You searched for: Enzymes

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Pancreatic Lipase-Related Protein 1 (PNLIPRP1) belongs to the Lipase family within the AB hydrolase superfamily. PNLIPRP1 is a secreted protein and contains one PLAT domain. PNLIPRP1 is involved in lipid metabolic process, acting as a negative regulator of pancreatic lipase activity by competing with pancreatic lipase for colipase occupancy. PNLIPRP1 may play a role in inhibiting dietary triglyceride digestion, but it lacks detectable lipase activity towards triglycerides, diglycerides, phosphatidylcholine, galactolipids or cholesterol esters.

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Tripeptidyl-Peptidase 1 (TPP1) belongs to the peptidase S53 family. TPP1 is detected in all tissues examined with highest levels in heart and placenta and relatively similar levels in other tissues. TPP1 is lysosomal serine protease with tripeptidyl-peptidase I activity. TPP1 may act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases. TPP1 requires substrates with an unsubstituted N-terminus. TPP1 mutations have also been shown to cause neuronal ceroid lipofuscinosis type 2 (CLN2).

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Carbonic Anhydrase-Related Protein 10 (CA10) belongs to the Carbonic Anhydrase family of Zinc Metalloenzymes. It is an acatalytic member of the alpha-carbonic anhydrase subgroup. CA10 expression is detected in the adult total brain and almost all parts of the central nervous system, but not in the fetal brain. CA10 catalyse the reversible hydration of carbon dioxide in various biological processes, which is fundamental to many processes such as respiration, renal tubular acidification and bone resorption. It is thought to play a role in the central nervous system, especially in brain development.

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Chitotriosidase-1 (CHIT1) is a glycoprotein that belongs to the Glycosyl Hydrolase 18 family and Chitinase class II subfamily. It is secreted by cultured macrophages and serves to degrade chitin, chitotriose and chitobiose. CHIT1 may participate in the defense against nematodes and other pathogens. It is highly expressed in the plasma of patients with Gaucher's disease type I, which can be used as diagnostic aid and to evaluate the success of treatment that brings levels back to normal. The amino acid sequence of human CHIT1 is 99%, 76%, 75% and 55% identical to that of chimpansee, rat, mouse and fruit fly, respectively.

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Chitinase-3-Like Protein 1 (CHI3L1) belongs to the glycosyl hydrolase 18 family. CHI3L1 is expressed in activated macrophages, articular chondrocytes, synovial cells as well as in liver. It lacks chitinase activity and is secreted by activated macrophages, chondrocytes, neutrophils and synovial cells. CHI3L1 is thought to play a role in defense against pathogens, or in tissue remodeling, and in the capacity of cells to respond to and cope with changes in their environment. In addition, CHI3L1 is associated with susceptibility to asthma-related traits type 7 (ASRT7) which assessed by methacholine challenge test, serum IgE levels, atopy, and atopic dermatitis.

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Carbonic Anhydrase-Related Protein 11 (CA11) is a secreted protein member of the alpha-carbonic anhydrase family. Carbonic Anhydrases (CAs) are a large family of zinc metalloenzymes that catalyse the reversible hydration of carbon dioxide. They participate in a variety of biological processes, including respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, saliva, and gastric acid. CA11 is expressed abundantly in the brain with moderate expression also present in spinal cord and thyroid. CA11 may play a general role in the central nervous system.

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Calcium/Calmodulin-Dependent Protein Kinase Type II Subunit Beta (CAMK2B) is a cytoplasmic protein that belongs to the serine/threonine protein kinase family and the Ca(2+)/calmodulin-dependent protein kinase subfamily. CAMK2B is a calcium/calmodulin-dependent protein kinase that functions autonomously after Ca2+/calmodulin-binding and autophosphorylation. It is involved in dendritic spine and synapse formation, neuronal plasticity and regulation of sarcoplamic reticulum Ca2+ transport in skeletal muscle. In neurons, CAMK2B plays an essential structural role in the reorganisation of the actin cytoskeleton during plasticity by binding and bundling actin filaments in a kinase-independent manner.

