Supplier: Thermo Fisher Scientific

Elastase substrate V

Supplier: ProSci Inc.

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.

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Carbonic Anhydrase 1 (CA1) is a cytosolic enzyme, belonging to the alpha-carbonic anhydrase family. It is highly expressed in erythrocytes and acts as an early marker for erythroid differentiation. Carbonic anhydrase 1 plays a improtant role in many biological processes such as calcification, cellular respiration, bone resorption, acid-base balance. It is activated by imidazole, histamine, L-adrenaline, L- and D-histidine, and L- and D-phenylalanine. At the same time, It is inhibited by sulfonamide derivatives and coumarins. In addition, CA1 is a zinc metalloenzyme that has reversible hydration of carbon dioxide. It can hydrate cyanamide to urea.

Supplier: Corning

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

Supplier: Thermo Fisher Scientific

Neuraminidase (from Clostridium perfringens)

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NadN (NAD nucleotidase) is a periplasmic enzyme from Haemophilus influenzae, a major pathogen of the respiratory tract in humans that has developed the capability to exploit host NAD(P) for its nicotinamide dinucleotide requirement. NadN plays a central role by degrading NAD into adenosine and NR (nicotinamide riboside), NMN to nicotinamide riboside and AMP to adenosine. It shows a broad substrate specificity, recognising either mono- or di-nucleotide nicotinamides and different adenosine phosphates with a maximal activity on 5'-adenosine monophosphate. It can be used as an economically alternative to produce NR (nicotinamide riboside). Catalytic activity: NAD=AMP + NMN=Ade+NR+PPi | AMP=Ade+Pi | NMN=NR+Pi.

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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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beta Galactosidase is a lysosomal beta Galactosidase that hydrolyses the terminal beta Galactose from Ganglioside and Keratan sulfate. In lysosome, the mature beta Galactosidase protein associates with Cathepsin A and Neuraminidase 1 to form the lysosomal multienzyme complex . An alternative splicing at the RNA level of beta Galactosidase results a catalytically inactive beta Galactosidase that plays an important role in vascular development. Defects of beta -galactosidase (GLB1) are the cause of diseases like GM1-gangliosidosis which is a lysosomal storage disease and Morquio Syndrome B that cause patients to have abnormal elastic fibers. More than 100 mutations have been identified for beta Galactosidase, which result in different residual activities of the mutant enzymes and a spectrum of symptoms in the two related diseases.

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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.

Supplier: ProSci Inc.

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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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).

Supplier: ProSci Inc.

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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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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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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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.