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| Product | Description | |
|---|---|---|
| Native Human Lactate Dehydrogenase 2 | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Applications: Research clinical chemistry life science. Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: >90%. (>200U/mL). Storage: 4°C. Source: Human Cardiac Tissue. Species: Human. EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Cat No: NATE-0386. |  |
| Native Human Lactate Dehydrogenase 3 | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Applications: Research linical chemistry life science. Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: >90%. (>200U/mL). Storage: 4°C. Source: Human Cardiac Tissue. Species: Human. EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Cat No: NATE-0388. | |
| Native Human Lactate Dehydrogenase 4 | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Applications: Diagnostic controls, calibrators & standards; clinical chemistry; testing/assay validation; life science; validation studies; manufacturing. Group: Enzymes. Synonyms: LDH-4 isoenzyme; 1H3M isoenzyme; ld4 isoenyzme. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: > 35 U/mg protein (> 110 U/mL). Stability: 2 years. Storage: 2-8°C. Form: Liquid; Suspension in 3.1 M ammonium sulfate, 20 mM tris chloride, 1 mM DTT, 1 mM EDTA, pH 7.5. Source: Human Liver. Species: Human. LDH-4 isoenzyme; 1H3M isoenzyme; ld4 isoenyzme; Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Cat No: NATE-0965. | |
| Native Human Lactate Dehydrogenase 5 | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Applications: Research linical chemistry life science. Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: >90%. (>200U/mL). Storage: 4°C. Source: Human Liver. Species: Human. EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Cat No: NATE-0390. | |
| Native Human Lactoperoxidase | Lactoperoxidase catalyzes the oxidation of iodide to iodine by hydrogen peroxide. This activity provides a gentle, specific alternative to chloramine T for the radioiodination of proteins and DNA. Applications: Diagnostic controls, calibrators & standards; testing/assay validation; life science; manufacturing. Group: Enzymes. Synonyms: Salivary peroxidase; SPO; LPO. Enzyme Commission Number: EC 1.11.1.7. CAS No. 9003-99-0. Peroxidase. Source: Human Saliva. Species: Human. Salivary peroxidase; lactoperoxidase; guaiacol peroxidase; plant peroxidase; Japanese radish peroxidase; horseradish peroxidase (HRP); soybean peroxidase (SBP); extensin peroxidase; heme peroxidase; oxyperoxidase; protoheme peroxidase; pyrocatechol peroxidase; scopoletin peroxidase; Coprinus cinereus peroxidase; Arthromyces ramosus peroxidase; EC 1.11.1.7; 9003-99-0; LPO; SPO. Cat No: NATE-0966. | |
| Native Human Leukocyte Esterase, Unsonicated | Leukocyte Esterase is used in a urine test for presence of white blood cells abnormalities associated with infection. Urine tests reveal the presence of granulocyte esterases. The esterases cleave a derivatized pyrazole amino acid ester to liberate derivatized hydroxy pyrazole. This pyrazole then reacts with a diazonium salt to produce a purple color. White blood cells in the urine usually indicate a urinary tract infection. Human leukocytes esterase test detects human esterase, an enzyme released by white blood cells. Human White blood cells are produced in the bone marrow and help to defend the body against infectious disease and foreign materials as part of the immun...ence of white blood cells and other abnormalities associated with infection. Applications: Diagnostic controls, calibrators & standards; immunoassays; clinical chemistry; testing/assay validation; life science; validation studies; characterization; manufacturing; urinalysis. Group: Enzymes. Synonyms: Unsonicated White Blood Cell Esterase; WBC Esterase. LE. Activity: 5.0 - 6.0 U/mL. Stability: 2 years. Appearance: Milky, off-white suspension. Storage: Store at -20°C. Form: Suspension in 154 mM sodium chloride. Source: Human Leukocytes. Species: Human. Unsonicated White Blood Cell Esterase; WBC Esterase; Whole Leukocyte Esterase; Leukocyte Esterase; LE. Cat No: NATE-0967. | |
| Native Human Lipase | Triacylglycerol lipase is an enzyme with system name triacylglycerol acylhydrolase. This enzyme catalyses the following chemical reaction:triacylglycerol + H2O<-> diacylglycerol + a carboxylate. The pancreatic enzyme acts only on an ester-water interface. Pancreatic lipase fulfills a key function in dietary fat absorption by hydrolyzing triglycerides into diglycerides and subsequently into monoglycerides and free fatty acids. buffered aqueous solution, > 250 units/mg protein (lowry). Applications: Lipase has been used in a study to assess the effects of acidification on human milk?s cellular and nutritional content. it has also been used in a study to investigate the effect of physical training on the adipose tissue of diet-induced obesity mice. Group: Enzymes. Synonyms: EC 3.1.1.3; 9001-62-1; Lipase; Triacylglycerol acylhydrolase; Triacylglycerol lipase; butyrinase; tributyrinase; T. Enzyme Commission Number: EC 3.1.1.3. CAS No. 9001-62-1. Lipase. Activity: > 250 units/mg protein (Lowry). Stability: 2-8°C. Form: buffered aqueous solution. Source: Human pancreas. Species: Human. EC 3.1.1.3; 9001-62-1; Lipase; Triacylglycerol acylhydrolase; Triacylglycerol lipase; butyrinase; tributyrinase; Tween hydrolase; steapsin; triacetinase; tributyrin esterase; Tweenase; amno N-AP; Takedo 1969-4-9; Meito MY 30; Tweenesterase; GA 56; capalase L; triglyceride hydrolase; t | |
