Results for Enzymes ( 25972 )
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Degrades extracellular matrix. Proposed to play a role in breast cancer invasion and metastasis. Exhibits trypsin-like activity as defined by cleavage of synthetic substrates with Arg or Lys as the P1 site.Defects in ST14 are a cause of ichthyosis autosomal recessive with hypotrichosis (ARIH). ARIH is a skin disorder characterized by congenital ichthyosis associated with the presence of less than the normal amount of hair.
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Caspase-8 (Cysteine-aspartic acid protease 8/Casp8a; also named MCH5, FLICA and MACH alpha 1) is a 28 kDa member of the peptidase C14A family of enzymes. It is widely expressed and is considered an initiating caspase for the apoptotic cascade. Caspase-8 acts on a wide variety of substrates, including procaspases?3, 4, 6, 7, 9 and 10, c?FLIPL and procaspase-8 itself. Human procaspase?8a is a 54?56 kDa, 479 amino acid (aa) protein. It contains two N?terminal death domains (aa 1?177), followed by a catalytic site that utilizes His317Gly318 plus Cys360. Normally, it is an inactive, cytosolic monomer. But following death?domain (DD) containing receptor oligomerization, Caspase?8 is recruited to the death-inducing signaling complex (DISC) that forms around the death domains of the oligomerized receptor.
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Catalyzes the oxidative deamination of primary and some secondary amine such as neurotransmitters, with concomitant reduction of oxygen to hydrogen peroxide and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. Preferentially oxidizes serotonin. Also catalyzes the oxidative deamination of kynuramine to 3-(2-aminophenyl)-3-oxopropanal that can spontaneously condense to 4-hydroxyquinoline.
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ACPP (Acid phosphatase, prostate; also PAP and ACP3) is a 48-52 kDa glycoprotein member of the histidine acid phosphatase family of enzymes. It exists as a 95-100 kDa nondisulfide-linked homodimer that hydrolyzes phosphate esters under low pH to generate free phosphate. ACPP is expressed by prostate epithelium and pain-detecting spinal cord neurons. In the spinal cord, ACPP dephosphorylates AMP.
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Human beta -Glucuronidase (EC 3.2.1.31) encoded by the GUSB gene is a lysosomal hydrolase involved in the stepwise degradation of glucuronic acid-containing glycosaminoglycans that include heparan sulfate, chondroitin sulfate and hyaluronan. The enzyme is only active on the glucuronic acid of the non-reducing end. The native protein has been reported as a tetrameric glycoprotein composed of identical subunits. Mutations in the GUSB gene are linked to mucopolysaccharidosis type VII. Accumulation of partially degraded glycosaminoglycans, with glucuronic acid residues at the non-reducing termini, are usually found in the lysosomes of patients with the disease. It has also been reported that this enzyme may contribute to the depletion of chondroitin from cartilage and thereby facilitate the damage of joints in rheumatoid arthritis.
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Recombinant Human Urokinase-Type Plasminogen Activator is a serine protease, which specifically cleaves the zymogen plasminogen to form the active enzyme plasmin. Urokinase-Type Plasminogen Activator is a potent marker of invasion and metastasis in many human cancers associated with breast, colon, stomach, bladder, brain, ovary and endometrium. Human Urokinase-Type Plasminogen Activator is initially synthesized as 431 amino acid precursor with a N-terminal signal peptide residues. The single chain molecule is processed into a disulfide-linked two-chain molecule. There exists two forms A chain, the long A chain contains an EGF-like domain that is responsible for binding of the uPA receptor. The B chain corresponds to the catalytic domain.