Hledali jste: Enzymy

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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.

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Brain-Specific Serine Protease 4 (BSSP-4) is a serine protease that preferentially cleaves the synthetic substrate H-D-Leu-Thr-Arg-pNA compared to tosyl-Gly-Pro-Arg-pNA. BSSP-4 is expressed abundantly in the epithelial cells of the airways, including trachea, esophagus and fetal lung, but scarce in adult lung and expressed at low levels in placenta, pancreas, prostate and thyroid gland. BSSP-4 belongs to the peptidase S1 family and related to trypsin, referentially hydrolyzing substrates after arginine and lysine residues. However, BSSP-4 is less susceptible to inhibition by common trypsin inhibitors such as aprotinin, alpha1-antitrypsin and secretory leukocyte protease inhibitor. BSSP-4 efficiently converts pro-urokinase- type plasminogen activator to its mature, active form.

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Lon Protease, is a member of the Lon protease family. They are found in archaea, bacteria and eukaryotes. Lon protease is ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins, including some antitoxins. It required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. It degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long and binds to DNA in a double-stranded, site-specific manner. Endogenous substrates include the regulatory proteins RcsA and SulA, the transcriptional activator SoxS, and UmuD. Its overproduction specifically inhibits translation through at least two different pathways, one of them being the YoeB-YefM toxin-antitoxin system.

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Carbonic Anhydrase 8 (CA8) belongs to the alpha-carbonic anhydrase family. Alpha-carbonic anhydrase is a large family of zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide. Because CA8 has some sequence similarity with other known carbonic anhydrase genes, it was firstly called as CA-related protein. Nevertheless, CA8 does not have a carbonic anhydrase catalytic activity. Defects in CA8 are the cause of cerebellar ataxia mental retardation and dysequilibrium syndrome type 3 (CMARQ3), which is a congenital cerebellar ataxia associated with dysarthia, quadrupedal gait and mild mental retardation.

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Isocitrate Dehydrogenase [NADP] Cytoplasmic (IDH1) belongs to the isocitrate and isopropylmalate dehydrogenases family. IDH1 exists as a homodimer, binding one magnesium or manganese ion per subunit. Mutations of IDH1 have been shown to cause metaphyseal chondromatosis with aciduria and are involved in the development of glioma IDH plays a role in the regeneration of NADPH for intraperoxisomal reductions, such as the conversion of 2, 4-dienoyl-CoAs to 3-enoyl-CoAs, as well as in peroxisomal reactions that consume 2-oxoglutarate, namely the alpha-hydroxylation of phytanic acid.

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Glucose-6-phosphate dehydrogenase (from Yeast)

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Deoxycytidine Kinase (DCK) is a member of the DCK/DGK family. DCK exists as a homodimer and is localised to the nucleus. DCK is required for the phosphorylation of the deoxyribonucleosides deoxycytidine (dC), deoxyguanosine (dG), and deoxyadenosine (dA). DCK has broad substrate specificity, and does not display selectivity based on the chirality of the substrate. In addition, DCK is also an essential enzyme for the phosphorylation of numerous nucleoside analogs widely employed as antiviral and chemotherapeutic agents. DCK is clinically important because of its relationship to drug resistance and sensitivity.

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Carboxypeptidase A1 (CPA1) is secreted as a pancreatic peptidase that comes from the precursor form of inactive procarboxypeptidase. CPA1 comprises a signal peptide, a pro region and a mature chain, and can be activated after cleavage of the pro peptide. It has a free C-terminal carboxyl group, with the preference of residues with aromatic or branched aliphatic side chains. CPA1 cleaves the C-terminal amide or ester bond of peptides and involves in zymogen inhibition. Three different forms of human pancreatic procarboxypeptidase A have been isolated. In contrast to procarboxypeptidase B which was always secreted by the pancreas as a monomer, procarboxypeptidase A occurs as a monomer and/or associated to one or two functionally different proteins, such as zymogen E.

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Tryptophan synthase is a multienzyme alpha2 beta 2 complex composed of two protein subunit. Tryptophan synthase catalyses the last two steps in the synthesis of L-tryptophan (L-Trp). The alpha-subunit catalyses cleavage of 3-indole-d-glycerol 3′-phosphate (IGP) to give indole and D-glyceraldehyde 3′-phosphate (G3P). Indole is then transferred through a 25-Å hydrophobic tunnel to the beta -subunit. The beta 2 subunit contains pyridoxal 5'-phosphate and catalyses several pyridoxal 5'-phosphate-dependent reactions, including/3-elimination reactions 6 and a thiol-dependent transamination reaction. This enzyme is commonly found in Eubacteria, Archaebacteria, Protista, Fungi, and Plantae, but is absent from Animalia. As humans do not have tryptophan synthase, this enzyme has been explored as a potential drug target.