| Native Human Lysogangliosides | Lyso-gangliosides are prepared by removing glycolipid enzymatically from natural gangliosides. They can be used to analyze various cell function, such as cell proliferation, differentiation, apoptosis, signal transduction, etc. It can also be used as a material of ganglioside derivatives in RI labeling, fluorescence labeling, immobilization since they have free amino group in sphingosine. Group: Enzymes. Synonyms: Lysogangliosides; Lyso-GM2; Lyso-gangliosides. Purity: Greater than 95% by TLC. Lysogangliosides. Storage: -20°C. Form: Lyophilized. Source: Human brain ganglioside GM2. Species: Human. Lysogangliosides; Lyso-GM2; Lyso-gangliosides. Cat No: NATE-0888. | |
| Native Human Lysozyme | Lysozymes, also known as muramidase or N-acetylmuramide glycanhydrolase, are glycoside hydrolases. These are enzymes (EC 3.2.1.17) that damage bacterial cell walls by catalyzing hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins. Lysozyme is abundant in a number of secretions, such as tears, saliva, human milk, and mucus. It is also present in cytoplasmic granules of the macrophages and the polymorphonuclear neutrophils (PMNs). Large amounts of lysozyme can be found in egg white. C-type lysozymes are closely related to alpha-lactalbumin in sequence and structure, making them part of the same family. In humans, the lysozyme enzyme is encoded by the LYZ gene. Group: Enzymes. Synonyms: muramidase; globulin G; mucopeptide gl. Enzyme Commission Number: EC 3.2.1.17. CAS No. 9001-63-2. Purity: > 95% (SDS-PAGE). Lysozyme. Activity: > 100 ,000 units/mg protein (E1%/280). Storage: -20°C. Form: Lyophilized from 50 mM sodium acetate, pH 6.0, with 100 mM NaCl. Source: Human neutrophils. Species: Human. muramidase; globulin G; mucopeptide glucohydrolase; globulin G1; N,O-diacetylmuramidase; lysozyme g; L-7001; 1,4-N-acetylmuramidase; mucopeptide N-acetylmuramoylhydrolase; PR1-lysozyme; lysozyme; LYZ; LZM; EC 3.2.1.17; 9001-63-2. Cat No: NATE-0433. | |
| Native Human Myeloperoxidase | Myeloperoxidase (MPO) is a peroxidase enzyme that in humans is encoded by the MPO gene on chromosome 17. MPO is most abundantly expressed in neutrophil granulocytes (a subtype of white blood cells), and produces hypohalous acids to carry out their antimicrobial activity. It is a lysosomal protein stored in azurophilic granules of the neutrophil and released into the extracellular space during degranulation. MPO has a heme pigment, which causes its green color in secretions rich in neutrophils, such as pus and some forms of mucus. Group: Enzymes. Synonyms: MPO; myeloperoxidase; Peroxidase; myelo; EC 1.11.1.7; 9003-99-0. Enzyme Commission Number: EC 1.11.1.7. CAS No. 9003-99-0. Peroxidase. Activity: > 50 units/mg protein. Storage: -20°C. Form: Lyophilized from 50 mM sodium acetate buffer, pH 6.0, 0.1 M sodium chloride. Source: Human leuk ocytes. Species: Human. MPO; myeloperoxidase; Peroxidase; myelo; EC 1.11.1.7; 9003-99-0. Cat No: NATE-0457. | |
| Native Human Myeloperoxidase A+B | Myeloperoxidase (MPO) is a peroxidase enzyme that in humans is encoded by the MPO gene on chromosome 17. MPO is most abundantly expressed in neutrophil granulocytes (a subtype of white blood cells), and produces hypohalous acids to carry out their antimicrobial activity. It is a lysosomal protein stored in azurophilic granules of the neutrophil and released into the extracellular space during degranulation. MPO has a heme pigment, which causes its green color in secretions rich in neutrophils, such as pus and some forms of mucus. Group: Enzymes. Synonyms: MPOAB; MPOA+B; Myeloperoxidase A+B. Purity: > 98% (SDS-PAGE). Peroxidase. Activity: Typically > 1,000 U/mL. Storage: 2-8°C. Form: Liquid. Source: Human Neutrophils. Species: Human. MPOAB; MPOA+B; Myeloperoxidase A+B. Cat No: NATE-0459. | |
| Native Human Myeloperoxidase Isoform A | Myeloperoxidase (MPO) is a peroxidase enzyme that in humans is encoded by the MPO gene on chromosome 17. MPO is most abundantly expressed in neutrophil granulocytes (a subtype of white blood cells), and produces hypohalous acids to carry out their antimicrobial activity. It is a lysosomal protein stored in azurophilic granules of the neutrophil and released into the extracellular space during degranulation. MPO has a heme pigment, which causes its green color in secretions rich in neutrophils, such as pus and some forms of mucus. Group: Enzymes. Synonyms: MPOA; Myeloperoxidase Isoform A; EC 1.11.1.7; 9003-99-0; MPO A. Enzyme Commission Number: EC 1.11.1.7. CAS No. 9003-99-0. Purity: > 98% (SDS-PAGE). Peroxidase. Mole weight: 151 kDa. Activity: Typically > 1 ,000 U/mL. Storage: 2-8°C. Form: Liquid. Source: Human Neutrophils. Species: Human. MPOA; Myeloperoxidase Isoform A; EC 1.11.1.7; 9003-99-0; MPO A. Cat No: NATE-0458. | |
| Native Human Myeloperoxidase Isoform B | Myeloperoxidase (MPO) is a peroxidase enzyme that in humans is encoded by the MPO gene on chromosome 17. MPO is most abundantly expressed in neutrophil granulocytes (a subtype of white blood cells), and produces hypohalous acids to carry out their antimicrobial activity. It is a lysosomal protein stored in azurophilic granules of the neutrophil and released into the extracellular space during degranulation. MPO has a heme pigment, which causes its green color in secretions rich in neutrophils, such as pus and some forms of mucus. Group: Enzymes. Synonyms: MPOB; MPO B; Myeloperoxidase Isoform B; EC 1.11.1.7; 9003-99-0. Enzyme Commission Number: EC 1.11.1.7. CAS No. 9003-99-0. Purity: > 96% (SDS-PAGE). Peroxidase. Mole weight: 149 kDa. Activity: > 500 U/mL. Storage: 2-8°C. Form: Liquid. Source: Human Neutrophils. Species: Human. MPOB; MPO B; Myeloperoxidase Isoform B; EC 1.11.1.7; 9003-99-0. Cat No: NATE-0460. | |
