Hledali jste: Enzymy
Enzymes accelerate, or catalyse, chemical reactions, and they are known to catalyse more than 5,000 biochemical reaction types. Most enzymes are proteins, although a few are catalytic RNA molecules. Choose specific enzymes for cleaving bonds, removing genomic DNA from RNA preparations, for producing fragments of proteins, or for use in ion exchange chromatography. Enzymes are used in the chemical industry and other industrial applications when extremely specific catalysts are required.
Human recombinant Carbonic Anhydrase 10 (from Cells)
Supplier: ProSci Inc.
Carbonic Anhydrase X (CA10) belongs to CA family of zinc metalloenzymes, which catalyze the reversible hydration of carbon dioxide in various biological processes such as respiration, renal tubular acidification and bone resorption. While CA10 is a secreted protein without Carbonic Anhydrase activity (i.e., the reversible hydration of CO2) due to point mutations in the zinc binding site, it has esterase activity. The human and mouse CA10 are expressed in the brain, indicating that they may play a role in brain development.
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Human recombinant Aldolase A (from E. coli)
Supplier: ProSci Inc.
Fructose Bisphosphate Aldolase A (ALDOA) belongs to the class I fructose-bisphosphate aldolase family. ALDOA is a glycolytic enzyme that catalyses the reversible conversion of fructose-1,6-bisphosphate to glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. In vertebrates, three forms of this ubiquitous glycolytic enzyme are found, Aldolase A in muscle, Aldolase B in liver and aldolase C in brain. Aldolase A Interacts with SNX9 and WAS. Aldolase A deficiency has been associated with myopathy and hemolytic anemia. In addition, Aldolase A plays an important role in glycolysis and gluconeogenesis; it may also act as a scaffolding protein.
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Human recombinant Cyclin-Dependent Kinase 2 (from E. coli)
Supplier: ProSci Inc.
Cyclin-dependent kinase 2 (CDK2) belongs to the cyclin-dependent kinase of Ser/Thr protein kinase. CDK2 acts as a catalytic subunit of the cyclin dependent kinase complex, whose activity is restricted to the G1-S phage of the cell cycle, it is essential for the G1/S transition. The kinase activity of CDK2 can be regulated by the association with a cyclin subunit, its phosphorylation state and CDK inhibitors. The activation of the CDK2/cyclin complex requires the phosphorylation of Thr160 and the dephosphorylation of Try14 and Tyr15. The inhibition of CDK2-cyclin complex can also be attributed to association with p27Kip1 and p21Waf1/Cip1. The activation of CDK2 has been shown to be necessary for apoptosis of quiescent cells, such as neurons, thymocytes and endothelial cells.
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Human recombinant prostaglandin-D2 Synthase (from cells)
Supplier: ProSci Inc.
Prostaglandin-H2 D-Isomerase (PTGDS) belongs to the Lipocalin family of calycin superfamily. PTGDS is preferentially expressed in the brain. PTGDS catalyses the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation. PTGDS is involved in a variety of CNS functions, such as sedation, REM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in oligodendrocytes. PTGDS binds small non-substrate lipophilic molecules and may act as a scavenger for harmful hydrophopic molecules and a secretory retinoid and thyroid hormone transporter. It possibly participates in development and maintenance of the blood-brain, blood-retina, blood-aqueous humor, blood-testis barrier, the central nervous system and male reproductive system.
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Pig Trypsin (from Pancreas)
Supplier: PanReac AppliChem
Pig Trypsin (from Pancreas)
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Mouse recombinant carboxylesterase 2E
Supplier: ProSci Inc.
Carboxylesterase 5 (CES5), also called cauxin or CES7, is a member of carboxylesterases family which plays an important role in the hydrolysis of ester and amide bonds. Carboxylesterase is a type of enzyme that capable of hydrolysing a variety of carboxylic acid esters and it's widely distributed in cells especially in mammalian liver. CES5 is with broad substrate specificity ranging from small molecule esters to longchain fatty acid esters and thioesters. It has been previously reported CES5 was in high concentrations in the urine (cauxin) of adult male cats, and within a protein complex of mammalian male epididymal fluids. Roles for CES5 may include regulating urinary levels of male cat pheromones, catalysing lipid transfer reactions within mammalian male reproductive fluids, and protecting neural tissue from drugs and xenobiotics.
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Human Recombinant Glycine N-Methyltransferase (from E. coli)
Supplier: ProSci Inc.
Glycine N-Methyltransferase (GNMT) is a tetrameric cytosolic protein. GNMT catalyses the synthesis of N-methylglycine from glycine using S-adenosylmethionine (AdoMet) as the methyl donor. It can affects DNA methylation by regulating the ratio of S-adenosylmethionine to S-adenosylhomocystine, playing an important role in maintaining normal AdoMet levels. GNMT is highly expressed in liver. As a major folate-binding protein, GNMT takes part in the detoxification pathway. Defects in GNMT are the cause of hypermethioninemia. the patients with this deficiency are mild hepatomegaly and chronic elevation of serum transaminases.
