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ACYP1, also known as Acylphosphatase-1, Acylphosphatase, erythrocyte isozyme, Acylphosphatase, organ-common type isozyme, Acylphosphate phosphohydrolase 1 and ACYPE, is a small cytosolic enzyme which catalyses the hydrolysis of the carboxyl-phosphate bond of acylphosphates. ACYP1 is a protein which belongs to the acylphosphatase family and contains 1 fibrinogen C-terminal domain. Two isoenzymes have been isolated, called muscle acylphosphatase and erythrocyte acylphosphatase, on the basis of their tissue localisation. This gene encodes the erythrocyte acylphosphatase isoenzyme. Alternatively spliced transcript variants that encode different proteins were identified through data analysis. Recombinant human ACYP1 protein was expressed in E. coli fused with HIS-tag at N-terminus.

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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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Cystathionine Gamma-Lyase (CTH) belongs to the trans-sulfuration enzymes family. CTH exists as a homotetramer and interacts with CALM in a calcium-dependent manner. CTH breaks down cystathionine into cysteine, ammonia and 2-oxobutanoate. CTH catalyses the last step in the trans-sulfuration pathway from methionine to cysteine and has broad substrate specificity. Defects in CTH will lead to cystathioninuria, which is an autosomal recessive phenotype characterised by abnormal accumulation of plasma cystathionine.

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Hydroxyacid Oxidase 1 (HAO1) is an enzyme that belongs to the FMN-Dependent alpha-Hydroxy Acid Dehydrogenase family. HAO1 contains 1 FMN Hydroxy Ccid Dehydrogenase domain. HAO1 is expressed primarily in the liver and pancreas. This protein has 2-Hydroxyacid Oxidase activity. Most HAO1 is active on the 2-Carbon substrate Glycolate, but it can also be active on 2-Hydroxy fatty acids, with higher activity towards 2-Hydroxy Palmitate and 2-Hydroxy Octanoate.

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Tryptophan synthase is an enzyme that catalyses the final two steps in the biosynthesis of tryptophan. It is commonly found in Eubacteria, Archaebacteria, Protista, Fungi, and Plantae, but is absent from animals such as humans. Tryptophan synthase typically exists as an alpha- beta beta - alpha complex.The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate: L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H₂O.The beta subunits catalyse the irreversible condensation of indole and serine to form tryptophan in a pyridoxal phosphate (PLP) dependent reaction. Their assembly into a complex leads to structural changes in both subunits resulting in reciprocal activation.

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Tryptophan synthase is an enzyme that catalyses the final two steps in the biosynthesis of tryptophan. It is commonly found in Eubacteria, Archaebacteria, Protista, Fungi, and Plantae, but is absent from animals such as humans. Tryptophan synthase typically exists as an alpha- beta beta - alpha complex.The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate: L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H₂O.The beta subunits catalyse the irreversible condensation of indole and serine to form tryptophan in a pyridoxal phosphate (PLP) dependent reaction. Their assembly into a complex leads to structural changes in both subunits resulting in reciprocal activation.

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Mouse cytosolic non-specific dipeptidase(CNDP2) is a cytoplasm protein which belongs to the peptidase M20A family. CNDP2 has 2 Isoform: Isoform 1 is ubiquitously expressed with higher levels in kidney and liver (at protein level). Isoform 2 is expressed in fetal tissues, it is only expressed in adult liver and placental tissues. CNDP2 hydrolyses a variety of dipeptides including L-carnosine and has a strong preference for Cys-Gly. It is a cytosolic enzyme that can hydrolyse carnosine to yield l-histidine and beta-alanine. CNDP2 is highly expressed in the histaminergic neurons in the tuberomammillary nucleus, implying that it may supply histidine to histaminergic neurons for histamine synthesis. It may play a role as tumour suppressor in hepatocellular carcinoma (HCC) cells.

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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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Mouse CD73 is a glycosyl phosphatidylinositol (GPI) anchored membrane protein that belongs to the 5'-nucleotidase family. CD73 is an ecto 5'Nucleotidase expressed by most cell types. CD73 hydrolyses extracellular nucleotides into membrane permeable nucleosides. CD73 is one of several enzymes responsible for the production of extracellular adenosine, a signalling molecule that is involved in responses to inflammation and tissue injury. CD73 is a lymphocyte maturation marker that has functions independent of its catalytic activity. CD73 is also a regulator of leukocyte extravasation, a function that requires its 5'Nucleotidase activity.CD73 has also been reported to regulate expression of pro-inflammatory molecules in mouse endothelium.

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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.

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X-Prolyl Aminopeptidase (XPNPEP1) is a proline-specific metalloaminopeptidase that specifically catalyses the removal of any unsubstituted N-terminal amino acid that is adjacent to a penultimate proline residue. Because of its specificity toward proline, it has been suggested that X-Prolyl Aminopeptidase is important in the maturation and degradation of peptide hormones, neuropeptides, and tachykinins, as well as in the digestion of otherwise resistant dietary protein fragments, thereby complementing the pancreatic peptidases. X-Prolyl Aminopeptidase is a member of the M24 family of metalloproteases, which also contains methionine aminopeptidases, X-Pro dipeptidase, aminopeptidase P2, aminopeptidase P homolog, proliferation-associated protein 1, and suppressor of Ty homolog or chromatin-specific transcription elongation factor large subunit. It is a soluble enzyme, in contrast to the GPI-anchored Aminopeptidase P2 encoded by XPNPEP2. Deficiency of X-Prolyl Aminopeptidase results in excretion of large amounts of imino-oligopeptides in urine. Human Aminopeptidase P1 is widely expressed. The amino acid sequence of human X-Prolyl Aminopeptidase is 99%, 97%, 95%, 74% and 73% identical to that of canine, bovine, mouse/rat, Xenopus and zebrafish, respectively.

