Personalcare Enzymes - suppliers, manufacturers, exporters


Native Human Creatine Kinase mix LAB GRADE

Creatine kinase plays a key role in the energy metabolism of cells with intermittently high and fluctuating energy requirements. Examples of such cells include cardiac or skeletal muscle cells and neural tissues of brain and retina. The enzyme catalyzes the reversible transfer of the phosphoryl group from phosphorylcreatine to ADP, in order to generate ATP.1 The molecular mass of the protein is found to be approximately 80 kDa Da. It is made up of 2 subunits, each having a molecular weight of 40 kDa ± 2000. The lighter subunit is present in larger amounts.

Native Rhizopus sp. Glucoamylase LAB GRADE

Glucan 1,4-alpha-glucosidase is an enzyme located on the brush border of the small intestine with system name 4-alpha-D-glucan glucohydrolase. This enzyme catalyses the following chemical reaction: Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose. Most forms of the enzyme can rapidly hydrolyse 1,6-alpha-D-glycosidic bonds when the next bond in the sequence is 1,4.

Heparinase Thromboestastograph Technical 98%

Molecular weight: 42,508 Da
Isoelectric point: 9.3 - 9.5
pH optimum for activity: 6.5 - 7.5
pH range for activity: 4 - 9
Optimal testing temperature range: 20 ° C - 37 ° C
Optimal storage temperature: -70 ° C

1, For the neutralization of heparin in blood and plasma samples before analysis.
2, For similar in vitro neutralization of low molecular weight heparins
3, As integral part of in vitro diagnostic tests for the neutralization of heparin (blood clotting tests, platelet tests).
4, In blood collection tubes for the neutralization of heparin.
5, For the preparation of low molecular weight heparins from unfractionated heparin.
6, As a research reagent (glycosaminoglycan degradation)
7, For the preparation of disaccharides of heparin and the preparation of oligosaccharide libraries.

Heparinase Activated Clotting Time (ACT)
Heparinase ACT may be performed several times during CABG surgery to assess heparin reversal, hemodilution and heparin rebound.
Hepzyme may be added to blood samples to reduce test ambiguity when the presence of heparin or low molecular weight heparin is suspected.

Heparinase Thromboestastograph (TEG)
Heparinase TEG may be performed several times during CABG surgery to assess heparin reversal, hemodilution heparin rebound, platelet function and fibrinolysis.

Heparinase Prothrombin Time (PT)
Heparinase is added to PT cartridges to make them heparin insensitive, for monitoring oral anticoagulation therapy.

Heparinase Rotation Thromboelastometry
Heparinase Rotation Thromboelastometry may be performed several times during CABG surgery to assess heparin reversal, hemodilution heparin rebound.

Native Clostridium sp. Diaphorase LAB GRADE

This enzyme is useful for colorimetric determination of NAD(P)H and many dehydrogenases when coupled with various dyes which act as hydrogen acceptors from NAD(P)H.

Native Potato Acid Phosphatase LAB GRADE 97%

Acid phosphatases (APase) are a family of enzymes that non-specifically catalyze the hydrolysis of monoesters and anhydrides of phosphoric acid to produce inorganic phosphate at an optimum pH of 4 to 7. Acid phosphatase from potatoes is a 111 kDa diner consisting of two subunits at 41 and 35 kDa. This phosphatase has also been shown to cleave DNA.

Native Sweet almond ?-Glucosidase LAB GRADE

Beta-glucosidase is a glucosidase enzyme that acts upon β1->4 bonds linking two glucose or glucose-substituted molecules (i.e., the disaccharide cellobiose). It is one of the cellulases, enzymes involved in the decomposition of cellulose and related polysaccharides; more specifically, an exocellulase with specificity for a variety of beta-D-glycoside substrates. It catalyzes the hydrolysis of terminal non-reducing residues in beta-D-glucosides with release of glucose.

Native Aspergillus sp. Catalase LAB GRADE 97%

Catalase is a common enzyme found in nearly all living organisms, where it functions to catalyze the decomposition of hydrogen peroxide to water and oxygen. Catalase has one of the highest turnover numbers of all enzymes; one molecule of catalase can convert millions of molecules of hydrogen peroxide to water and oxygen per second. Catalase is a tetramer of four polypeptide chains, each over 500 amino acids long. It contains four porphyrin heme (iron) groups that allow the enzyme to react with the hydrogen peroxide. The optimum pH for catalase is approximately 7, while the optimum temperature varies by species.

Native Calf Adenosine Deaminase LAB GRADE 98%

Adenosine deaminase is an enzyme (EC involved in purine metabolism. It is needed for the breakdown of adenosine from food and for the turnover of nucleic acids in tissues. Present in virtually all mammalian cells, its primary function in Humans is the development and maintenance of the immune system.

Native Candida sp. Alcohol oxidase LAB GRADE

In enzymology, an alcohol oxidase (EC is an enzyme that catalyzes the chemical reaction a primary alcohol + O2 ↔ an aldehyde + H2O2. Thus, the two substrates of this enzyme are primary alcohol and O2, whereas its two products are aldehyde and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor.

Native Cystathionine-?-synthase LAB GRADE 97%

Cystathionine-β-synthase, also known as CBS, is an enzyme (EC that in humans is encoded by the CBS gene. CBS uses the cofactor pyridoxal-phosphate (PLP) and can be allosterically regulated by effectors such as the ubiquitous cofactor S-adenosyl-L-methionine (adoMet). This enzyme belongs to the family of lyases, to be specific, the hydro-lyases, which cleave carbon-oxygen bonds. CBS is a multidomain enzyme composed of an N-terminal enzymatic domain and two CBS domains. The CBS gene is the most common locus for mutations associated with homocystinuria.


1...7891011...31 uses cookies to ensure that we give you the best experience on our website. By using this site, you agree to our Privacy Policy and our Terms of Use. X