You searched for: Enzymy

Supplier: OMEGA BIO-TEK

Proteinase K Solution

Supplier: G-Biosciences

Recombinant human caspases 1 - 3 and 6 - 10 are supplied lyophilised in quantities of 25 units. One unit of the specific recombinant caspase is the enzyme activity that cleaves one nanomole of a specific caspase substrate per hour at 37 °C in a reaction solution containing 50mM HEPES (at a pH of 7,2), 50 mM NaCl, 0,1% CHAPS, 10 mM EDTA, 5% glycerol and 10 mM DTT.

Supplier: G-Biosciences

Recombinant human caspases 1 - 3 and 6 - 10 are supplied lyophilised in quantities of 25 units. One unit of the specific recombinant caspase is the enzyme activity that cleaves one nanomole of a specific caspase substrate per hour at 37 °C in a reaction solution containing 50mM HEPES (at a pH of 7,2), 50 mM NaCl, 0,1% CHAPS, 10 mM EDTA, 5% glycerol and 10 mM DTT.

Supplier: G-Biosciences

Recombinant human caspases 1 - 3 and 6 - 10 are supplied lyophilised in quantities of 25 units. One unit of the specific recombinant caspase is the enzyme activity that cleaves one nanomole of a specific caspase substrate per hour at 37 °C in a reaction solution containing 50mM HEPES (at a pH of 7,2), 50 mM NaCl, 0,1% CHAPS, 10 mM EDTA, 5% glycerol and 10 mM DTT.

Supplier: EDVOTEK

Proteinase K

Supplier: G-Biosciences

Recombinant human caspases 1 to 3 and 6 to 10 are supplied lyophilised in quantities of 25 units. One unit of the specific recombinant caspase is the enzyme activity that cleaves one nanomole of a specific caspase substrate per hour at 37 °C in a reaction solution containing 50mM HEPES (at a pH of 7,2), 50 mM NaCl, 0,1% CHAPS, 10 mM EDTA, 5% glycerol and 10 mM DTT.

Supplier: Thermo Fisher Scientific

The Pierce™ Human Rhinovirus (HRV) 3C Protease is a recombinant cysteine protease used to remove fusion tags from proteins with the HRV 3C cleavage sequence and is dual tagged for easy removal from the sample after cleavage.

Supplier: Thermo Fisher Scientific

Cellulase

Supplier: ProSci Inc.

Mouse Carboxylesterases 3 (CES3) is a member of five families of mammalian carboxylesterases that plays a role in catalysing hydrolytic and transesterification reactions with xenobiotics, anticancer pro-drugs and narcotics, and detoxifying organophosphates and insecticides. Mammalian carboxylesterases are enzymes with broad substrate specificities ranging from small molecule esters to longchain fatty acid esters. It is shown that CESs has key roles in the metabolism of a wide variety of clinical drugs, illicit narcotics and chemical nerve agents. CES3 is broadly expressed in liver, colon and brain.

Supplier: ProSci Inc.

Protein Disulfide-Isomerase A6 (PDIA6) is a 48.5kDa protein that belongs to the protein disulfide isomerase family (PDI). PDIA6 is an enzyme in the endoplasmic reticulum in eukaryotes which catalyses the formation and breakage of disulfide bonds between cysteine residues within proteins as they fold. The PDIA6 expressed in platelets, its functions as a chaperone that inhibits aggregation of misfolded proteins. PDIA6 is part a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1. PDIA6 also plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin.

Supplier: ProSci Inc.

Sulfotransferase 1A2 (SULT1A2) is a member of the Sulfotransferase 1 family. Sulfotransferase enzymes catalyse the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds. SULT1A2 is a cytoplasmic protein and exists as a homodimer. SULT1A2 mediates the metabolic activation of carcinogenic N-hydroxyarylamines to DNA binding products and might thus participate as a modulating factor of cancer risk.

Supplier: ProSci Inc.

