You searched for: Enzymes

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Mouse Lactate dehydrogenase A (LDHA) is a member of the LDH/MDH superfamily and LDH family. LDHA catalyses the inter-conversion of pyruvate and L-lactate with concomitant inter-conversion of NADH and NAD+. LDHA is found in most somatic tissues, though predominantly in muscle tissue and tumours. It has also been shown that LDHA plays an important role in the development, invasion and metastasis of malignancies. Mutations in LDHA have been linked to exertional myoglobinuria.

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GDP-L-Fucose Synthase is a NADP(H)-binding protein. It catalyses the two-step epimerase and the reductase reactions in GDP-D-mannose metabolism, converting GDP-4-keto-6-D-dexoymannose to GDP-L-fucose. GDP-L-Fucose is the substrate of several fucosyltransferase, involving the expression of mamy glycoconjugates, including blood group ABH antigens and development adhesion antigens. Mutations in the TSTA3 gene may cause leukocyte adhesion deficiency type II.

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Acyl-Protein Thioesterase 2 is a cytoplasmic protein that belongs to the AB Hydrolase 2 family. LYPLA2 is a lysophospholipase and hydrolyses fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS. LYPLA2 has hydrolase activity that converts Palmitoyl-protein to palmitate and protein. LYPLA2 regulates the multifunctional lysophospholipids by acting on biological membranes. LYPLA2 participates in Glycerophospholipid metabolism pathway, fatty acid metabolic process and lipid metabolic process.

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Phosphomannomutase 1 (PMM1) blongs to the eukaryotic PMM family. Phosphomannomutase 1 can catalyses the conversion between D-mannose 6-phosphate and D-mannose 1-phosphate which is a substrate for GDP-mannose synthesis. GDP-mannose is used for synthesis of dolichol-phosphate-mannose which required for a number of critical mannosyl transfer reactions. PMM1 is highly expressed in liver, heart, brain, and pancreas, but lower expression in skeletal muscle. In addition, PMM1 may be responsible for the degradation of glucose-1,6 bisphosphate in ischemic brain.

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CAMK1D is a serine/threonine kinase that is a member of the calcium/calmodulin-dependent protein kinase family. It contains a protein kinase domain. CAMK1D expressed in polymorphonuclear leukocytes and may be part of the chemokine signal transduction pathway that regulates granulocyte function. It may also be involved in modulation of neuronal apoptosis. It activates CREB-dependent gene transcription, regulates calcium-mediated granulocyte function and respiratory burst and promotes basal dendritic growth of hippocampal neurons.

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Lysine-tRNA ligase, also known as Lysyl-tRNA synthetase, LysRS, KARS and KIAA0070, belongs to the class-II aminoacyl-tRNA synthetase family. The N-terminal cytoplasmic domain (1-65) is a functional tRNA-binding domain, which is required for nuclear localisation, is involved in the interaction with DARS, but has a repulsive role in the binding to EEF1A1. A central domain (208-259) is involved in homodimerisation and is required for interaction with HIV-1 GAG and incorporation into virions. KARS catalyses the specific attachment of an amino acid to its cognate tRNA in a two step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. Defects in KARS are the cause of Charcot-Marie-Tooth disease recessive intermediate type B (CMTRIB).

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Dipeptidyl peptidase 3(DPP3), is a member of the S9B family in clan SC of the serine proteases. DPP3 has post-proline dipeptidyl aminopeptidase activity, cleaving Xaa-Pro dipeptides from the N-termini of proteins. This cytoplasmic protein binds a single zinc ion with its zinc-binding motif (HELLGH). It releases an N-terminal dipeptide from a peptide comprising four or more residues, with broad specificity and also acts on dipeptidyl 2-naphthylamides.Increased activity of this protein has a relationship with endometrial and ovarian cancers.

