You searched for: Enzymes

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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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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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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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Nicotinate-Nucleotide Pyrophosphorylase (QPRT) belongs to the nadC/modD family. QPRT plays an improtant role in catabolism of quinolinate which acts as a potent endogenous exitotoxin to neurons. In addition, QPRT serves as an an intermediate in the Tryptophan-Nicotinamide Adenine Dinucleotide pathway. QPRT participates in some pathways including Cofactor biosynthesis, NAD(+) biosynthesis and the Nicotinate D-Ribonucleotide from Quinolinate. In addition, QPRT is involved in the catabolism of Quinolinic Acid (QA). The activity toward QA is slightly repressed by phosphoribosylpyrophosphate (PRPP) in both a competitive and a non-competitive manner.

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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 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.

Supplier: Thermo Fisher Scientific

Elastase substrate V

Supplier: Thermo Fisher Scientific

Neuraminidase

Supplier: ProSci Inc.

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.

Supplier: Thermo Fisher Scientific

Cellulase

Supplier: Merck Millipore (Novagen)

Convenient solution for selective degradation of RNA.

Supplier: Merck Millipore (Calbiochem‎)

Bovine thrombin (from plasma)

Supplier: Merck Millipore (Calbiochem‎)

Bovine thrombin (from plasma)

Supplier: Corning

Trypsin is used to enzymatically release adherent cells from tissue culture plates for passaging

Supplier: Thermo Fisher Scientific

Glucose-6-phosphate dehydrogenase (from Yeast)

Supplier: Merck Millipore (Calbiochem‎)

Recombinant, human Wee1 fused at the N-terminus to a GST-His6-thrombin cleavage site sequence and expressed in S. frugiperda insect cells using a baculovirus expression system.

Supplier: Merck Millipore (Novagen)

Benzonase® nuclease degrades all forms of DNA and RNA while having no proteolytic activity. Benzonase® is compatible with BugBuster® and PopCulture® protein extraction reagents and therefore can be added to these reagents to eliminate viscosity and remove nucleic acids from E. coli extracts.

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Beta-1,4-galactosyltransferase 3 (B4GALT3) belongs to the glycosyltransferase 7 family. It is responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. It is highest expression in placenta, prostate, testis, ovary, intestine and muscle, and in fetal brain.

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Human Esterase D is a serine hydrolase that is involved in the detoxification of formaldehyde. Esterase D plays a part in a variety of substrates, including O-acetylated sialic acids, which may involves in the recycling of sialic acids. Esterase D can be used as a genetic marker for retinoblastoma and Wilson’s disease.

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PEPD belongs to the peptidase M24B family of Eukaryotic-type prolidase subfamily. PEPD is a cytosolic dipeptidase that hydrolyses dipeptides with proline or hydroxyproline at the carboxy terminus. It is important in collagen metabolism because of the high levels of imino acids. Defects in PEPD are a cause of prolidase deficiency which is an autosomal recessive disorder associated with iminodipeptiduria.

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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.

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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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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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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.

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Carboxypeptidase Q (Cpq) is a member of the peptidase M28 family. PGCP is involved in a number of fundamental biological processes such as the hydrolysis of circulating peptides, catalyzing the hydrolysis of dipeptides with unsubstituted terminals into amino acids. Carboxypeptidase may play an important role in the liberation of thyroxine hormone from its thyroglobulin (Tg) precursor. The monomeric form is inactive while the homodimer is active.

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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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Protein Disulfide-Isomerase A4 (PDIA4) is an endoplasmic reticulum luminal protein that belongs to the protein disulfide isomerase family. Human PDIA4 is synthesised as a 625 amino acid precursor that contains a 20 amino acid signal sequence, and a 625 amino acid mature chain, including three thioredoxin domains. PDIA4 catalyses the rearrangement of -S-S- bonds in proteins and is thought to be a deoxycytidine kinase. In addition, PDIA4 serves as a proteases protein disulfide isomerase, phospholipase or an arrangement of these.

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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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Glutamine Synthetase reglutes intracellular concentration of glutamate. Glutamine Synthetase catalyses the synthesis of glutamine from glutamate and ammonia. Glutamine is an important source of energy and that takes part in cell prolifetation, inhibition of apoptosis, and cell signaling. Glutamine Synthetase is expressed during early fetal stages, and has a role in maintaining body PH by removing ammonia from circulation. Mutations in the GLUL gene are related to congenital glutamine deficiency.

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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.