You searched for: Enzymes

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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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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.

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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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Selenophosphate synthetase 1 (SEPHS1) belongs to the selenophosphate synthase 1 family, Class II subfamily. It has four different isoforms by alternative splicing. Isoform 1 and isoform 2 are gradually expressed during the cell cycle until G2/M phase and then decreased, which Isoform 3 is gradually expressed during the cell cycle until S phase and then decreased. SEPHS1 can be activated by phosphate ions and by potassium ions. It can synthesise synthesises selenophosphate from selenide and ATP. Selenophosphate is the selenium donor used to synthesise selenocysteine, which is co-translationally incorporated into selenoproteins at in-frame UGA codons.

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Peptidyl-Prolyl Cis-Trans Isomerase-Like 1 (PPIase) belongs to the cyclophilin-type PPIase family. PPIases can accelerate the folding of proteins and catalyze the cis-trans isomerisaion of proline imidic peptide bonds in oligopeptides. PPIase is a ubiquitous protein and has highly expression in heart ,skeletal and muscle. PPIase contains a PPIase cyclophilin-type domain and four Cyclosporin A binding regions. PPIase might play an important role in proliferation of cancer cells through modulation of phosphorylation of stathmin. It is suggested that PPIase can act as as a novel molecular target for colon-cancer therapy.

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Polypeptide N-acetylgalactosaminyltransferase 3(GALNT3) belongs to the glycosyltransferase 2 family and galNAc-T subfamily. It expressed in organs that contain secretory epithelial glands and it highly expressed in pancreas, skin, kidney and testis. There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding .This protein plays a major role in regulating phosphate levels within the body (phosphate homeostasis). Among its many functions, phosphate plays a critical role in the formation and growth of bones in childhood and helps maintain bone strength in adults.

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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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Acid sphingomyelinase-like phosphodiesterase 3a (SMPDL3A ) is a novel liver X receptor (LXR) -regulated gene, with an LXR response element within its promoter. The induction of SMPDL3A is LXR-dependent and is restricted to human blood cells with no induction observed in mouse cellular systems. LXR function as physiological sensors of cholesterol metabolites (oxysterols), regulating key genes involved in cholesterol and lipid metabolism. LXRs have been extensively studied in both human and rodent cell systems, revealing their potential therapeutic value in the contexts of atherosclerosis and inflammatory diseases.

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Carbonic Anhydrase 14 (CA14) belongs to the Alpha-Carbonic Anhydrase family. It is highly expressed in all parts of the central nervous system and lowly expressed in adult liver, heart, small intestine, colon, kidney, urinary bladder, and skeletal muscle. CA14 along with other Carbonic Anhydrases (CAs) participate in a variety of biological processes, including respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, saliva, and gastric acid. CA14 is predicted to be a type I membrane protein and catalyses the reversible hydration of carbon dioxide.

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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. NAD kinase from Bacillus subtilis 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. Catalytic activity: ATP + NAD+ = ADP + NADP+.

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Sorbitol dehydrogenase, also known as L-iditol 2-dehydrogenase and SORD, is a member of the zinc-containing alcohol dehydrogenase family. SORD exsits in a homotetramer and binds one zinc ion per subunit. SORD is expressed in kidney and epithelial cells of both benign and malignant prostate tissue. SORD can converts sorbitol to fructose and catalyses the interconversion of polyols and their corresponding ketoses, and together with aldose reductase to make up the sorbitol pathway. SORD is up-regulated by androgens and down-regulated by castration. SORD may play a role in the sperm motility by providing an energetic source for sperm.

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Sentrin-Specific Protease 7 (SENP7) acts as a SUMO-2/3-specific protease. SENP7 is likely to regulate the metabolism of poly-SUMO-2/3 rather than SUMO-1 conjugation in vivo. SENP7 has a restricted substrate specificity, and displaying paralogue-specific isopeptidase activity. The C-terminal catalytic domain of SENP7 depolymerised poly-SUMO-2 chains but does not have activity against poly-SUMO-1 chains. SENP7 also had isopeptidase activity against di-SUMO-2- and SUMO-2-modified RanGAP1 (Ran GTPase-activating protein 1) but had limited activity against SUMO-1-modified RanGAP1.

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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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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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Flap Endonuclease 1 (FEN1) is a member of the XPG/RAD2 endonuclease family. During DNA replication, FEN1 cleaves the 5'-overhanging flap structure and processes the 5' ends of Okazaki fragments for synthesis. FEN1 also exhibits RNase H activity by possessing 5'-3' exonuclease activity on gapped double-stranded or nicked DNA, FEN1 is involved in the long patch base excision repair (LP-BER) pathway, it can cleave within the apurinic/apyrimidinic (AP) site-terminated flap. FEN1 can prevent flaps from equilibrating into structures that lead to duplications and deletions. FEN1 is also involved in replication and repair of rDNA and in repairing mitochondrial DNA.

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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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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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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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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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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.

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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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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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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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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.