You searched for: Enzymes

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Peptidyl-Prolyl Cis-Trans Isomerase H (PPIH) belongs to the Cyclophilin-type PPIase family that accelerate the folding of proteins. PPIases can catalyze the cis-trans isomerisaion of Proline Imidic peptide bonds in oligopeptides. PPIH participates in pre-mRNA splicing. It is a specific component of the complex that includes pre-mRNA processing factors PRPF3, PRPF4, and PRPF18, as well as U4/U5/U6 tri-snRNP. In addition, PPIH has PPIase activity and may play a role as a chaperone mediating the interactions between different proteins inside the spliceosome.

Supplier: Thermo Fisher Scientific

Thermo Scientific dsDNase is an engineered shrimp DNase designed for rapid and safe removal of contaminating genomic DNA from RNA samples. It is an endonuclease that cleaves phosphodiester bonds in DNA to yield oligonucleotides with 5’-phosphate and 3’-hydroxyl termini. Highly specific activity towards double-stranded DNA ensures that RNA and single-stranded DNA, such as cDNA and primers are not cleaved. dsDNase is easily inactivated by moderate heat treatment (55 °C). These features make dsDNase an excellent choice for gDNA elimination prior reverse transcription. It allows for dramatically simplified workflow which combines genomic DNA elimination and cDNA synthesis into one-tube procedure.

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Carbonic Anhydrase 4 (CA4) 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. Carbonic anhydrase 4 is a glycosylphosphatidyl-inositol-anchored membrane isozyme expressed on the luminal surfaces of pulmonary (and certain other) capillaries and proximal renal tubules. Carbonic anhydrase 4 may stimulate the sodium/bicarbonate transporter activity of SLC4A4 that acts in pH homeostasis. It may have a role in inherited renal abnormalities of bicarbonate transport. Furthermore, Carbonic anhydrase 4 is essential for acid overload removal from the retina and retina epithelium and acid release in the choriocapillaris.

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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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PDIA3 protein is also known as Protein disulfide-isomerase A3. It is a protein that in humans is encoded by the PDIA3 gene.PDIA3 is an enzyme that belongs to the endoplasmic reticulum and interacts with lectin chaperones calreticulin and calnexin to modulate folding of newly synthesised glycoproteins. PDIA3 interacts with thiazide-sensitive sodium-chloride cotransporter in the kidney and is induced by glucose deprivation. PDIA3 is part of the major histocompatibility complex (MHC) class I peptide-loading complex (TAP1), which is important for formation of the final antigen conformation and export from the endoplasmic reticulum to the cell surface.

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Carbonic Anhydrase 13 (CA13) belongs to the carbonic anhydrase family which can catalyses the reversible hydration recation of carbon dioxide. Carbonic anhydrases participate in many biological processes, including respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, saliva, and gastric acid. CA13 is a cytosolic enzyme and is widely expressed in human, such as thymus, small intestine, spleen, prostate, ovary, colon and testis, indicating that it may play a key role in several organs. CA13 is inhibited by acetazolamide.

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AKR1C3, is an enzyme which belongs to the aldo/keto reductase family. It is expressed in many tissues including adrenal gland, brain, kidney, liver, lung, mammary gland, placenta, small intestine, colon, spleen, prostate and testis. AKR1C3 catalyses the conversion of aldehydes and ketones to alcohols. It catalyses the reduction of prostaglandin (PG) D2, PGH2 and phenanthrenequinone (PQ) and the oxidation of 9-alpha,11-beta-PGF2 to PGD2,which functions as a bi-directional 3-alpha-, 17-beta- and 20-alpha HSD. It can interconvert active androgens, estrogens and progestins with their cognate inactive metabolites.

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Human Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3 (B3GAT3) is an enzyme that in humans is encoded by the B3GAT3 gene, belongs to the glycosyltransferase 43 family. B3GAT3 is involved in a number of biological processes such as catalyzing the formation of the glycosaminoglycan-protein linkage by way of a glucuronyl transfer reaction in the final step of the biosynthesis of the linkage region of proteoglycans, forming the linkage tetrasaccharide present in heparan sulfate and chondroitin sulfate, gGlycosaminoglycans biosynthesis, transfering a glucuronic acid moiety from the uridine diphosphate-glucuronic acid (UDP-GlcUA) to the common linkage region trisaccharide Gal-beta-1,3-Gal-beta-1,4-Xyl covalently bound to a Ser residue at the glycosaminylglycan attachment site of proteoglycans.It also plays a role in the biosynthesis of l2/HNK-1 carbohydrate epitope on glycoproteins , hows strict specificity for Gal-beta-1,3-Gal-beta-1,4-Xyl, exhibiting negligible incorporation into other galactoside substrates including Galbeta1-3Gal beta1-O-benzyl, Galbeta1-4GlcNAc and Galbeta1-4Glc and stimulates 2-phosphoxylose phosphatase activity of PXYLP1 in presence of uridine diphosphate-glucuronic acid (UDP-GlcUA) during completion of linkage region formation.