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Beta-D-glucuronidase from E. coli is a  highly specific enzyme in hydrolysing glucuronides. Beta-D-glucuronidase (GLUase) activity can be measured as the rate of production of fluorescent methylumbelliferone (MU), resulting from the hydrolysis of the substrate 4-methylumbelliferyl- beta -d-glucuronide (MUGLU), which is an effective and rapid method for detection and verification of E. coli in food, water, and environmental samples. High purity recombinant beta-Glucuronidase is used in research, biochemical enzyme assays and in vitro diagnostic analysis, detecting a wide range of drugs such as opioids, benzodiasepines, steroids, cannabinoids, and others.

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Thymidine kinase 1(TK1) belongs to the thymidine kinase family. It is located in the cytoplasm, and phosphorylated on Ser-13 in mitosis during post-translational modification. Two forms of this protein have been identified in animal cells, one in cytosol TK1 and one in mitochondria TK2. Thymidine kinases have a key function in the synthesis of DNA and thereby in cell division, as they are part of the unique reaction chain to introduce deoxythymidine into the DNA. Activity of the cytosolic enzyme is high in proliferating cells and peaks during the S-phase of the cell cycle, while it is very low in resting cells. TK1 acts as a homotetramer, and can transform thymidime to thymidine 5'-phosphate with the help of ATP.

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LTA4H, which is short for Leukotriene A-4 hydrolase, is a 611 aa. protein. It belongs to the peptidase M1 family, and exists in cytoplasm. This protein has at least 4 isforms produced by alternative splicing, and two of them are expressed in monocytes, lymphocytes, neutrophils, reticulocytes, platelets and fibroblasts. LTA4H involves in lipid metabolism and leukotriene B4 biosynthesis. It is a epoxide hydrolase that catalyses the final step in the biosynthesis of the proinflammatory mediator leukotriene B4. It also has aminopeptidase activity.

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Lysosomal Pro-X Carboxypeptidase (PRCP) belongs to the peptidase S28 family. PRCP is detected in many tissues, with highest levels observed in placenta, lung, and liver. It is also present in the heart, brain, pancreas, and kidney. PRCP exists as a homodimer. PRCP cleaves C-terminal amino acids linked to proline in peptides such as angiotensin II, III and des-Arg9-bradykinin. This cleavage occurs at acidic pH, but enzymatic activity is retained with some substrates at neutral pH. PRCP has been shown to be an activator of the cell matrix-associated prekallikrein.

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Carboxypeptidase M (CPM) belongs to the peptidase M14 family, and exists in cell membrane. The protein binds 1 zinc ion per subunit, and cleavage of C-terminal arginine or lysine residues from polypeptides. CPM specifically removes C-terminal basic residues (Arg or Lys) from peptides and proteins. It is believed to play important roles in the control of peptide hormone and growth factor activity at the cell surface, and in the membrane-localised degradation of extracellular proteins.

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ARG1 is a member of the ureohydrolase family of enzymes. ARG1 can catalyse the hydrolysis of arginine to ornithine and urea. In the urea cycle, ARG1 catalyses the fifth and final step, a series of biochemical reactions in mammals during which the body disposes of harmful ammonia. ARG1 is a cytosolic enzyme and expressed widely in the liver as part of the urea cycle. Inherited deficiency of this ARG1 causes argininemia, which is an autosomal recessive disorder characterised by hyperammonemia.

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Aminoglycoside 3'-phosphotransferase (APH(3')), also known as aminoglycoside kinase, is an aminoglycoside-modifying enzyme and widely presented in resistant bacteria. These ATP-dependent enzymes phosphorylate the 3'-hydroxyl of a variety of aminoglycosides including kanamycins, neomycins, paromomycins, neamine, ribostamycin, geneticin, and paromamine. These phosphorylated aminoglycosides fail to bind to their respective ribosomal binding sites with high affinity; hence resistance is conferred to the drugs that are phosphorylated. APH(3') is primarily found in certain species of gram-positive bacteria.

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Phosphinothricin N-acetyltransferase (PAT) is an enzyme that acetylates the free NH2 group of L-phosphinothricin (L-PPT) in the presence of acetyl-CoA as a co-substrate. It is highly specific for L-PPT and does not acetylate other L-amino acids or structurally similar molecules. L-PPT is a glutamate analog that can inhibit glutamine synthetase activity in plants, resulting in the accumulation of ammonia to toxic levels and impairment of photosynthesis. The introduction of a PAT gene into a plant genome can confer resistance to glufosinate herbicide during post-emergent applications.

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Proteinase-3 is a neutral serine proteinase that belongs to the peptidase S1 family and Elastase subfamily. It contains one peptidase S1 domain and it is expressed mainly in neutrophil granulocytes. The primary function of Proteinase-3 is thought to be degradation of extracellular proteins at sites of inflammation, but excessive or prolonged proteolytic activity may cause harmful effects in the body. It is the epitope of anti-neutrophil cytoplasmic antibodies (ANCAs) of the cANCA (cytoplasmic subtype) class, a type of antibody frequently found in the disease Wegener's granulomatosis.

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Aldo-Keto Reductase 1C4/AKR1C4 is a member of the aldo/keto reductase family that consists of more than 40 known enzymes and proteins. AKR1C4 has highly expressed in Liver. It can catalyses the bioreduction of chlordecone, a toxic organochlorine pesticide, to chlordecone alcohol in liver. AKR1C4 catalyses the transformation of the potent androgen dihydrotestosterone (DHT) into the less active form, 5- alpha-Androstan-3- alpha,17- beta -diol (3- alpha-diol). In addition, AKR1C4 also has some 20- alpha-Hydroxysteroid Dehydrogenase activity.

