You searched for: Enzymes

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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 nicotinate phosphoribosyltransferase (NAPRTase) is localised in the cytoplasm and is involved in biological processes such as NAD biosynthetic and metabolic processes, nicotinamide metabolic process, nicotinate nucleotide salvage, response to oxidative stress and water-soluble vitamin metabolic process. It functions by catalyzing the conversion of nicotinic acid (NA) to NA mononucleotide (NaMN) and is essential for NA to increase cellular NAD levels and prevent oxidative stress of the cells. 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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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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Carbonic Anhydrase 5B (CA5B) is a member of alpha-carbonic anhydrase family (CAs) that catalyze the reversible hydration of carbon dioxide. CAs is associated with many biological processes, including calcification, respiration, bone resorption, acid-base balance and the formation of aqueous humor. CA5B is highly expressed in heart, pancreas, kidney, placenta, lung, and skeletal muscle, but it is restricted to the liver. CA5B is localised in the mitochondria and shows the highest sequence similarity to the other mitochondrial CA, CA-VA. CA5B is inhibited by coumarins, sulfonamide derivatives such as acetazolamide (AZA), saccharin, and Foscarnet.

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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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Native thrombin from human plasma, bound to agarose beads.

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Endoplasmic Reticulum Mannosyl-Oligosaccharide 1,2- alpha-Mannosidase (MAN1B1) belongs to the glycosyl hydrolase 47 family. MAB1B1 is a single-pass type II membrane protein and widely expressed in many tissues. MAB1B1 is involved in glycoprotein quality control targeting of misfolded glycoproteins for degradation. MAB1B1 can be inhibited by both 1-deoxymannojirimycin (dMNJ) and kifunensine. Defects in MAN1B1 are the cause of mental retardation autosomal recessive type 15 (MRT15). Mental retardation is characterised by significantly below average general intellectual functioning, it is also associated with impairments in adaptative behavior and manifested during the developmental period.

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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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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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Native thrombin from human plasma. Formulation useful for procedures in which the presence of citrate is undesirable.

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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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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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Restriction grade thrombin is a highly purified preparation qualified to specifically cleave target proteins produced with appropriate vectors. This preparation is functionally tested for activity with fusion proteins and is free of detectable contaminating proteases.

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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.

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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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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.

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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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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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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.

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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.

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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.

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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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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.

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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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Inositol Monophosphatase 1 (IMPA1) belongs to the inositol monophosphatase family. IMPA1 is responsible for the provision of inositol required for synthesis of phosphatidylinositol and polyphosphoinositides, IMPA1 can use myo-inositol-1,3-diphosphate, myo-inositol-1,4-diphosphate, scyllo-inositol-phosphate, glucose-1-phosphate, glucose-6-phosphate, fructose-1-phosphate, beta-glycerophosphate, and 2-AMP as substrates. IMPA1 has been implicated as the pharmacological target for lithium action in brain. IMPA1 shows magnesium-dependent phosphatase activity and is inhibited by therapeutic concentrations of lithium. In addition, IMPA1 plays a improtant role in intracellular signal transduction.

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Proteinase K (also protease K, endopeptidase K, peptidase K or Tritirachium alkaline phosphatase) (EC 3.4.21.64) is a non specifc, broad spectrum serine protease that is isolated from the saprophytic fungus Tritirachium album.

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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.