| Native Human Myeloperoxidase Isoform C | Myeloperoxidase (MPO) is a peroxidase enzyme that in humans is encoded by the MPO gene on chromosome 17. MPO is most abundantly expressed in neutrophil granulocytes (a subtype of white blood cells), and produces hypohalous acids to carry out their antimicrobial activity. It is a lysosomal protein stored in azurophilic granules of the neutrophil and released into the extracellular space during degranulation. MPO has a heme pigment, which causes its green color in secretions rich in neutrophils, such as pus and some forms of mucus. Applications: Protein cystalline research. Group: Enzymes. Synonyms: MPOC; MPO C; Myeloperoxidase Isoform C; EC 1.11.1.7; 9003-99-0. Enzyme Commission Number: EC 1.11.1.7. CAS No. 9003-99-0. Purity: > 96% (SDS-PAGE). Peroxidase. Mole weight: 146 kDa. Activity: Typically > 1 ,000 U/mg protein. Storage: 2-8°C. Form: Liquid. Source: Human Neutrophils. Species: Human. MPOC; MPO C; Myeloperoxidase Isoform C; EC 1.11.1.7; 9003-99-0. Cat No: NATE-0461. | |
| Native Human Myoglobin | Whereas hemoglobin is the carrier of oxygen, myoglobin stores oxygen in the tissues. Like hemoglobin, it also contains a noncovalently bound heme group. The molecule of myoglobin consists of a single polypeptide chain with molecular weight of 16,000 and sequence analysis shows that it has similarities with hemoglobin. Following myocardial infraction myoglobin is lost from cardiac muscle cells and its presence in serum may be used as a diagnostic indicator. Group: Others. Synonyms: Myoglobin; Human Myoglobin. Purity: 0.99. Storage: Store at -20° C. Form: Freeze-dried powder. Source: Human Heart/Muscle. Species: Human. Myoglobin; Human Myoglobin. Cat No: NATE-1880. | |
| Native Human Myosin Subfragment-1 | Myosins comprise a family of ATP-dependent motor proteins and are best known for their role in muscle contraction and their involvement in a wide range of other motility processes in eukaryotes. They are responsible for actin-based motility. The term was originally used to describe a group of similar ATPases found in the cells of both striated muscle tissue and smooth muscle tissue. Applications: Diagnostic controls, calibrators & standards; testing/assay validation; life science; manufacturing. Group: Others. Synonyms: Myosin Subfragment-1; Myosin; Myosin S-1; Myosin 1. Activity: 1 mg/mg solid. Stability: 5 years. Storage: Store at -20°C. Form: Lyophilized from 0.02 mM tris, 0.2 M sodium chloride, pH 8.5. Source: Human Heart. Species: Human. Myosin Subfragment-1; Myosin; Myosin S-1; Myosin 1. Cat No: NATE-0968. | |
| Native Human Neuron Specific Enolase | Neuron specific enolase (NSE) is an enzyme that in humans is encoded by the ENO2 gene. Gamma-enolase is a phosphopyruvate hydratase. Gamma-enolase is one of the three enolase isoenzymes found in mammals. This isoenzyme, a homodimer, is found in mature neurons and cells of neuronal origin. A switch from alpha enolase to gamma enolase occurs in neural tissue during development in rats and primates. Applications: Neuron-specific enolase from human brain has been used in a study to assess human amniotic mesenchymal stem cells in the treatment of focal cerebral ischemia. it has also been used in a study to investigate sinonasal teratocarcinosarcoma with rhabdoid features. Group: Enzymes. Synonyms: EC 4.2.1.11; Neuron Specific Enolase; NSE; enolase; 2-phosphoglycerate dehydratase; 14-3-2-protein; nervous-system specific enolase; phosphoenolpyruvate hydra. Enzyme Commission Number: EC 4.2.1.11. CAS No. 9014-8-8. Enolase. Storage: -20°C. Form: buffered aqueous solution. Source: Human brain. Species: Human. EC 4.2.1.11; Neuron Specific Enolase; NSE; enolase; 2-phosphoglycerate dehydratase; 14-3-2-protein; nervous-system specific enolase; phosphoenolpyruvate hydratase; 2-phosphoglycerate dehydratase; 2-phosphoglyceric dehydratase; 2-phosphoglycerate enolase; γ-enolase; 2-phospho-D-glycerate hydro-lyase; phosphopyruvate hydratase. Cat No: DIA-225. | |
| Native Human Oxyhemoglobin | Hemoglobin is found in the erythrocytes of all vertebrates. It is a conjugated protein with the prosthetic group heme which contains iron. The heme group is involved with the transport of oxygen from the lungs to tissues, while the globin portion of hemoglobin plays a major role in transporting carbon dioxide from the tissues to the lungs. The iron in heme is in the ferrous state. In oxyhemoglobin, it is apparently still in the ferrous state, but the oxygen is loosely bound to it. Group: Others. Synonyms: Oxyhemoglobin; hemoglobin; Human Oxyhemoglobin. Purity: 90% (biuret). Activity: At least 50 U/mg protein. Storage: Store at -20° C. Form: Freeze-dried powder. Source: Human Erythrocytes. Species: Human. Oxyhemoglobin; hemoglobin; Human Oxyhemoglobin. Cat No: NATE-1881. | |
| Native Human Pepsinogen I | Pepsinogen is the zymogen of pepsin. It is processed by autocatalytic cleavage of 44 amino acids to generate active pepsin. Serum levels of pepsinogen have been measured to identify gastric cancer risk. Applications: Research life science. Group: Zymogens. Synonyms: Pepsinogen I. Pepsinogen. Activity: >96%. Storage: 4°C. Source: Human Stomach. Species: Human. Pepsinogen I. Cat No: NATE-0545. | |
| Native Human Pepsinogen II | Pepsinogen is the zymogen of pepsin. It is processed by autocatalytic cleavage of 44 amino acids to generate active pepsin. Serum levels of pepsinogen have been measured to identify gastric cancer risk. Applications: Research life science. Group: Zymogens. Synonyms: Pepsinogen II. Pepsinogen. Activity: >96%. Storage: 4°C. Source: Human Stomach. Species: Human. Pepsinogen II. Cat No: NATE-0546. | |
