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Native Bovine Auto-Activated Protein Kinase LAB GRADE 97%

Auto-Activated Protein Kinase phosphorylates and inactivates protein phosphatase 2A. The funtion appears to be related to the catalytic domain of p21-activated p65 (PAK) protein kinase which is produced in apoptotic cells. AK is also involved in cytoskeleton organization and other signal transduction processes.

Native Clostridium histolyticum Collagenase LAB GRADE 97%

Collagenases are enzymes that break the peptide bonds in collagen. They assist in destroying extracellular structures in the pathogenesis of bacteria such as Clostridium. They are a considered a virulence factor, facilitating the spread of gas gangrene. They normally target the connective tissue in muscle cells and other body organs.

Native Crotalus atrox venom 5'-Nucleotidase LAB GRADE 97%

5'-nucleotidase is an enzyme with system name 5'-ribonucleotide phosphohydrolase. This enzyme catalyses the following chemical reaction:a 5'-ribonucleotide + H2O↔ a ribonucleoside + phosphate. This enzyme has a wide specificity for 5'-nucleotides.

Native Elizabethkingia meningoseptica PNGase F LAB GRADE

In enzymology, a peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase (EC is an enzyme that catalyzes a chemical reaction that cleaves a N4-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides.

Native Pseudomonas sp. Cholesterol Esterase LAB GRADE 97%

Sterol esterase belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is steryl-ester acylhydrolase. This enzyme participates in bile acid biosynthesis.

Native Rabbit Angiotensin Converting Enzyme LAB GRADE 97%

Angiotensin-converting enzyme (EC, or "ACE" indirectly increases blood pressure by causing blood vessels to constrict. It does that by converting angiotensin I to angiotensin II, which constricts the vessels. For this reason, drugs known as ACE inhibitors are used to lower blood pressure. ACE, angiotensin I and angiotensin II are part of the renin-angiotensin system (RAS), which controls blood pressure by regulating the volume of fluids in the body. ACE is secreted in the lungs and kidneys by cells in the endothelium (inner layer) of blood vessels.


Native Streptococcus hemolyticus Streptokinase LAB GRADE

Streptokinase (SK) is an enzyme secreted by several species of streptococci that can bind and activate human plasminogen. SK is used as an effective and inexpensive thrombolysis medication in some cases of myocardial infarction (heart attack) and pulmonary embolism. Streptokinase belongs to a group of medications known as fibrinolytics, and complexes of streptokinase with human plasminogen can hydrolytically activate other unbound plasminogen by activating through bond cleavage to produce plasmin.

Adenosylhomocysteinease from Human, recombinant LAB GRADE

S-adenosylhomocysteine hydrolase belongs to the adenosylhomocysteinase family. It catalyzes the reversible hydrolysis of S-adenosylhomocysteine (AdoHcy) to adenosine (Ado) and L-homocysteine (Hcy). Thus, it regulates the intracellular S-adenosylhomocysteine (SAH) concentration thought to be important for transmethylation reactions. Deficiency in this protein is one of the different causes of hypermethioninemia. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. Adenosylhomocysteinase is an enzyme that converts S-adenosylhomocysteine to homocysteine and adenosine. This enzyme catalyses the following chemical reaction: S-adenosyl-L-homocysteine + H2O↔ L-homocysteine + adenosine. The enzyme contains one tightly bound NAD+ per subunit.


Native Aerococcuss viridans Pyruvate oxidase LAB GRADE 97%

In enzymology, a pyruvate oxidase (EC is an enzyme that catalyzes the chemical reaction: pyruvate + phosphate + O2 ↔ acetyl phosphate + CO2 + H2O2. The 3 substrates of this enzyme are pyruvate, phosphate, and O2, whereas its 3 products are acetyl phosphate, CO2, and H2O2.

Native Aeromonas proteolytica Aminopeptidase LAB GRADE 97%

Aminopeptidase from Aeromonas proteolytica is a metalloenzyme, which contains 2 atoms of Zn2+ in a single polypeptide with an approximate molecular weight of 29.5 kDa as determined by sedimentation. This enzyme has a high degree of stability, being stable even at tempeRatures of 70°C for several hours. Partial inactivation occurs in 8 M urea. Maximum stability and activity are between pH 8.0-8.5. Aminopeptidase from Aeromonas proteolytica can function as an esterase.

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