Search results

The three isoenzymes (MM, MB, and BB) are found in muscle, cardiac and brain tissues. These recombinant proteins are ideal for calibrating diagnostic instruments and researching neuromuscular diseases. Creatine Kinases can be used for indications in many neuromuscular applications. These disorders include cardiac disease, mitochondrial disorders, inflammatory myopathies, myasthenia, polymyositis, McArdle''s disease, NMJ disorders, muscular dystrophy, ALS, hypo and hyperthyroid disorders, central core disease, acid maltase deficiency, myoglobinuria, rhabdomyolysis, motor neuron diseases, rheumatic diseases, and other that create elevated or reduced levels of Creatine Kinases.

Creatine Kinase, Mitochondrial 2 (CKMT2) is a member of the ATP:guanido phosphotransferase family. CKMT2 is responsible for the transfer of high energy phosphate from mitochondria to the cytosolic carrier, creatine. CKMT2 reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes have a principal role in energy transduction in tissues with large, variable energy demands, such as skeletal muscle, heart, brain and spermatozoa. Mitochondrial creatine kinase occurs in 2 different oligomeric forms: dimers and octamers, contrary to the exclusively dimeric cytosolic creatine kinase isoenzymes. The CKMT2 gene contains sequences homologous to a number of motifs which are shared among some nuclear genes encoding mitochondrial proteins and therefore may be crucial for the coordinated activation of these genes during mitochondrial biogenesis.

PTEN, a tumor suppressor, has been implicated in a large number of human tumors and is conserved from humans to worms. PTEN has a tensin like domain and a catalytic domain similar to that of the dual specificity protein tyrosine phosphatases. Characterization of PTEN protein showed that it is a phosphatase that acts on proteins and on 3-phosphorylated phosphoinositides, and can therefore modulate signal transduction pathways that involve lipid second messengers. In contrast to most of the protein tyrosine phosphatases, PTEN preferentially dephosphorylates phosphoinositide substrates. PTEN negatively regulates intracellular levels of phosphatidylinositol-3,4,5-trisphosphate in cells and acts as a tumor suppressor by negative regulation of AKT/PKB signaling pathway. Recent results indicate that at least part of its role is to regulate the activity of the serine/threonine kinase AKT/PKB, and thus influence cell survival signaling.

ECHS1 is part of the hydratase/isomerase superfamily. ECHS1 is localized in the mitochondrial matrix and Expressed in muscle, liver and fibroblasts, with low expression in kidney and spleen, ECHS1 exists as a homohexamer that takes part in the second phase of the mitochondrial fatty acid β-oxidation pathway.

Glutathione reductase (Gor) is a member of the class-I pyridine nucleotide disulfide oxidoreductase family. The main role of the Gor protein is to uphold high levels of reduced glutathione in the cytosol. With the associated oxidation of NADPH, Gor transforms oxidized glutathione to the reduced form. The active site of the Gor protein is a redox-active disulfide bond.

Arylsulfatase A (ARSA) hydrolyzes cerebrosidesulfate to cerebroside and sulfate. ARSA is inhibited by phosphate. The phosphate develops a covalent bond with the active site 3-oxoalanine. ARSA gene defects cause metachromatic leucodystrophy (MLD), a progressive demyelination disease which results in various neurological symptoms and ultimately death.

Malate dehydrogenase (EC1.1.1.37) is an enzyme in the citric acid cycle that catalyzes the conversion of malate into oxaloacetate (using NAD+) and vice versa (this is a reversible reaction). Malate dehydrogenase is not to be confused with malic enzyme, which catalyzes the conversion of pyruvate using NADPH.
Malate dehydrogenase is also involved in gluconeogenesis, the synthesis of glucose from smaller molecules. Pyruvate in the mitochondria is acted upon by pyruvate carboxylase to form oxaloacetate, a citric acid cycle intermediate. In order to get the oxaloacetate out of the mitochondria, malate dehydrogenase reduces it to malate, and it then traverses the inner mitochondrial membrane. Once in the cytosol, the malate is oxidized back to oxaloacetate by cytosolic malate dehydrogenase. Finally, phosphoenol-pyruvate carboxy kinase (PEPCK) converts oxaloacetate to phosphoenol pyruvate.

Tyrosylprotein Sulfotransferase 1, also known as TPST1 is the enzyme which catalyzes the sulfation reaction of protein tyrosines, a post-translational modification of proteins. TPST1 belongs to the protein sulfotransferase family. In addition, TPST1 utilizes 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) as the sulfonate donor and also binds proteins with target tyrosineresidues to eventually form the tyrosine O-sulfate ester group in addition to the desulfonated 3’-phosphoadenosine-5’-phosphate.

Enteropeptidase or enterokinase is an enzymeinvolved in human digestion. It is produced by cells in the duodenum wall, and is secreted from duodenum's glands, the crypts of Lieberk?hn, whenever ingested food enters the duodenum from the stomach. Enteropeptidase has the critical job of turning trypsinogen(a zymogen) to trypsin, indirectly activating a number of pancreaticdigestive enzymes.
Enteropeptidase is a serine proteaseenzyme(EC3.4.21.9). Enteropeptidase is a part of the Chymotrypsin-clan of serine proteases, and is structurally similar to these proteins.