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Transaldolase (TALDO1) belongs to the transaldolase family of Type 1 subfamily. TALDO1 is expressed selectively in oligodendrocytes of the brain. TALDO1 is a key enzyme of the nonoxidative pentose phosphate pathway providing ribose-5-phosphate for nucleic acid synthesis and NADPH for lipid biosynthesis. This pathway can also maintain glutathione at a reduced state and thus protect sulfhydryl groups and cellular integrity from oxygen radicals. TALDO1 deficiency results in telangiectases of the skin, hepatosplenomegaly and enlarged clitoris.

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L-Xylulose Reductase is an enzyme that belongs to the Short-Chain Dehydrogenases/Reductases (SDR) family. L-Xylulose Reductase is responsible for the metabolism of Xylulose, converting it into Xylitol. L-Xylulose Reductase catalyses the NADPH-dependent reduction of several Pentoses, Tetroses, Trioses, alpha-Dicarbonyl compounds and L-Xylulose. L-Xylulose Reductase participates in the Uronate Cycle of Glucose metabolism. It may play a role in the water absorption and cellular osmoregulation in the proximal renal tubules by producing Xylitol, an osmolyte, thereby preventing osmolytic stress from occurring in the renal tubules.

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Chymotrypsin-Like Elastase Family Member 3A (CELA3A) is an enzyme that contains one peptidase S1 domain. ELA3A belongs to the peptidase S1 family of the Elastase subfamily. ELA3A is secreted from the pancreas as a zymogen and, like other serine proteases such as trypsin, chymotrypsin and kallikrein, it has a digestive function in the intestine. ELA3A may also function in the intestinal transport and metabolism of cholesterol. ELA3A is efficient protease with alanine specificity but only little elastolytic activity. ELA3A preferentially cleaves proteins after alanine residues.

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Proteinase K

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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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Tritirachium album proteinase K

Supplier: Thermo Fisher Scientific

Neuraminidase (from Clostridium perfringens)

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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: Merck Millipore (Calbiochem‎)

Native lipase from Chromobacterium viscosum. Catalyses hydrolysis of triglycerides to glycerol and fatty acids.

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rLysozyme™ solution contains a highly purified and stabilised recombinant lysozyme that can be used for lysis of gram negative bacteria, such as E. coli.

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Protein disulfide-isomerase A5 is a 519 amino acids protein that belongs to the protein disulfide isomerase family.It contains 3 thioredoxin domains.It can catalyse the rearrangement of -S-S- bonds in proteins.

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Human Sulfotransferase (SULT1C4) is an enzyme that in humans is encoded by the SULT1C4 gene, belongs to the sulfotransferase 1 family. SULT1C4 is expressed at high levels in fetal lung and kidney and at low levels in fetal heart, adult kidney, ovary and spinal chord. Sulfotransferase utilises 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyse the sulfate conjugation of drugs, xenobiotic compounds, hormones, and neurotransmitters. It shows activity towards p-nitrophenol and N-hydroxy-2-acetylamino-fluorene (N-OH-2AAF). SULT1C4 plays an important role incatalyzing the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds.

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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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Nicotinate Phosphoribosyltransferase (NAPRTase) is involved in the biological processes of pyridine nucleotide biosynthesis and nicotinate nucleotide salvage and functions by catalyzing the conversion of nicotinic acid (NA) to NA mononucleotide (NaMN). 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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Sulfotransferase 4A1 (ST4A1) is a member of the Sulfotransferase 1 family. ST4A1 is highly expressed in the cerebral cortex and frontal lobe, but no expression is detected in the pancreas. ST4A1 is a brain-specific sulfotransferase believed to be involved in the metabolism of neurotransmitters. ST4A1 acts on catecholamines and T4 in a manner that may not involve sulfonation. ST4A1 may have a role in the metabolism of drugs and neurotransmitters in the CNS. In addition, ST4A1 is related to schizophrenia.

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Fumarylacetoacetase belongs to the FAH family. Fumarylacetoacetase is primary expressed in liver and kidney. It exists as a homodimer and catalyses the hydrolysis of 4-fumarylacetoacetate into fumarate and acetoacetate. Defects in Fumarylacetoacetase cause tyrosinemia type 1, which is congenital metabolism defect characterised by elevated levels of tyrosine in the blood and urine, and hepatorenal manifestations. Typical features include renal tubular injury, self-mutilation, hepatic necrosis, episodic weakness, and seizures.

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Carboxypeptidase M (CPM) belongs to the peptidase M14 family, and exists in cell membrane. The protein binds 1 zinc ion per subunit, and cleavage of C-terminal arginine or lysine residues from polypeptides. CPM specifically removes C-terminal basic residues (Arg or Lys) from peptides and proteins. It is believed to play important roles in the control of peptide hormone and growth factor activity at the cell surface, and in the membrane-localised degradation of extracellular proteins.

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LTA4H, which is short for Leukotriene A-4 hydrolase, is a 611 aa. protein. It belongs to the peptidase M1 family, and exists in cytoplasm. This protein has at least 4 isforms produced by alternative splicing, and two of them are expressed in monocytes, lymphocytes, neutrophils, reticulocytes, platelets and fibroblasts. LTA4H involves in lipid metabolism and leukotriene B4 biosynthesis. It is a epoxide hydrolase that catalyses the final step in the biosynthesis of the proinflammatory mediator leukotriene B4. It also has aminopeptidase activity.