| Native Human Plasmin | Plasmin functions as a key enzyme of the fibrinolytic cascade, and is also important in inflammation processes. Plasmin exhibits preferential cleavage at the carboxyl side of lysine and arginine residues with higher selectivity than trypsin. Converts polymerized fibrin into soluble products. Plasmin functions as a key enzyme of the fibrinolytic cascade, and is also important in inflammation processes. Applications: A complex between plasmin and an inhibitor has been isolated in a study via affinity chromatography from urokinase-activated human plasma. it has also been used in a study to investigate activation of human epithelial sodium channel (enac) by plasmin and chymotrypsin. Group: Enzymes. Synonyms: fibrinase; fibrinolysin; actase; serum tryptase; thrombolysin; plasmin; EC 3.4.21.7; 9001-90-5; PLG. Enzyme Commission Number: EC 3.4.21.7. CAS No. 9001-90-5. PLG. Activity: > 2.0 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing sodium phosphate, mannitol, and NaCl. Source: Human plasma. Species: Human. fibrinase; fibrinolysin; actase; serum tryptase; thrombolysin; plasmin; EC 3.4.21.7; 9001-90-5; PLG. Cat No: NATE-0598. | |
| Native Human Prostatic Acid Phosphatase | Prostatic acid phosphatase (PAP), also prostatic specific acid phosphatase (PSAP), is an enzyme produced by the prostate. It may be found in increased amounts in men who have prostate cancer or other diseases. The highest levels of acid phosphatase are found in metastasized prostate cancer. Diseases of the bone, such as Paget's disease or hyperparathyroidism, diseases of blood cells, such as sickle-cell disease or multiple myeloma or lysosomal storage diseases, such as Gaucher's disease, will show moderately increased levels. Group: Enzymes. Synonyms: Prostatic acid phosphatase; PAP; prostatic specific acid phosphatase; PSAP; EC 3.1.3.2; ACP; Acid Phos; 5'-nucleotidase; 5'-NT; Ecto-5'-nucleotidase; Thiamine monophosphatase; TMPase; PAPf39. Enzyme Commission Number: EC 3.1.3.2. CAS No. 9001-77-8. Purity: Partially Purified. Apase. Mole weight: 100 kDa. Activity: > 200 U/mL (Dimension Clinical Chemistry System). Appearance: Cloudy, straw colored liquid. Storage: -20°C. Form: Liquid. Source: Human Semen. Species: Human. Prostatic acid phosphatase; PAP; prostatic specific acid phosphatase; PSAP; EC 3.1.3.2; ACP; Acid Phos; 5'-nucleotidase; 5'-NT; Ecto-5'-nucleotidase; Thiamine monophosphatase; TMPase; PAPf39. Cat No: NATE-0505. | |
| Native Human Proteinase 3 | Proteinase 3 also known as PRTN3 is an enzyme that in humans is encoded by the PRTN3 gene. PRTN3 is a serine protease enzyme expressed mainly in neutrophil granulocytes. Its exact role in the function of the neutrophil is unknown, but, in human neutrophils, proteinase 3 contributes to the proteolytic generation of antimicrobial peptides. It is also the epitope of anti-neutrophil cytoplasmic antibodies (ANCAs) of the c-ANCA (cytoplasmic subtype) class, a type of antibody frequently found in the disease granulomatosis with polyangiitis (formerly known as "Wegener's granulomatosis"). Group: Enzymes. Synonyms: PRTN3; proteinase 3; ACPA; AGP7; C-ANCA; CANCA; MBN; MBT; NP-4; NP4; P29; PR-3; PR3; EC 3.4.21.76. Enzyme Commission Number: EC 3.4.21.76. CAS No. 128028-50-2. Purity: > 96% (SDS-PAGE). PRTN3. Activity: Typically > 0.1 U/mg protein. Storage: -20°C. Form: Liquid. Source: Human Neutrophils. Species: Human. PRTN3; proteinase 3; ACPA; AGP7; C-ANCA; CANCA; MBN; MBT; NP-4; NP4; P29; PR-3; PR3; EC 3.4.21.76. Cat No: NATE-0620. | |
| Native Human Protein C | Protein C is a plasma, vitamin κ-dependent zymogen of a serine protease that can inhibit blood coagulation by inhibiting thrombin formation, selectively inactivating Factors Va and VIIIa. The Protein C anticoagulant pathway is triggered when thrombin binds to the endothelial cell proteoglycan, thrombomodulin. This complex, which cannot clot blood, is a potent activator of the protein C zymogen. Activation involves the release of a dodecapeptide from the N-terminal domain of the heavy chain. The activated Protein C (APC) then binds to protein S on cell surfaces and inactivates the coagulation factors Va and VIIIa by proteolysis. APC has also been shown to bind to receptors on the endothelium of large blood vessels. Group: Enzymes. Synonyms: PROC; protein C; blood-coagulation factor XIVa; activated blood coagulation factor XIV; activated protein C; autoprothr. Enzyme Commission Number: EC 3.4.21.69. CAS No. 42617-41-4. Purity: > 90% (SDS-PAGE). Protein C. Mole weight: heavy chain mol wt 41 kDa; light chain mol wt 21 kDa. Storage: -20°C. Form: Lyophilized powder from 20 mM Tris-HCl, pH 7.4, containing 0.1 M NaCl. Source: Human plasma. Species: Human. PROC; protein C; blood-coagulation factor XIVa; activated blood coagulation factor XIV; activated protein C; autoprothrombin II-A; protein Ca; APC; GSAPC; 42617-41-4; EC 3.4.21.69; PROC1. Cat No: NATE-0626. | |
| Native Human Renin | Renin, also known as an angiotensinogenase, is an enzyme that participates in the body's renin-angiotensin aldosterone system (RAAS)--also known as the renin-angiotensin-aldosterone axis--that mediates extracellular volume (i.e., that of the blood plasma, lymph and interstitial fluid), and arterial vasoconstriction. Thus, it regulates the body's mean arterial blood pressure. Renin is often improperly referred to as a hormone even though it has no peripheral receptors and rather has an enzymatic activity with which it hydrolyses angiotensinogen to angiotensin I. Applications: Research elisa assay life science clinical chemistry. Group: Enzymes. Synonyms: REN; HNFJ2; Renin; angiotensinogenase. CAS No. 9015-94-5. Renin. Activity: >90% (>0.5 U/mg). Storage: 4°C. Source: Human Kidney. Species: Human. REN; HNFJ2; Renin; angiotensinogenase. Cat No: NATE-0650. | |