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NAD kinase catalyses the transfer of a phosphate group from ATP to NAD+ to generate NADP+, which in its reduced form acts as an electron donor for biosynthetic reactions. NADP+ is an essential coenzyme in metabolism and provides reducing power to biosynthetic processes such as fatty acid biosynthesis. NAD kinase from Mycobacterium tuberculosis is not ATP-dependent but has a broader substrate specificity than human NAD kinase. It can economically produce NADP+ by using other nucleoside triphosphates as well as inorganic polyphosphate as a source of phosphorus. Was identified as a high-confidence drug target. Catalytic activity: ATP + NAD+ = ADP + NADP+.

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Dihydropteridine reductase, also known as HDHPR and Quinoid dihydropteridine reductase, QDPR and DHPR, belongs to the short-chain dehydrogenases/reductases (SDR) family. QDPR exists as a homodimer. QDPR is part of the pathway that recycles a substance called tetrahydrobiopterin, also known as BH4 and tryptophan hydroxylases. The regeneration of this substance is critical for the proper processing of several other amino acids in the body. Tetrahydrobiopterin also helps produce certain chemicals in the brain called neurotransmitters, which transmit signals between nerve cells. Defects in QDPR are the cause of BH4-deficient hyperphenylalaninemia type C (HPABH4C) which is a rare autosomal recessive disorder and is lethal.

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Tyrosine-Protein Kinase Blk (BLK) contains one protein kinase domain, one SH2 domain and one SH3 domain. BLK is a non-receptor tyrosine kinase, which is involved in B-lymphocyte development, differentiation and signaling. B-cell receptor (BCR) signaling requires a tight regulation of several protein tyrosine kinases and phosphatases, and associated coreceptors. Signaling through BLK plays an important role in transmitting signals through surface immunoglobulines and supports the pro-B to pre-B transition, as well as the signaling for growth arrest and apoptosis downstream of B-cell receptor. Defects in BLK are a cause of maturity-onset diabetes of the young type 11 (MODY11).

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Mouse Ca14,also known as Carbonic anhydrase 14,is a member of large family of zinc metalloenzymes .It could catalyse reversible hydration of carbon dioxide. The reaction is fundamental to many processes such as respiration, renal tubular acidification and bone resorption. Fifteen CA isoforms have been reported so far. They have different patterns of tissue-specific expression and physiologic roles. Some CAs may serve as markers for tumours and hypoxia. CA XIV is a polypeptide consisting of an extracellular N-terminal catalytic domain, a membrane-spanning segment and a short intracellular C- terminal segment with several potential phosphorylation sites. A subset of CAs lack CA activity due to point mutations but retain esterase function. CA14 is widely expressed in the central nervous system

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Chitinase 3-Like Protein 2 (CHI3L2) is a 39 kDa secreted glycoprotein which belongs to the glycosyl hydrolase 18 family and the most closely related to human cartilage glycoprotein 39, which promotes the growth of human synovial cells as well as skin and fetal lung fibroblasts. Highest expression of CHI3L2 is in chondrocytes, followed by synoviocytes, lung and heart. It is not detected in spleen, pancreas, and liver. CHI3L2 may also be expressed in developing brain and placenta. Increased levels of CHI3L2 have been demonstrated in synovial fluids of patients with rheumatoid or osteoarthritis as well as in some other pathologies and in malignant tumors, particularly in glioblastomas. CHI3L2 may bind glycan structure with high affinity, but not heparin. It has has no chitotriosidase activity, but is likely to bind some type of glycan.

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Messenger RNA (mRNA) degradation plays a key role in the control of gene expression in all organisms by limiting the number of times that each mRNA molecule can be used as a template for protein synthesis. RNA pyrophosphohydrolase, also called RppH, is a master regulator of 5'-dependent mRNA decay. It accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage. RppH preferentially hydrolyses diadenosine penta-phosphate with ATP as one of the reaction products, and can be able to hydrolyse diadenosine hexa- and tetra-phosphate. However, this protein has no activity on diadenosine tri-phosphate, ADP-ribose, NADH and UDP-glucose. In the meningitis causing strain E. coli K1, it has been shown to play a role in HBMEC (human brain microvascular endothelial cells) invasion in vitro.