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Fructose-1,6-Bisphosphatase 1 (FBPase 1) is a member of the FBPase class 1 family. FBPase 1 is a gluconeogenesis regulatory protein, which catalyses the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate and inorganic phosphate. FBPase 1 can assume an active R-state, or an inactive T-state. FBPase 1 deficiency is inherited as an autosomal recessive disorder mainly in the liver and causes life-threatening episodes of hypoglycemia and metabolic acidosis in newborn infants or young children. FBPase 1 coupled with phosphofructokinase (PFK) is involved in the metabolism of pancreatic islet cells.

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Pyruvate Kinase Isozymes R/L (PKLR) belongs to the pyruvate kinase family, There are 4 isozymes of pyruvate kinase in mammals: L, R, M1 and M2. L type is major isozyme in the liver; R is found in red cells; M1 is the main form in muscle, heart and brain; M2 is found in early fetal tissues. PKLR exists as a homotetramer and catalyses the production of phosphoenolpyruvate from pyruvate and ATP. Defects in PKLR are also the cause of pyruvate kinase deficiency of red cells, which is a frequent cause of hereditary non-spherocytic hemolytic anemia.

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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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Isopentenyl Pyrophosphate Isomerase 2 (IDI2) belongs to the IPP isomerase type 1 family. Both isozymes, IDI1 and IDI2 are localised to the peroxisome by a PTS1-dependent pathway. IDI2 is expressed in skeletal muscle, which contains one nudix hydrolase domain. IDI2 binds one magnesium per subunit. IDI2 catalyses the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). It is reported that IDI2 is regulated independently from IDI1, by a mechanism that may involve PPAR- alpha.

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Calcium/Calmodulin-Dependent Protein Kinase Type 1 (CAMK1) belongs to the protein kinase superfamily, CAMK Ser/Thr protein kinase family, and CaMK subfamily. CAMK1 contains one protein kinase domain and widely expressed. CAMK1 is phosphorylated by CaMKK1 and CaMKK2 on Thr-177. CAMK1 regulates transcription activators activity, cell cycle, hormone production, cell differentiation, actin filament organisation, and neurite outgrowth. CAMK1 plays a role in K+ and ANG2-mediated regulation of the aldosterone synthase (CYP11B2) to produce aldosterone in the adrenal cortex.

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Carboxypeptidase A4 (CPA4) is a member of the peptidase M14 family. CPA4 is metalloprotease that could be involved in the histone hyperacetylation pathway. CPA4 binds one zinc ion per subunit and could catalyse to release of a C-terminal amino acid, with preference for -Phe, -Leu, -Ile, -Met, -Tyr and -Val.They have distinct expression patterns and different specificities for example, preferentially cleaving aromatic (carboxypeptidase As) or basic (carboxypeptidase Bs) residues. Several, such as carboxypeptidase Xs, have lost their catalytic activity. Carboxypeptidases play important roles in digestion of food, processing of bioactive peptides and blood coagulation.

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Trans-2-Enoyl-CoA Reductase Mitochondrial (MECR) belongs to the zinc-containing alcohol dehydrogenase family. MECR localises to the mitochondrion. It is highly expressed in skeletal and heart muscle and expressed at lower levels in the placenta, liver, kidney and pancreas, with weakly or no expression in the lung. MECR exists as a homodimer, which catalyses the reduction of trans-2-enoyl-CoA to acyl-CoA with chain length from C6 to C16 in an NADPH-dependent manner with preference to medium chain length substrate. MECR may take part in the mitochondrial synthesis of fatty acids.

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Sialate O-Acetylesterase (SIAE) belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. SIAE is widely expressed with high expression levels in the testis, prostate, and colon. SIAE catalyses N-acetyl-O-acetylneuraminate and H2O to N-acetylneuraminate and acetate. SIAE removes O-acetyl ester groups from position 9 of the parent sialic acid, N-acetylneuraminic acid. SIAE down-regulates B lymphocyte antigen receptor signaling (involving CD22), and is required for immunological tolerance. Loss of function mutations in SIAE are much more frequently found in humans with autoimmune diseases especially rheumatoid arthritis and type 1 diabetes.