| Native Human Superoxide Dismutase | Superoxide dismutase (SOD) catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. SOD plays a critical role in the defense of cells against the toxic effects of oxygen radicals. SOD competes with nitric oxide (NO) for superoxide anion (which reacts with NO to form peroxynitrite), thereby SOD promotes the activity of NO. SOD has also been shown to suppress apoptosis in cultured rat ovarian follicles, neural cell lines, and transgenic mice by preventing the conversion of NO to peroxynitrate, an inducer of apoptosis. Applications: Superoxide dismutase from human erythr ocytes has been used in a study to identify in vitro glycated sites of hu...-3; SOD-4; hemocuprein; erythrocuprein; cytocuprein; cuprein ; hepatocuprein; 9054-89-1. Enzyme Commission Number: EC 1.15.1.1. CAS No. 9054-89-1. SOD. Activity: > 2,500 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing potassium phosphate buffer salts. Source: Human erythrocytes. Species: Human. Superoxide dismutases; EC 1.15.1.1; superoxidase dismutase; copper-zinc superoxide dismutase; Cu-Zn superoxide dismutase; ferrisuperoxide dismutase; superoxide dismutase I; superoxide dismutase II; SOD; Cu,Zn-SOD; Mn-SOD; Fe-SOD; SODF; SODS; SOD-1; SOD-2; SOD-3; SOD-4; hemocuprein; erythrocuprein; cytocuprein; cuprein ; hepatocuprein; 9054-89-1. Cat No: NATE-0680. | |
| Native Human Thrombin | Thrombin is a serine protease that in humans is encoded by the F2 gene. Prothrombin (coagulation factor II) is proteolytically cleaved to form thrombin in the coagulation cascade, which ultimately results in the reduction of blood loss. Thrombin in turn acts as a serine protease that converts soluble fibrinogen into insoluble strands of fibrin, as well as catalyzing many other coagulation-related reactions. Lyophilized powder containing sucrose, sodium chloride and tris. thrombin is the final coagulation protease in regard to hemostasis, promoting both procoagulant and anticoagulant effects. Group: Enzymes. Synonyms: thrombin; 9002-04-4; EC 3.4.21.5; fibrinogenase; thrombase; thrombofort; topical; thrombin-C; tropostasin; activated blood-coagulation factor II; blood-coagulation factor IIa; factor IIa; E thrombin; β-thrombin; γ-thromb. Enzyme Commission Number: EC 3.4.21.5. CAS No. 9002-4-4. Thrombin. Activity: 600-2,000 NIH units/mg protein (biuret) or > 2,000 NIH units/mg protein (E1%/280 = 19.5); > 125 NIH units/mg protein (biuret). Form: lyophilized powder. Source: Human plasma. Species: Human. thrombin; 9002-04-4; EC 3.4.21.5; fibrinogenase; thrombase; thrombofort; topical; thrombin-C; tropostasin; activated blood-coagulation factor II; blood-coagulation factor IIa; factor IIa; E thrombin; β-thrombin; γ-thrombin. Cat No: NATE-0699. | |
| Native Human Topoisomerase I | Topoisomerase I relaxes supercoiled DNA molecules. The enzyme initiates transient breakages and rejoins of phosphodiester bonds in superhelical turns of closed-circular DNA. Enzyme activity is independent of right-and left-handed superhelices. Cellular topoisomerase i is present in retroviral particles and enhances viral cdna synthesis. Applications: Topoisomerase i has been used in a study to assess implications for the regulation of hiv-1 replication. topoisomerase i has also been used in a study to investigate the tumor suppressor protein kinase chk2 is a mediator of anoikis of intestinal epithelial cells. Group: Enzymes. Synonyms: Topoisomerase I; EC 5.99.1.2; type I DNA topoisomerase; untwisting enzyme; relaxing enzyme; nicking-c. Enzyme Commission Number: EC 5.99.1.2. CAS No. 80449-01-0. TOPO I. Mole weight: mol wt 100 kDa. Activity: > 2 units/μL. Storage: -70°C. Form: buffered aqueous glycerol solution; Solution containing 20 mM sodium phosphate, pH 7.4, 300 mM NaCl, 50 μg/mL BSA, 50% glycerol, and between 25-100 mM imidazole (concentration will be lot dependent). Source: Human. Topoisomerase I; EC 5.99.1.2; type I DNA topoisomerase; untwisting enzyme; relaxing enzyme; nicking-closing enzyme; swivelase; ω-protein; deoxyribonucleate topoisomerase; topoisomerase; type I DNA topoisomerase; DNA topoisomerase; TOPO I. Cat No: NATE-0707. | |
| Native Human Topoisomerase II α | Topoisomerase II α (TopoIIα) is a gene product with conserved catalytic activities and it promotes the progression of DNA damage. The α isoform is present in proliferating cells. Applications: Topoisomerase ii α has been used in a study to assess aging pr ocesses in the human brain. topoisomerase ii α has also been used in a study to investigate its activity in hiv-1 replication. Group: Enzymes. Synonyms: type II DNA topoisomerase; DNA-gyrase; deoxyribonucleate topoisomerase; deoxyribonucleic topoisomerase; topoisomerase; DNA topoisomerase II; DNA topoisomerase (ATP-hydrolysing); EC 5.99.1.3; Topoisomerase II α; TOPO II. Enzyme Commission Number: EC 5.99.1.3. CAS No. 37318-49-3. TOPO II. Mole weight: mol wt 170 kDa. Storage: -70°C. Form: liquid; Solution in 10 mM Tris-HCl, pH 7.1, 0.25 M NaCl, 1 mM EDTA, 0.5 mM PMSF, 1 mM 2-mercaptoethanol, 10% glycerol. Source: Human. type II DNA topoisomerase; DNA-gyrase; deoxyribonucleate topoisomerase; deoxyribonucleic topoisomerase; topoisomerase; DNA topoisomerase II; DNA topoisomerase (ATP-hydrolysing); EC 5.99.1.3; Topoisomerase II α; TOPO II. Cat No: NATE-0710. | |
| Native Human Trypsin | Trypsin (EC 3.4.21.4) is a serine protease from the PA clan superfamily, found in the digestive system of many vertebrates, where it hydrolyses proteins. Trypsin is produced in the pancreas as the inactive protease trypsinogen. Trypsin cleaves peptide chains mainly at the carboxyl side of the amino acids lysine or arginine, except when either is followed by proline. It is used for numerous biotechnological processes. The process is commonly referred to as trypsin proteolysis or trypsinisation, and proteins that have been digested/treated with trypsin are said to have been trypsinized. Applications: Trypsin has been used in a study to assess the similarities between the hepatitis e virus and human astrovirus. trypsin has also been used in a study to characterize a unique technique for culturing primary adult human epithelial progenitor, or stem, cells. Group: Enzymes. Synonyms: α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; trypta. Enzyme Commission Number: EC 3.4.21.4. CAS No. 9002-7-7. Trypsin. Activity: vial of > 1 ,000 BAEE units. Storage: 2-8°C. Form: salt-free, lyophilized powder. Source: Human pancreas. Species: Human. α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; tryptar; trypure; pseudotrypsin; tryptase; tripcellim; sperm receptor hydrolase; Alpha-trypsin; Beta-trypsin; EC 3.4.21.4; Trypsin. Cat No: NATE-0722. | |