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Collagenases are enzymes that break the peptide bonds in collagen.

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Collagenases are enzymes that break the peptide bonds in collagen.

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Zymolyase-20T is an enzyme preparation from a submerged culture of Arthrobacter luteus which effectively lyses cell walls of viable yeast cells. The primary enzyme in this preparation responsible for lysis of viable yeast cells is ß-1,3-glucan laminaripentaohydrolase. It hydrolyzes glucose polymers at the ß-1,3-glucan linkages releasing laminaripentaose as the principal product.

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One bacterial amylase unit is defined as that quantity of enzyme which will dextrinise one milligram of starch per minute at pH 6,6 and 30 °C.

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Papain, powder, purified, is a cysteine protease enzyme the is present in the papaya fruit.

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Pepsin is an acid protease, contains a proteolytic enzyme. It contains the "cathepsin" component which has milk curdling activity. It has a broad range of substrate activity and demonstrates an esterase acitivity. It generally attacks peptide bonds.

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For typical assay, dissolve enzyme at a concentration of 1 mg/ml in 0,05 M TES with 0,36 mM calcium chloride, pH 7,5. Dilutions run are 1/10 and 1/20 in the above buffer.

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Glucose-6-phosphate dehydrogenase (G6PD or G6PDH) is a cytosolic enzyme in the pentose phosphate pathway, a metabolic pathway that supplies reducing energy to cells (such as erythrocytes) by maintaining the level of the co-enzyme nicotinamide adenine dinucleotide phosphate (NADPH).

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Cellulase refers to a group of enzymes which, acting together, hydrolyse cellulose. The b-glucosidases, including cellobiose, are primarily active on the smaller molecular weight cellulose hydrolysates. During cellulose breakdown they are active on the dimers and oligomers of cellulose.

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Ascorbate Oxidase is an enzyme belonging to the family of oxidoreductases that catalyses the reaction: Ascorbic acid +¹/₂ O₂ ascorbate oxidase → Dehydroascorbic acid +H₂O.

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HRP is a plant glycohemoprotein belongs to the ferroprotoporphyrin group of peroxidases. It is used in biochemistry applications such as western blots, ELISA and Immunohistochemistry. It is used to amplify a weak signal and increase detectability of a target molecule, such as a protein. HRP labeled immunoglobulins are used as probes for the demonstration of tissue antigens and in enzyme immunoassay (EIA) systems for determination of soluble and insoluble antigens.

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Activity: Each vial contains 500 units β-Lactamase I and 50 units β-Lactamase II Unit Definition: One unit is defined as the amount of enzyme which will hydrolyse 1,0 micromole of benzyl penicillin and 1,0 micromole of cephalosporin C per minute at 25 °C in the presence of EDTA pH 7,0.

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Alkaline phosphatase is a hydrolase enzyme responsible for removing phosphate groups from many types of molecules, including nucleotides, proteins, and alkaloids.

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Unit Definition: Enzyme activity is determined by a change in optical density in a solution of hyaluronic acid. Activity is compared to a hyaluronidase International Standard and is expressed as an International Unit (U).

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Pancreatin are natural chemicals that help break down fats, proteins, and carbohydrates. Pancreatin is a digestive enzyme produced by the pancreas and delivered to the small intestine for the hydrolysis of complex nutrients.

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The hyaluronidase is purified from Streptomyces hyalurolyticus. This enzyme belongs to the endo-beta-hexosaminidase and endo-eliminase type enzyme that produces oligo-saccharide (unsaturated tetraose and pentose) by hydrolysing the beta-1,4-linkage of hyaluronic acid. It is stable in both high temperature and acid or alkaline range. It has high substrate specificity and hydrolyzes hyaluronic acid only in mucopolysaccharide.

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Collagenases degrade native helical collagen fibrils. The enzyme has an important role in connective tissue metabolism and is produced by specific cells involved in repairs and remodelling processes. It is a type II enzyme that contains greater clostripain activity. It is generally used for heart, bone, muscle, thyroid, cartilage, and liver cells. Ca²⁺ is required for its activation while metal chelating agents such as cysteine, EDTA or o-phenanthroline inhibits its activity.