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Protein disulfide-isomerase A5 is a 519 amino acids protein that belongs to the protein disulfide isomerase family.It contains 3 thioredoxin domains.It can catalyse the rearrangement of -S-S- bonds in proteins.

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Dipeptidase 1 (DPEP1) is a kidney membrane enzyme that belongs to the peptidase M19 family. DPEP1 is a homodimer and is inhibited by L-penicillamine. DPEP1 hydrolyses a variety of dipeptides and is implicated in renal metabolism of glutathione and its conjugates. DPEP1 is responsible for hydrolysis of the beta-lactam ring of antibiotics, such as penem and carbapenem. DPEP1 may play an important role in the regulation of leukotriene activity. DPEP1 expression in cancer is significantly higher than that in normal tissue. However, DPEP1 expression decreased with pathological differentiation, lymph-node and distant metastasis.

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Nicotinate Phosphoribosyltransferase (NAPRTase) is involved in the biological processes of pyridine nucleotide biosynthesis and nicotinate nucleotide salvage and functions by catalyzing the conversion of nicotinic acid (NA) to NA mononucleotide (NaMN). It is a crucial factor in the NAD+ biosynthesis pathway. Catalytic activity: Beta-nicotinate D-ribonucleotide + diphosphate = nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate.

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Carboxypeptidase B1 is an exopeptidase which specifically cleaves the C-terminal Arg and Lys residues with a preference for Arg. Expressed mainly in pancreas, CPB1 is a useful serum marker for acute pancreatitis and pancreatic graft rejection.Human CPB1 consists of a signal peptide, a pro region, and a mature chain. The purified rhCPB1 corresponds to the pro form, which can be activated by trypsin, the only pancreatic protease capable of generating active enzyme from the zymogen in vitro.

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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.

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Caspase-10 (CASP10) is a 521 amino acid protein member of the Cysteine-Aspartic Acid Protease (Caspase) family. CASP10 contains two DED (Death Effector) domains and is detectable in most tissues. CASP10 cleavage by Granzyme B and autocatalytic activity generate the two active subunits: Caspase-10 subunit p23/17, Caspase-10 subunit p12. Caspases are a family of cytosolic aspartate-specific cysteine proteases involved in the execution-phase of cell apoptosis, the initiation and execution. Human caspases can be subdivided into three functional groups: cytokine activation (caspase-1, -4, -5, and -13), apoptosis initiation (caspase-2, -8, -9, -and -10), and apoptosis execution (caspase-3, -6, and -7). CASP10 cleaves and activates caspases 3 and 7, but itself is processed by caspase 8. Defects in CASP10 are associated with apoptosis defects seen in type II autoimmune lymphoproliferative syndrome.

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Sulfotransferase 4A1 (ST4A1) is a member of the Sulfotransferase 1 family. ST4A1 is highly expressed in the cerebral cortex and frontal lobe, but no expression is detected in the pancreas. ST4A1 is a brain-specific sulfotransferase believed to be involved in the metabolism of neurotransmitters. ST4A1 acts on catecholamines and T4 in a manner that may not involve sulfonation. ST4A1 may have a role in the metabolism of drugs and neurotransmitters in the CNS. In addition, ST4A1 is related to schizophrenia.

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Yeast alcohol dehydrogenase

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Fumarylacetoacetase belongs to the FAH family. Fumarylacetoacetase is primary expressed in liver and kidney. It exists as a homodimer and catalyses the hydrolysis of 4-fumarylacetoacetate into fumarate and acetoacetate. Defects in Fumarylacetoacetase cause tyrosinemia type 1, which is congenital metabolism defect characterised by elevated levels of tyrosine in the blood and urine, and hepatorenal manifestations. Typical features include renal tubular injury, self-mutilation, hepatic necrosis, episodic weakness, and seizures.

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Mouse carboxypeptidase A2(CPA2) is a secreted pancreatic procarboxy -peptidase which belongs to the peptidase M14 family. CPA2 consists of a signal peptide, a pro region and a mature chain. It can be activated after cleavage of the pro peptide. CPA2 cleaves the C-terminal amide or ester bond of peptides that have a free C-terminal carboxyl group. The hydrolytic action of CPA2 was identified with a preference towards long substrates with aromatic amino acids in their C-terminal end, particularly tryptophan.

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Fructose-bisphosphate aldolase C (ALDOC) belongs to the class I fructose-bisphosphate aldolase family. It is an enzyme that, in humans, is encoded by the ALDOC gene. ALDOC is expressed exclusively in the hippocampus and Purkinje cells of the brain. ALDOC is a glycolytic enzyme which catalyses the reversible aldol cleavage of fructose-1,6-biphosphate and fructose 1-phosphate to dihydroxyacetone phosphate and either glyceraldehyde-3-phosphate or glyceraldehydes respectively