| Native Human Tryptase | Tryptase is a member of the serine protease S1 family. It is the predominant neutral protease of the mast cell granules. Within the mast cell granule it exists as a heparin-stabilized active tetramer. Stabilization is a result of the high negative charge density of the glycosaminoglycan. This stabilization activity is observed with heparins with a MW > 6 kDa as well as other glycosaminoglycans such as dextran sulfate or chondroitin sulfates. Removal of heparin results in dissociation of the tetramer and inactivation of the enzyme. High concentrations of NaCl will result in the dissociation of heparin. Tryptase is a glycoprotein released from mast cells during anaphylaxis, which pe...acterized recombinant rat mast cell protease 7 expressed in pichia pastoris. tryptase has also been used in a study to investigate drug allergies in mast cell disease. Group: Enzymes. Synonyms: tryptase; mast cell tryptase; mast cell protease II; skin tryptase; lung tryptase; pituitary tryptase; mast cell neutral proteinase; mast cell tryptase; mast cell neutral proteinase; mast cell serine proteinase II; mast cell proteinase II; mast cell serine proteinase tryptase; rat mast cell protease II; tryptase M; EC 3.4.21.59. Enzyme Commission Number: EC 3.4.21.59. CAS No. 97501-93-4. Tryptase. Mole weight: Molecular Weight: ~135 kDa (Human) (Non-covalently linked tetramer with two sets o | |
| Native Human Urokinase | Urokinase is a serine protease (EC 3.4.21.73). Urokinase was originally isolated from human urine, but is present in several physiological locations, such as blood stream and the extracellular matrix. The primary physiological substrate is plasminogen, which is an inactive form (zymogen) of the serine protease plasmin. Activation of plasmin triggers a proteolysis cascade that, depending on the physiological environment, participates in thrombolysis or extracellular matrix degradation. This links urokinase to vascular diseases and cancer. Urokinase from human urine. Group: Enzymes. Synonyms: Urokinase; EC 3.4.21.73; urokinase-type plasminogen activator; uPA; U-plasminogen activator; Cellular plasminogen activator; Urinary plasminogen activator. Enzyme Commission Number: EC 3.4.21.73. CAS No. 9039-53-6. Purity: Purity by SDS Electrophoresis ? 95 %. uPA. Activity: > 500 units/mg protein. Form: Lyophilized from 1 mL of 50 mM Tris-HCl, pH 7.4 with 100 mM NaCl, 0.1% PEG 6000, and 200 mM mannitol. Source: Human urine. Species: Human. Urokinase; EC 3.4.21.73; urokinase-type plasminogen activator; uPA; U-plasminogen activator; Cellular plasminogen activator; Urinary plasminogen activator. Cat No: PHAM-262. | |
| Native Inulin | Native Inulin. CAS No. 308066-66-2. Product ID: 8-05075. |  |
| Native Jack bean α (1-2,3,6)-Mannosidase | α-Mannosidase is an acid hydrolase which is located in plant vacuoles and is thought to be involved with the turnover of N-linked glycoproteins. α-Mannosidase has been shown to inhibit the proliferation of B-lymphocytes. α-Mannosidase from Canavalia ensiformis is a tretamer composed of two subunits that each contain two components at 44 and 66 kDa. Group: Enzymes. Synonyms: α-mannosidase; α-D-mannosidase; p-nitrophenyl-α-mannosidase; α-D-mannopyranos. Purity: Contaminating glycosidase activities are determined using p-nitrophenyl glycoside substrates and are reported when they are > 0.001% of the enzyme activity. Mannosidase. Mole weight: ~190 kDa daltons. Activity: > 150 U/mL. Stability: The enzyme is stable at 2-8°C and-20°C. The enzyme is unstable below pH 5.5 unless Zn2+ ions are present. It is stable between 6.0-8.5 for 17 hours at 37°C. Ag+ and Hg2+ are potent inhibitors of enzyme activity. Storage: Store at 2-8°C Shipped with cold pack for next day delivery. Form: A sterile-filtered solution in 20 mM Tris-HCl, 20 mM NaCl, pH 7.5. Source: Jack bean. α-mannosidase; α-D-mannosidase; p-nitrophenyl-α-mannosidase; α-D-mannopyranosidase; 1,2-α-mannosidase; 1,2-α-D-mannosidase; exo-α-mannosidase; EC 3.2.1.24; 9025-42-7; Mannosidase. Cat No: NATE-0438. | |
| Native Jack Bean β-(1-2,3,4,6) Hexosaminidase, Sequencing-grade | Hexosaminidase, sometimes called β-N-acetylhexosaminidase, is reported to liberate terminal β-linked N-acetylglucosamine and N-acetylgalactosamine from a variety of substrates. The activity of β-N-actylglucosaminidase may be determined with the chromogenic substrate p-nitrophenyl-N-acetyl-β-D-glucosaminide. β-N-actylglucosaminidase hydrolyzes the terminal nonreducing N-acetyl-D-hexosamine residues. This enzyme contains two predominant isozymes, Hex A, a heterodimer, and Hex B, a homodimer. N-acetylglucosamine, acetamide, N-2-acetamido-2-deoyglucosylamine, N-acetylnojirimycin, and N-acetyldeoxynojirmycin are known inhibitors. Group: Enzymes. Synonyms: β-(1-2,3,4,6) Hexosaminidase; hexosaminidase; β-acetylaminodeoxyhexosidase; N-acetyl-β-D-hexosaminidase; N-acetyl-beta-hexosaminidase; β-hexosaminidase; β-acetylhexosaminidinase; β-D-N-acetylhe. Hexosaminidase. Source: Jack Bean. β-(1-2,3,4,6) Hexosaminidase; hexosaminidase; β-acetylaminodeoxyhexosidase; N-acetyl-β-D-hexosaminidase; N-acetyl-beta-hexosaminidase; β-hexosaminidase; β-acetylhexosaminidinase; β-D-N-acetylhexosaminidase; β-N-acetyl-D-hexosaminidase; β-N-acetylglucosaminidase; hexosaminidase A; N-acetylhexosaminidase; β-D-hexosaminidase. Cat No: NATE-0343. | |