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Peptidyl-prolyl cis-trans isomerase FKBP2(FKBP2 for short), also named 13 kDa FK506-binding protein, FK506-binding protein 2, Immunophilin FKBP13, Rotamase, is a endoplasmic reticulum peripheral membrane protein. It contains 1 PPIase FKBP-type domain and belongs to the FKBP-type PPIase family, FKBP2 subfamily which takes part in immunoregulation and basic cellular processes involving protein folding and trafficking. FKBP2 is a cis-trans prolyl isomerase that binds the immunosuppressants FK506 and rapamycin. FKBP2 functions as an ER chaperone and as a component of membrane cytoskeletal scaffolds.

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Aspartoacylase 3, also known as ACY3, N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming), Acylase III, Aminoacylase-3, Aspartoacylase-2, Aspartoacylase-2, HCV core-binding protein 1 and ASPA2, is a member of the Aspartoacylase subfamily. ACY3 plays an important role in deacetylating mercapturic acids in kidney proximal tubules and acts on N-acetyl-aromatic amino acids.ACY3 is located in the cytoplasm of S2 and S3 proximal tubules and the apical domain of S1 proximal tubules. ACY3 protein is also expressed at low levels in stomach, testis, heart, brain, lung and liver, and may function as an HCV (Hepatitis C virus) core binding protein.

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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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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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Recombinant Human Proprotein Convertase Subtilisin/Kexin Type 9/PCSK9 (D374Y) is a gain of function mutant of human PCSK9 protein. Human PCSK9 is a secretory subtilase belonging to the proteinase K subfamily. PCSK9 is synthesised as a soluble zymogen that undergoes autocatalytic intramolecular processing in the ER, the pro domain and mature chain are secreted together through noncovalent interactions. PCSK9 binds with low-density lipoprotein receptor (LDLR) and it plays a major regulatory role in cholesterol homeostasis. Inhibition of PCSK9 function by preventing PCSK9/LDLR interaction is currently being explored as a means of lowering cholesterol levels. PCSK9 also binds to apolipoprotein receptor 2 (ApoER2), and play a role in the neural development.

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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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Carboxypeptidase A2 (CPA) is a secreted pancreatic procarboxy-peptidase that 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. CPA2 comprises a signal peptide, a pro region and a mature chain, and can be activated after cleavage of the pro peptide. Three different forms of human pancreatic procarboxypeptidase A have been isolated, and the A1 and A2 forms are always secreted as monomeric proteins with different biochemical properties. 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, and is involved in zymogen inhibition.

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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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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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Ubiquinone Biosynthesis Protein COQ7 Homolog (COQ7) is a mitochondrion inner membrane and peripheral membrane protein which belongs to the COQ7 family. It is expressed dominantly in heart and skeletal muscle. COQ7 is synthesised as a preprotein that is imported into the mitochondrial matrix, where the sequence is cleaved off and the mature protein becomes loosely associated with the inner membrane. COQ7 is involved in lifespan determination in ubiquinone-independent manner and also involved in ubiquinone biosynthesis. COQ7 is potential central metabolic regulator. Human COQ7 protein contains 179 amino acids, is mostly helical, and contains an alpha-helical membrane insertion. It has been shown that mutations in the gene are associated with increased life span. Defects of the gene slow down a variety of developmental and physiological processes, including the cell cycle, embryogenesis, post-embryonic growth, rhythmic behaviors and aging.

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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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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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The active form of CPE cleaves C-terminal amino acid residues of the peptide, and is thus involved in the biosynthesis of peptide hormones and neurotransmitters including insulin, enkephalin, etc. It is thought that membrane-associated CPE acts as a sorting receptor for targeting regulated secretory proteins which are mostly prohormones and neuropeptides in the trans-Golgi network of the pituitary and in secretory granules into the secretory pathway. Defects in this protein are implicated in type II diabetes due to impaired glucose clearance and insulin resistance.

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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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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.