Kidney-Type Arginase (ARG2) is a member of the arginase family. Arginase is a manganese-containing enzyme which catalyses the hydrolysis of arginine to ornithine and urea. ARG2 is highly expressed in kidney and prostate, not founded in the liver, heart and pancreas. ARG2 has been implicated in the regulation of the arginine/ornithine concentrations in the cell. ARG2 may take part in the regulation of extra-urea cycle arginine metabolism and in down-regulation of nitric oxide synthesis. The extrahepatic arginase functions to regulate L-arginine bioavailability to NO synthase.

Supplier: ProSci Inc.

Deoxyuridine 5'-Triphosphate Nucleotidohydrolase Mitochondrial (dUTPase) belongs to the dUTPase family. dUTPase exits as a homotrimer and is involved in nucleotide metabolism. dUTPase produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. The dUTPase increase in PCR product yield, length and fidelity enables further down-stream applications. These effects make dUTPase useful in PCR fidelity and yield-sensitive applications. dUTPase is specific for dUTP and is critical for the fidelity of DNA replication and repair.

Supplier: ProSci Inc.

Aldehyde Dehydrogenase Family 1 Member A1 (ALDH1A1) is a cytoplasmic enzyme that belongs to the Aldehyde Dehydrogenase family. ALDH1A1 is the second enzyme of the major oxidative pathway of alcohol metabolism. Two major liver isoforms of this enzyme, cytosolic and mitochondrial, can be distinguished by their electrophoretic mobilities, kinetic properties and subcellular localisations. ALDH1A1 is the main cytosolic isoform, which has a lower affinity for aldehydes than the mitochondrial enzyme. ALDH1A1 binds free retinal and cellular retinol-binding protein-bound retinal. It can convert/oxidise retinaldehyde to retinoic acid.

Supplier: ProSci Inc.

These enzymes remove C-terminal amino acids from peptides and proteins and exert roles in the physiological processes of blood coagulation/fibrinolysis, inflammation, food digestion and pro-hormone and neuropeptide processing. CPM is widely distributed in a variety of tissues and cells. CPM is involved in peptide metabolism on both the cell surface and in extracellular fluids. CPM functions not only as a protease but also as a binding partner in cell-surface protein-protein interactions.

Supplier: ProSci Inc.

Ribonuclease 3 (RNASE3) is a basic protein that is localised to the eosinophil primary matrix and belongs to the pancreatic ribonuclease family. RNASE3 is released during degranulation of eosinophils. RNASE3 possesses a wide variety of biological activities. RNASE3 interacts with bacterial lipopolysaccharide (LPS) and lipoteichoic acid (LTA). RNASE3 exhibits antibacterial activity, including cytoplasmic membrane depolarisation of preferentially Gram-negative, but also Gram-positive strains. It promotes E. coli outer membrane detachment, alteration of the overall cell shape and partial loss of cell content.

Supplier: ProSci Inc.

Peptidyl-Prolyl Cis-Trans Isomerase FKBP7 (FKBP7) is a member of the FKBP-type peptidyl-prolyl cis/trans isomerase (PPIase) family. FKBP7 contains two EF-hand domains and one PPIase FKBP-type domain. FKBP7 exhibits PPIase activity and function as molecular chaperones. In addition, FKBP7 accelerates the folding of proteins during protein synthesis. It has been shown that Hsp90 complex to the nucleus bind its PPIase domain to cytoplasmic dynein, the motor protein responsible for retrograde movement along microtubules.

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.

Supplier: ProSci Inc.

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.

Supplier: ProSci Inc.

Thimet Oligopeptidase (THOP1) belongs to the peptidase M3 family which includes neurolysin and mitochondrial intermediate peptidase. THOP1 is located in Cytoplasm. THOP1 is widely expressed in human tissues and can detected in different subcellular locations. THOP1 is preferential cleavage for bonds with hydrophobic residues at P1, P2 and P3' and a small residue at P1' in substrates of 5 to 15 residues. THOP1 is involved in the metabolism of neuropeptides under 20 amino acid residues and degradation of cytoplasmic peptide. In addition, THOP1 also can degrade the beta-amyloid precursor protein and generate amyloidogenic fragments.