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H. influenzae recombinant NAD Nucleotidase (from E. coli)
Supplier: ProSci Inc.
NadN (NAD nucleotidase) is a periplasmic enzyme from Haemophilus influenzae, a major pathogen of the respiratory tract in humans that has developed the capability to exploit host NAD(P) for its nicotinamide dinucleotide requirement. NadN plays a central role by degrading NAD into adenosine and NR (nicotinamide riboside), NMN to nicotinamide riboside and AMP to adenosine. It shows a broad substrate specificity, recognising either mono- or di-nucleotide nicotinamides and different adenosine phosphates with a maximal activity on 5'-adenosine monophosphate. It can be used as an economically alternative to produce NR (nicotinamide riboside). Catalytic activity: NAD=AMP + NMN=Ade+NR+PPi | AMP=Ade+Pi | NMN=NR+Pi.
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Human recombinant Aminopeptidase P2 (from cells)
Supplier: ProSci Inc.
Xaa-Pro aminopeptidase 2 (XPNPEP2) belongs to the peptidase M24B family of metalloproteases. Human XPNPEP2 is widely expressed in various tissues, such as kidney, lung, heart, placenta, liver, small intestine and colon. However, it doesn’t express in brain, skeletal muscle, pancreas, spleen, thymus, prostate, testis and ovary. XPNPEP2 is a Homotrimer which binds 2 manganese ions per subunit. The metalloprotease XPNPEP2 may play a role in the inflammatory process and other reactions produced in response to injury or infection and the metabolism of the vasodilator bradykinin.
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Human recombinant Cystathionine Gamma-Lyase (from E. coli)
Supplier: ProSci Inc.
Cystathionine Gamma-Lyase (CTH) belongs to the trans-sulfuration enzymes family. CTH exists as a homotetramer and interacts with CALM in a calcium-dependent manner. CTH breaks down cystathionine into cysteine, ammonia and 2-oxobutanoate. CTH catalyses the last step in the trans-sulfuration pathway from methionine to cysteine and has broad substrate specificity. Defects in CTH will lead to cystathioninuria, which is an autosomal recessive phenotype characterised by abnormal accumulation of plasma cystathionine.
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E. coli recombinant tryptophan synthase (from E. coli)
Supplier: ProSci Inc.
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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Human recombinant beta-Galactosidase (from Cells)
Supplier: ProSci Inc.
beta Galactosidase is a lysosomal beta Galactosidase that hydrolyses the terminal beta Galactose from Ganglioside and Keratan sulfate. In lysosome, the mature beta Galactosidase protein associates with Cathepsin A and Neuraminidase 1 to form the lysosomal multienzyme complex . An alternative splicing at the RNA level of beta Galactosidase results a catalytically inactive beta Galactosidase that plays an important role in vascular development. Defects of beta -galactosidase (GLB1) are the cause of diseases like GM1-gangliosidosis which is a lysosomal storage disease and Morquio Syndrome B that cause patients to have abnormal elastic fibers. More than 100 mutations have been identified for beta Galactosidase, which result in different residual activities of the mutant enzymes and a spectrum of symptoms in the two related diseases.
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Human recombinant uridine phosphorylase 1 (from E. coli)
Supplier: ProSci Inc.
Uridinephosphorylase 1 (UPP1) is a member of the family of pentosyltransferase. UPP1 catalyses the reversible phosphorolysis of uridine to uracil. The expression levels and the enzymatic activity of UPP1 are higher in human solid tumors than in adjacent normal tissues. The high level of UPP1 expression in some tumors makes it a potential prognosticfactor for some cancers, such as oral squamous cell carcinoma. UPP1 is important for the homeostatic regulation of intracellular and plasma uridine concentratios. UPP1 plays an important role in the pyrimidine salvage pathway through its catalysis of the reversible phosphorolysis of uridine to uracil.
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Corning® Trypsin
Supplier: Corning
0,05% Trypsin/0,53 mM EDTA in HBSS (Hank’s Balanced Salt Solution) with sodium bicarbonate, without calcium and magnesium.
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Human recombinant alpha-Galactosidase A (from cells)
Supplier: ProSci Inc.
alpha-Galactosidase A is a homodimeric glycoprotein that belongs to the glycosyl hydrolase 27 family. It is a lysosomal enzyme and used as a long-term enzyme replacement therapy in patients with a confirmed diagnosis of Fabry disease. alpha-Galactosidase A can hydrolyze terminal alpha-galactosyl moieties from glycolipids and glycoproteins and catalyze the hydrolysis of melibiose into galactose and glucose. Defects alpha-Galactosidase A are the cause of Fabry disease (FD) which is a rare X-linked sphingolipidosis disease with glycolipid accumulates in many tissues. The disease consists of an inborn error of glycosphingolipid catabolism. FD patients show systemic accumulation of globotriaoslyceramide (Gb3) and related glycosphingolipids in the plasma and cellular lysosomes throughout the body. Patients may show ocular deposits, febrile episodes, and burning pain in the extremities. Death results from renal failure, cardiac or cerebral complications of hypertension or other vascular disease.