Supplier: Thermo Fisher Scientific

Elastase substrate V

Supplier: Corning

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

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Carboxypeptidase B2 (CPB2) is a secreted enzyme that belongs to the peptidase M14 family. CPB2 is synthesised by the liver and circulates in the plasma as a plasminogen-bound zymogen by the liver and circulates in the plasma as a plasminogen-bound zymogen. CPB2 cleaves C-terminal arginine or lysine residues from biologically active peptides, such as kinins or anaphylatoxins, in the circulation regulating their activities. CPB2 also down-regulates fibrinolysis by removing C-terminal lysine residues from fibrin that has already been partially degraded by plasmin. CPB2 exhibits carboxypeptidase activity when it is activated by proteolysis at residue Arg92 of the thrombin/thrombomodulin complex. Activated CPB2 reduces fibrinolysis by removing the fibrin C-terminal residues that are important for the binding and activation of plasminogen.

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Carboxylesterase 1 (CES1) is a member of a large family of carboxylesterases that are responsible for the hydrolysis of ester and amide bonds. These enzymes have broad substrate specificity ranging from small molecule esters such as phenylester to long chain fatty acid esters and thioesters. They are major determinants of the pharmacokinetic behavior of most therapeutic agents containing an ester or amide bond. CES1 shares the serine hydrolase fold observed in other esterases. CES1 hydrolyses aromatic and aliphatic esters, but has no catalytic activity toward amides or a fatty acyl-CoA ester. CES1 participates in detoxification of drugs such as cocaine and heroin in serum and liver. It may also play a role in detoxification in the lung and/or protection of the central nervous system from ester or amide compounds.

Supplier: Thermo Fisher Scientific

Cellulase

Supplier: Thermo Fisher Scientific

Glucose-6-phosphate dehydrogenase (from Yeast)

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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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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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Tripeptidyl-Peptidase 1 (TPP1) belongs to the peptidase S53 family. TPP1 is detected in all tissues examined with highest levels in heart and placenta and relatively similar levels in other tissues. TPP1 is lysosomal serine protease with tripeptidyl-peptidase I activity. TPP1 may act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases. TPP1 requires substrates with an unsubstituted N-terminus. TPP1 mutations have also been shown to cause neuronal ceroid lipofuscinosis type 2 (CLN2).

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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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Chitotriosidase-1 (CHIT1) is a glycoprotein that belongs to the Glycosyl Hydrolase 18 family and Chitinase class II subfamily. It is secreted by cultured macrophages and serves to degrade chitin, chitotriose and chitobiose. CHIT1 may participate in the defense against nematodes and other pathogens. It is highly expressed in the plasma of patients with Gaucher's disease type I, which can be used as diagnostic aid and to evaluate the success of treatment that brings levels back to normal. The amino acid sequence of human CHIT1 is 99%, 76%, 75% and 55% identical to that of chimpansee, rat, mouse and fruit fly, respectively.

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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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Carbonic Anhydrase-Related Protein 11 (CA11) is a secreted protein member of the alpha-carbonic anhydrase family. Carbonic Anhydrases (CAs) are a large family of zinc metalloenzymes that catalyse the reversible hydration of carbon dioxide. They 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. CA11 is expressed abundantly in the brain with moderate expression also present in spinal cord and thyroid. CA11 may play a general role in the central nervous system.

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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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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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Dihydropteridine reductase, also known as HDHPR and Quinoid dihydropteridine reductase, QDPR and DHPR, belongs to the short-chain dehydrogenases/reductases (SDR) family. QDPR exists as a homodimer. QDPR is part of the pathway that recycles a substance called tetrahydrobiopterin, also known as BH4 and tryptophan hydroxylases. The regeneration of this substance is critical for the proper processing of several other amino acids in the body. Tetrahydrobiopterin also helps produce certain chemicals in the brain called neurotransmitters, which transmit signals between nerve cells. Defects in QDPR are the cause of BH4-deficient hyperphenylalaninemia type C (HPABH4C) which is a rare autosomal recessive disorder and is lethal.

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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 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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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.