Supplier: ProSci Inc.

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.

Supplier: ProSci Inc.

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.

Supplier: ProSci Inc.

SENP2 is an enzyme that belongs to the peptidase C48 family. SENP2 is a protease that catalyses two essential functions in the SUMO pathway: processing of full-length SUMO1, SUMO2 and SUMO3 to their mature forms and deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins. SUMO1 is a small ubiquitin-like protein that can be covalently conjugated to other proteins. It has been implicated as a down-regulator of CTNNB1 levels and may therefore be a modulator of the Wnt pathway.

Supplier: ProSci Inc.

Sulfotransferase 1A3/1A4 (SULT1A3) is 295 amino acids in length and localises to the cytoplasm. It is a member of the Sulfotransferase 1 family. SULT1A3 can be found in the liver, colon, kidney, lung, brain, spleen, small intestine, placenta, and leukocytes. SULT1A3 exists as a homodimer and it catalyses the sulfation of phenolic monoamines, such as dopamine, norepinephrine and serotonin, and phenolic and catecholic drugs.

Supplier: ProSci Inc.

Sulfotransferase 1A1 (SULT1A1) is a cytosolic sulfotransferases that is expressed in the liver, lung, adrenal, brain, platelets, and skin. SULT1A1 is a phenol sulfotransferases with thermostable enzyme activity. SULT1A1 utilises 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyse the sulfate conjugation of catecholamines, phenolic drugs and neurotransmitters. It is responsible for the sulfonation and activation of minoxidil. SULT1A1 mediates the metabolic activation of carcinogenic N-hydroxyarylamines to DNA binding products and could so participate as modulating factor of cancer risk.

Supplier: ProSci Inc.

Carnosine Dipeptidase 1 (CNDP1) belongs to the M20 metalloprotease family. CNDP1 is specifically expressed in the brain, serum and adult nervous central system. It is identified as human carnosinase. CNDP1 contains trinucleotide (CTG) repeat length polymorphism in the coding region and is inhibited by the metal chelator 1,10-o-phenantrolin. In addition, CNDP1 can hydrolyse the beta-Ala|-His dipeptide (carnosine), anserine, Xaa-|-His dipeptides and other dipeptides including homocarnosine. CNDP1 deficiency has been associated with homocarnosinosis disease.

Supplier: ProSci Inc.

Carbonic Anhydrase (CA) XII, also known as Car12 and CA12, is an extracellular enzyme involved in the regulation of the microenvironment acidity and tumour malignant phenotype, was originally identified as a protein overexpressed in some types of cancers. It has showed that CA XII is induced by hypoxia and oestrogen and expressed at high levels on various types of cancer. The enzyme is directly involved in tumour progression, and its inhibition has an anti-tumour effect. Apart from its role in carcinogenesis, the enzyme contributes to various other diseases like glaucoma and arteriosclerotic plaques, among others. CA XII is therefore regarded as promising target for specific therapies, and may be used as a novel prognostic marker in combination with histologic grade of the tumours.

Supplier: ProSci Inc.

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.

Supplier: ProSci Inc.

beta -1,4-galactosyltransferase 4 (B4GALT4) is a single-pass type II membrane protein that belongs to the Glycosyltransferase 7 family. B4GALT4 consist of the following 2 domains: N-Acetyllactosamine Synthase and beta -N-Acetylglucosaminyl-Glycolipid beta -1,4-Galactosyltransferase. B4GALT4 is highly expressed in the heart, placenta, kidney, and pancreas; it is lowly expressed in the brain, colon, lung, muscle, ovary, testis, and uterus. B4GALT4 function is responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids.

Supplier: ProSci Inc.

GALK2 acts as a galactokinase when galactose is present at high concentrations. GALK2 may be involved in a salvage pathway for the reutilisation of free GalNAc derived from the degradation of complex carbohydrates. GALK2 has been reported to participate in pathways , such as Amino sugar and nucleotide sugar metabolism, Galactose metabolism and Metabolic pathways.