| Native Jack bean β (1-4,6)-Galactosidase | β-galactosidase, also called beta-gal or β-gal, is a hydrolase enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides. Substrates of different β-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins. Group: Enzymes. Synonyms: β (1-4,6)-Galactosidase; β-Galactosidase; beta-gal; β-gal; GLB; 9031-11-2; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat. Enzyme Commission Number: EC 3.2.1.23. CAS No. 9031-11-2. β-gal. Activity: > 6 units/mg protein. Source: Jack bean. β (1-4,6)-Galactosidase; β-Galactosidase; beta-gal; β-gal; GLB; 9031-11-2; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat. Cat No: NATE-0296. | |
| Native Jack bean β-N-Acetylhexosaminidase | The enzyme exhibits a broad specificity, cleaving non-reducing terminal β (1-2,3,4,6)-linked N-acetylglucosamine (GlcNAc) and N-acetylgalactosamine (GalNAc) residues. This enzyme is very useful in the study of isolated glycans, glycolipids and glycoproteins, especially in combination with β-N-acetylhexosaminidase from S. pneumoniae. Group: Enzymes. Synonyms: β-N-Acetylhexosaminidase; N-Acetyl-β-D-glucosaminidase, β-N-Acetylglucosaminidase. β-N-Acetylhexosaminidase. Source: Jack bean. β-N-Acetylhexosaminidase; N-Acetyl-β-D-glucosaminidase, β-N-Acetylglucosaminidase. Cat No: NATE-0783. | |
| Native Jack bean Urease | Ureases (EC 3.5.1.5), functionally, belong to the superfamily of amidohydrolases and phosphotriesterases. It is an enzyme that catalyzes the hydrolysis of urea into carbon dioxide and ammonia. The reaction occurs as follows: (NH2)2CO + H2O ? CO2 + 2NH3. Applications: This enzyme is useful for enzymatic determination of urea in clinical analysis. Group: Enzymes. Synonyms: EC 3.5.1.5; Urease. Enzyme Commission Number: EC 3.5.1.5. CAS No. 9002-13-5. Activity: 100U/mg-solid or more. Appearance: White amorphous powder, lyophilized. Form: Freeze dried powder. Source: Jack bean. EC 3.5.1.5; Urease. Cat No: PHAM-180. | |
| Native Klebsiella pneumoniae Citrate Lyase | Citrate lyase is found in several microorganisms and catalyzes the first step of Citrate degradation, forming acetate and oxaloacetate. The enzyme contains 3 polypeptide subunits, α-subunit (a transferase), β-subunit (acyl lyase) and γ-subunit (acyl-carrier protein). Group: Enzymes. Synonyms: EC 4.1.3.6, citrase; citRatase; citritase; citridesmolase; Citrate aldolase; citric aldolase; Citrate lyase; Citrate oxaloacetate-lyase; Citrate oxaloacetate-lyase [(pro-3S)-CH2COO-?acetate]; 9012-83-3. Enzyme Commission Number: EC 4.1.3.6. CAS No. 9012-83-3. Citrase. Activity: > 0.20 unit/mg solid. Storage: 2-8°C. Form: Lyophilized powder containing bovine serum albumin, sucrose, MgSO4 and EDTA. Source: Klebsiella pneumoniae. EC 4.1.3.6, citrase; citRatase; citritase; citridesmolase; Citrate aldolase; citric aldolase; Citrate lyase; Citrate oxaloacetate-lyase; Citrate oxaloacetate-lyase [(pro-3S)-CH2COO-?acetate]; 9012-83-3. Cat No: NATE-0135. | |
| Native Klebsiella pneumoniae Pullulanase | Pullulanase is a lipoprotein generated as a precursor containing a 19-amino acid signal peptide followed by a palmitate-modified cysteine residue. The signal peptide gets cleaved prior to secretion into the extracellular matrix. Pullulanase is a lipoprotein generated as a precursor containing a 19-amino acid signal peptide followed by a palmitate-modified cysteine residue. the signal peptide gets cleaved prior to secretion into the extracellular matrix. Applications: Pullulanase has been used in a study to assess its l ocation in escherichia coli k12 carrying the cloned structural gene from klebsiella pneumoniae. it has also been used in a study to investigate the role of...lpha;-1,6-glucanohydrolase; 9075-68-7. Enzyme Commission Number: EC 3.2.1.41. CAS No. 9075-68-7. Pullulanase. Activity: Type I, 10-30 units/mg protein; Type II, > 5 units/mg protein (biuret). Storage: -20°C. Form: Type I, Lyophilized powder containing potassium phosphate buffer salts and stabilizer; Type II, ammonium sulfate suspension, Suspension in 3.2 M (NH4)2SO4 solution, pH 6.2. Source: Klebsiella pneumoniae. Pullulanase; EC 3.2.1.41; limit dextrinase (erroneous); amylopectin 6-glucanohydrolase; bacterial debranching enzyme; debranching enzyme; α-dextrin endo-1,6-α-glucosidase; R-enzyme; pullulan α-1,6-glucanohydrolase; 9075-68-7. Cat No: NATE-0643. | |
| Native Kluyveromyces lactis β-Galactosidase | β-galactosidase, also called beta-gal or β-gal, is a hydrolase enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides. SubstRates of different β-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins. A β-galactosidase preparation produced by submerged fermentation of a selected strain of the yeast kluyveromyces lactis. Applications: Lactose was hydrolyzed to monosaccharides using β-galactosidase from kluyveromyces fragilis. Group: Enzymes. Synonyms: Beta-Galactosidase; Galactosidase; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat. CAS No. 9031-11-2. β-gal. Activity: > 2600 units/g. Source: Kluyveromyces lactis. Beta-Galactosidase; Galactosidase; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat. Cat No: NATE-0297. | |
| Native Laccase from Cerrena unicolor | Laccase is a blue copper oxidase that reduces molecular oxygen to water. Laccase oxidizes polyphenols, methoxy-substituted phenols and diamines, but not tyrosine. Oxidation by laccase is an one-electron reaction that generates a free radical. Applications: Decolorization of dyes decompostion of phenolic and aromatic compounds. Group: Enzymes. Synonyms: Laccases; EC 1.10.3.2; 80498-15-3; urishiol oxidase; urushiol oxidase; p-diphenol oxidase; benzenediol:oxygen oxidoreductase. Enzyme Commission Number: EC 1.10.3.2. CAS No. 80498-15-3. Laccase. Stability: 12 months. Storage: store at -20 °C. Form: Freeze-dried powder, no stabilizing agent added. Source: Cerrena unicolor. Laccases; EC 1.10.3.2; 80498-15-3; urishiol oxidase; urushiol oxidase; p-diphenol oxidase; benzenediol:oxygen oxidoreductase. Cat No: NATE-1578. | |