ALDH2 is part of the aldehyde dehydrogenase family of proteins which catalyze the chemical transformation from acetaldehyde to acetic acid. ALDH2 is the second enzyme of the major oxidative pathway of alcohol metabolism. ALDH2 has 2 major liver isoforms: cytosolic and mitochondrial, which differ by their electrophoretic mobilities, kinetic properties, and subcellular localizations. Nearly all Caucasians have 2 major isozymes, whereas roughly 50% of Orientals have only the cytosolic isozyme, omitting the mitochondrial isozyme. The extremely higher rate of acute alcohol intoxication with Orientals compared to Caucasians is due to the fact of the absence of mitochondrial isozyme. ALDH2 has a low Km for acetaldehydes, and is localized in mitochondrial matrix.

Thioredoxin reductase (TrxR/NTR), an enzyme belonging to the flavoprotein family of pyridine nucleotide-disulfide oxidoreductases. Thioredoxin reductase (TrxR), a component of the thioredoxin system, including thioredoxin (Trx) and NADPH, catalyzes the transfer of electrons from NADPH to Trx, acts as a reductant of disulfide-containing proteins and participates in the defense system against oxidative stresses.

Glucokinase also known as GLK is a member of the bacterial glucokinase family. GLK is not highly significant in E.coli since glucoseis already transported into the cell through the PTS system as glucose 6-phosphate.

Ribonuclease 7 (RNASE7) is one of the final RNase A superfamily ribonucleases. RNASE7 was isolated from skin-derived stratum corneum. RNASE7 protein demonstrated potent ribonuclease activity and hence may contribute to the well-known ribonuclease activity of human skin. RNASE7 has revealed a broad spectrum antimicrobial activity against many pathogenic microorganisms and extraordinarily potent activity.

Carbonic anhydrase 1 is a zinc metalloenzyme that catalyses reversible hydration of CO2 (CO2 + H2O ? HCO3- + H+). Carbonic anhydrase 1 is essential to many biological processes such as cellular respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, salvia, and gastric acid. Carbonic anhydrase 1 is abundant in erythrocytes and an early marker for erythroid differentiation.

SORD enzyme is part of of the zinc-containing alcohol dehydrogenase family that is broadly expressed in kidney and in the lens eye. SORD enzymatically catalyzes the zinc-dependent interconversion of polyols, such as sorbitol and xylitol, to their respective ketoses.

Biotinidase also known BTD, belongs to the nitrilase superfamily, which contains 12 families of nitrilases, amidases, carbamylases, and N-acyltrasferases. BTD catalyzes the hydrolysis of biocytin, the product of biotin-dependent carboxylase degradation, to biotin and lysine. BTD has a vital regulatory part in chromatin/DNA function. Mutations in BTD protein lead to Biotinidase deficiency.

Deoxyribonuclease I Bovine (bDNase), an enzyme which selectively cleaves DNA. Bovine Dnase is an endonuclease enzyme which splits phosphodiester linkages within polynucleotides, acting primarely on single stranded DNA (ssDNA), double stranded DNA (ddDNA) and chromatin. Dnase is activated by bivalent metals such as Mg+2 and Ca+2 .
Dnase enzymes are common reagents used in biochemical methods requiring diestion of DNA and recovery of RNA, or where DNA is to be removed without affecting structural proteins or enzymes. Dnase enzymes are also used in tissue culture to digest DNA from damaged cells, resulting in reduced viscosity, and for removal of membrane-bound DNA fragments.

Beta-lactamase is a type of enzyme (EC 3.5.2.6) produced by some bacteria that is responsible for their resistance to beta-lactam antibiotics like penicillins, cephalosporins, cephamycins and carbapenems. These antibiotics have a common element in their molecular structure: a four-atom ring known as a beta-lactam. The lactamase enzyme breaks that ring open, deactivating the molecule's antibacterial properties.

Carboxyl ester lipase also known as CEL, formely called cholesterol esterase or bile salt-stimulated lipase, is an enzyme with lipolytic capablity of hydrolyzing cholesteryl esters, tri-, di-, and mono- phospholipids, acylglycerol, ceramide and lysophospholipids. The carboxyl terminus of the enzyme controls enzymatic activity by creating hydrogen bonds with the surface loop to partlyshield the active site. The active catalytic site triad of serine-histidine-aspartate is centrally located in the enzyme structure and is partly covered by a surface loop. Bile salt binding to the loop domain set free the active site for accessibility by water-insoluble substrates. CEL is produced mainly in the pancreas and lactating mammary gland, thus the protein is also expressed in liver, macrophages, and in the vessel wall.

RNASE2, also known as EDN, is best-known as one of the 4 major proteins found in the large specific granules of human eosinophilic leukocytes. This protein is also expressed constitutively in human liver tissue and its expression can be induced in macrophages by proinflammatory stimuli. RNASE2 is a non-secretory ribonuclease which belongs to the pancreatic ribonuclease family, a subset of the ribonuclease A superfamily. Diseases associated with EDN include Dermatitis, Atopic, 8 and Pulmonary Eosinophilia.

Kell blood group glycoprotein homolog or KEL, is an enzyme, part of the zinc endopeptidase of the neprilysin (NEP) group of proteins. KEL has a crucial part in the production of the potent bioactive ET-3, which also includes enzymes that are endothelin convertingenzymes (PEX, XCE, DINE &various NEP-like proteins). KEL uses a single disulfide bond to XK, a gated membranal transporter. The Kell antigen system that includes two proteins, is very crucial among blood group systems.

Polymerase II Polypeptide I (POLR2I) is a member of the archaeal RpoM/eukaryotic RPA12/RPB9/RPC11 RNA polymerase family. POLR2I is a subunit of RNA polymerase II, which is a polymerase responsible for synthesizing messenger RNA in eukaryotes. DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the 4 ribonucleoside triphosphates as substrates. In addition POLR2I synthesizes mRNA precursors and numerous functional non-coding RNAs.