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M. tuberculosis Recombinant NAD Synthetase (from E. coli)
Supplier: ProSci Inc.
NAD synthetase is an essential enzyme involved in both the de novo biosynthesis and salvage of NAD+, catalysing the final step of both pathways. Since NAD has a vital role in cell metabolism, the enzyme represents a valid target for the development of new antimycobacterial agents. It can use both glutamine or ammonia as a nitrogen source. Catalytic activity: ATP + deamido-NAD+ + L-glutamine + H₂O = AMP + diphosphate + NAD+ + L-glutamate.
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M. tuberculosis Recombinant NAD Kinase (from E. coli)
Supplier: ProSci Inc.
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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Mouse recombinant carbonic anhydrase 14 (from E. coli)
Supplier: ProSci Inc.
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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Human recombinant Fructose-1,6-Bisphosphatase 1 (from cells)
Supplier: ProSci Inc.
Fructose-1,6-bisphosphatase 1(FBP1) is a homotetramer protein and belongs to the FBPase class 1 family. It involves in carbohydrate biosynthesis; gluconeogenesis pathway. FBP1 is a gluconeogenesis regulatory protein which catalyses the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate and inorganic phosphate. FBP1 deficiency is associated with hypoglycemia and metabolic acidosis. FBP1 regulates mouse endogenous glucose production. FBP1 coupled with phosphofructokinase (PFK) takes part in the metabolism of pancreatic islet cells.
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Human recombinant CaM Kinase II subunit beta (from E. coli)
Supplier: ProSci Inc.
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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Human recombinant B Lymphocyte Kinase (from E. coli)
Supplier: ProSci Inc.
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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Human recombinant Alkaline Phosphatase (from cells)
Supplier: ProSci Inc.
Alkaline Phosphatase, Tissue-Nonspecific Isozyme (ALPL) is a cell membrane protein which belongs to the alkaline phosphatase family. There are at least four distinct but related alkaline phosphatases in humans: intestinal AP (IAP), placental AP(PLAP), germ cell AP (GCAP) and their genes are clustered on chromosome 2, tissue-nonspecific isozyme (TNAP) which gene is located on chromosome 1. Alkaline phosphatases (APs) are dimeric enzymes, it catalyse the hydrolysis of phosphomonoesters with release of inorganic phosphate. The native ALPL is a glycosylated homodimer attached to the membrane through a GPI-anchor. This isozyme may play a role in skeletal mineralisation. Mutations in ALPL gene have been linked directly to different forms of hypophosphatasia,characterised by poorly mineralised cartilage and bones, and this disorder can vary depending on the specific mutation since this determines age of onset and severity of symptoms.
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Human recombinant Carbonic Anhydrase 10 (from E. coli)
Supplier: ProSci Inc.
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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Human recombinant Chitinase 3-like 2 (from cells)
Supplier: ProSci Inc.
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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Human recombinant PPIase D (from E. coli)
Supplier: ProSci Inc.
Peptidyl-Prolyl Cis-Trans Isomerase D (PPID) belongs to the cyclophilin-type PPIase family and PPIase D subfamily. PPID is widely expressed and it contains one PPIase cyclophilin-type domain and three TPR repeats. PPID catalyses the cis-trans isomerisation of proline imidic peptide bonds in oligopeptides and accelerates the folding of proteins. PPID can bind to the immunosuppressant cyclosporine A and is known that its overexpression suppresses the apoptosis in cancer cells.
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Human recombinant Chitinase-3-like 1 (from cells)
Supplier: ProSci Inc.
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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E. coli recombinant RNA pyrophosphohydrolase (from E. coli)
Supplier: ProSci Inc.
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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Human recombinant sulphotransferase 1B1 (from E. coli)
Supplier: ProSci Inc.
Sulfotransferase Family Cytosolic 1B Member 1 (SULT1B1) is a cytosolic enzyme that belongs to the Sulfotransferase 1 family. Human SULT1B1 is a 296 amino acid protein that is highly expressed in the liver, peripheral blood leukocytes, colon, small intestine, and spleen. SULT1B1 utilises 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor, and it can catalyse the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds.
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Human recombinant sulphotransferase 1C4 (from E. coli)
Supplier: ProSci Inc.
Human Sulfotransferase (SULT1C4) is an enzyme that in humans is encoded by the SULT1C4 gene, belongs to the sulfotransferase 1 family. SULT1C4 is expressed at high levels in fetal lung and kidney and at low levels in fetal heart, adult kidney, ovary and spinal chord. Sulfotransferase utilises 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyse the sulfate conjugation of drugs, xenobiotic compounds, hormones, and neurotransmitters. It shows activity towards p-nitrophenol and N-hydroxy-2-acetylamino-fluorene (N-OH-2AAF). SULT1C4 plays an important role incatalyzing the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds.