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NADP monosodium salt LAB GRADE 96

NADP, Monosodium Salt is a coenzyme that is widely distributed in living matter. Participates in oxidation-reduction reactions. https://www.creative-enzymes.com/product/NADP-Monosodium-Salt_16262.html

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Poly guluronate lyase LAB GRADE 1

In enzymology, a poly(alpha-L-guluronate) lyase (EC 4.2.2.11) is an enzyme that catalyzes the chemical reaction: Eliminative cleavage of polysaccharides containing a terminal alpha-L-guluronate group, to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends. This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides.

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UDP-Glc Dehydrogenase LAB GRADE 1

UDP-glucose 6-dehydrogenase is a cytosolic enzyme that in humans is encoded by the UGDH gene. The protein encoded by this gene converts UDP-glucose to UDP-glucuronate and thereby participates in the biosynthesis of glycosaminoglycans such as hyaluronan, chondroitin sulfate, and heparan sulfate. These glycosylated compounds are common components of the extracellular matrix and likely play roles in signal transduction, cell migration, and cancer growth and metastasis. The expression of this gene is up-regulated by transforming growth factor beta and down-regulated by hypoxia.

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mannan endo-1,6-?-mannosidase IP 1

Mannan endo-1,6-alpha-mannosidase (EC 3.2.1.101, exo-1,6-beta-mannanase, endo-alpha-1->6-D-mannanase, endo-1,6-beta-mannanase, mannan endo-1,6-beta-mannosidase, 1,6-alpha-D-mannan mannanohydrolase) is an enzyme with systematic name 6-alpha-D-mannan mannanohydrolase. This enzyme catalyses the following chemical reaction: Random hydrolysis of (1->6)-alpha-D-mannosidic linkages in unbranched (1->6)-mannans.

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Oligogalacturonate lyase LAB GRADE 1

In enzymology, an oligogalacturonide lyase (EC 4.2.2.6) is an enzyme that catalyzes the chemical reaction: 4-(4-deoxy-beta-D-gluc-4-enuronosyl)-D-galacturonate → 2 5-dehydro-4-deoxy-D-glucuronate. Hence, this enzyme has one substrate, 4-(4-deoxy-beta-D-gluc-4-enuronosyl)-D-galacturonate, and one product, 5-dehydro-4-deoxy-D-glucuronate. This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides.

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Rhamnogalacturonan Lyase LAB GRADE 1

Rhamnogalacturonan Lyase is an endo-1,4-α-rhamnogalacturonan lyase. This enzyme catalyses the following chemical reaction: Endotype eliminative cleavage of L-alpha-rhamnopyranosyl-(1->4)-alpha-D-galactopyranosyluronic acid bonds of rhamnogalacturonan I domains in ramified hairy regions of pectin leaving L-rhamnopyranose at the reducing end and 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end.

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UDP-glucose 6-dehydrogenase LAB GRADE 1

Also acts on UDP-α-D-2-deoxyglucose.

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mannan endo-1,6-mannosidase LAB GRADE 1

Mannan endo-1,6-alpha-mannosidase (EC 3.2.1.101) is an enzyme with systematic name 6-alpha-D-mannan mannanohydrolase.

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Acetyl-L-carnitine chloride LAB GRADE 96

Endogenous mitochondrial metabolite that transports acetyl groups across the mitochondrial membrane. Exogenous acetylcarnitine enhances mitochondrial function in aged rats. As an acetate donor to coenzyme A, it increases the central and peripheral acetylcholine synthesis and function. Acetylcarnitine has antinociceptive activity that may be mediated by enhanced activity of muscarinic cholinergic receptors or mGlu2 glutamate receptors. https://www.creative-enzymes.com/product/AcetylLcarnitine-Chloride_16266.html

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Human Coagulation Factor VII LAB GRADE 96

Human factor VII is a single chain, vitamin K-dependent, plasma glycoprotein which is synthesized in the liver. Prior to secretion into the blood, post translational modification by a vitamin K-dependent carboxylase produces ten-carboxyglutamic acid (gla) residues located in the NH2-terminal portion of the molecule, which facilitate cell membrane binding. Factor VII is proteolytically activated to the serine protease, factor VIIa, during coagulation. Factor VII can be activated by thrombin, factor IXa, factor Xa or factor XIIa. The activation results in cleavage of the single chain molecule on the COOH-terminal side of arginine-152, to produce an NH2-terminal derived light chain (Mr=20,000) and a COOH-terminal derived heavy chain (Mr=30,000) which remain covalently associated by a single disulfide bond. The light chain region contains the gla domain, as well as two growth factor domains which are homologous to human epidermal growth factor (EGF). A single β-hydroxyaspartic acid identified in factor VII is also located in the light chain region. The heavy chain region of factor VIIa contains the catalytic domain. Factor VIIa and the cofactor, tissue factor, may combine on negatively charged cell surfaces in a calcium dependent manner to form the extrinsic factor Xase enzyme complex. This enzyme complex catalyzes the conversion of both factor IX to factor IXa and factor X to factor Xa. The cDNA for factor VII has been isolated and the nucleotide sequence determined. Factor VII shares extensive sequence homology with other serine proteases including factor IX, factor X and protein C.Human factor VII is purified using a combination of conventional techniques and immunoaffinity chromatography. The purified protein is supplied in 50% (vol/vol) glycerol/H2O and should be stored at -20°C. Purity is determined by SDS-PAGE analysis and activity is measured in a factor VII clotting assay.

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