagenase (Type B, filtered, animal free) has higher collagenase and casein activity.

β-Glucuronidase/Arylsulfatase, Helix pomatia is an enzyme with arylsulfatase activity that is isolated from Roman snails (Helix pomatia). β-Glucuronidase/Arylsulfatase, Helix pomatia exhibits broad-spectrum hydrolytic specificity towards various β-glucuronides and sulfate conjugates. β-Glucuronidase/Arylsulfatase, Helix pomatia is used for simultaneous deconjugation of drug-conjugated metabolites in urine samples.

Canine Fibrinogen is a natural fibrinogen derived from canine plasma. Canine Fibrinogen specifically binds to the host SpsL, but shows weak binding affinity to fibrinogen from other mammals including humans. Canine Fibrinogen binds to the N2N3 subdomain of SpsL via the "anchor-lock-latch" model, and interacts with multiple sites in its α-chain C domain. The binding of Canine Fibrinogen to SpsL promotes bacterial aggregation, biofilm formation, and enhances bacterial resistance to neutrophil phagocytosis. Canine Fibrinogen can be used in studies related to canine skin infections.

Bovine Factor X is a vitamin K-dependent plasma serine protease that is activated to generate Factor Xa. Bovine Factor X mediates the common coagulation pathway and catalyzes the conversion of prothrombin to thrombin. Bovine Factor X is the first enzyme to act in the common pathway of thrombosis in the coagulation cascade. Bovine Factor X can be used in studies related to Factor X deficiency.