| Native Laccase from White rot fungi | Laccase (Laccase E.C. 1. 10. 3. 2) is a glucoproteinase containing copper. It can catalyze phenols and its derivatives, aromatic amine and its derivatives, carboxylic acids and its derivatives, steroid hormone, biochrome, organometallic compounds and non-phenols substrate. Applications: For indigo-dye-fading technique of jean processing by using laccase and catalysis enzymes in jean-washing industry, for selectively catalyze lignin-degradation and pulp bleaching by using laccase combined medium and xylanase. it is also a new environment friendly technique in wastepaper deinking process. for chlorophenols organic compounds degradation of wastewater treatment (which in line with ph requirements of laccase). for baking. for extract sugar. it can raise color value remaining. for others using as fiberboard adhesive, hair dyeing, lacquer dyeing film formation, crosslinking agent and biological measurement. Group: Enzymes. Synonyms: Laccases; EC 1.10. CAS No. 80498-15-3. Laccase. Activity: 10,000u/ml. Stability: 6 months at 5°C, activity remain ≥90%. Increase dosage after shelf life. Appearance: Liquid. Storage: Should be stored in a cool place to avoid effect of high temperature. Source: White rot fungi. Laccases; EC 1.10.3.2; 80498-15-3; urishiol oxidase; urushiol oxidase; p-diphenol oxidase; benzenediol:oxygen oxidoreductase. Cat No: NATE-1021. | |
| Native Lactate Dehydrogenase from Thermophillic bacteria | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Applications: Diagnostic test and biosensors; nadh recycling. this enzyme is a potential candidate for biocatalysis, suitable for pharmaceutical development / manufacturing. Group: Enzymes. Synonyms: Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Storage: Store at -20°C. Form: Frozen Liquid. Source: Thermophillic bacteria. Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Cat No: DIA-400. | |
| Native Lactobacillus 30a L-Histidine Decarboxylase | Histidine decarboxylase (HDC) is the enzyme that catalyzes the reaction that produces histamine from histidine with the help of vitamin B6 as follows:Conversion of histidine to histamine by histidine decarboxylase. In humans, the histidine decarboxylase enzyme is encoded by the HDC gene. Applications: Major synthetic enzyme for histamine; decarboxylates l-histidine to form histamine. Group: Enzymes. Synonyms: Histidine decarboxylase; HDC; 9024-61-7; EC 4.1.1.22; L-histidine decarboxylase; L-histidine carboxy-lyase; L-Histidine Decarboxylase. Enzyme Commission Number: EC 4.1.1.22. CAS No. 9024-61-7. HDC. Activity: 0.25-0.5 unit/mg solid. Storage: -20°C. Form: crude acetone powder. Source: Lactobacillus 30a. Histidine decarboxylase; HDC; 9024-61-7; EC 4.1.1.22; L-histidine decarboxylase; L-histidine carboxy-lyase; L-Histidine Decarboxylase. Cat No: NATE-0336. | |
| Native Lactobacillus delbrückii D-Lactate Dehydrogenase, Grade I | In enzymology, a D-lactate dehydrogenase is an enzyme that catalyzes the chemical reaction: (D)-lactate + 2 ferricytochrome c<-> pyruvate + 2 ferrocytochrome c. Thus, the two substrates of this enzyme are (D)-lactate and ferricytochrome c, whereas its two products are pyruvate and ferrocytochrome c. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with a cytochrome as acceptor. This enzyme participates in pyruvate metabolism. It employs one cofactor, FAD. Dehydrogenase that catalyzes the interconversion of d(-)-lactate to pyruvate. rely on the proven diagnostic quality of this product. benefit from the...ase; D-lactate (cytochrome) dehydrogenase; cytochrome-dependent D-(-)-lactate dehydrogenase; D-lactate-cytochrome c reductase; D-(-)-lactic cytochrome c reductase. CAS No. 9028-36-8. D-LDH. Activity: >180 U/mg. Stability: At +2 to +8°C within specification range for 12 months. Store dry. Appearance: White to yellowish lyophilizate. Source: Lactobacillus delbrückii. EC 1.1.1.28; D-Lactic Dehydrogenase; 9028-36-8; (D)-lactate:ferricytochrome-c 2-oxidoreductase; lactic acid dehydrogenase; D-lactate (cytochrome) dehydrogenase; cytochrome-dependent D-(-)-lactate dehydrogenase; D-lactate-cytochrome c reductase; D-(-)-lactic cytochrome c reductase. Cat No: NATE-0976. | |
| Native Lactobacillus delbrückii D-Lactate Dehydrogenase, Grade II | In enzymology, a D-lactate dehydrogenase is an enzyme that catalyzes the chemical reaction: (D)-lactate + 2 ferricytochrome c<-> pyruvate + 2 ferrocytochrome c. Thus, the two substrates of this enzyme are (D)-lactate and ferricytochrome c, whereas its two products are pyruvate and ferrocytochrome c. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with a cytochrome as acceptor. This enzyme participates in pyruvate metabolism. It employs one cofactor, FAD. Dehydrogenase that catalyzes the interconversion of d(-)-lactate to pyruvate. rely on the proven diagnostic quality of this product. Applications: U...ase; D-lactate (cytochrome) dehydrogenase; cytochrome-dependent D-(-)-lactate dehydrogenase; D-lactate-cytochrome c reductase; D-(-)-lactic cytochrome c reductase. CAS No. 9028-36-8. D-LDH. Activity: >150 U/mg. Stability: At +2 to +8°C within specification range for 12 months. Store dry. Appearance: White to yellowish lyophilizate. Source: Lactobacillus delbrückii. EC 1.1.1.28; D-Lactic Dehydrogenase; 9028-36-8; (D)-lactate:ferricytochrome-c 2-oxidoreductase; lactic acid dehydrogenase; D-lactate (cytochrome) dehydrogenase; cytochrome-dependent D-(-)-lactate dehydrogenase; D-lactate-cytochrome c reductase; D-(-)-lactic cytochrome c reductase. Cat No: NATE-0977. | |
| Native Lactobacillus leichmanii D-Lactic Dehydrogenase | D-lactic dehydrogenase catalyzes the conversion of D-lactate into D-pyruvate while reducing NAD+ to NADH and H+. Applications: In the food industry, the primary catalysis is coupled to conversion of nadh and h+ to nad+ with diaphorase coupled with converting the non-fluorescent resazurin to the highly fluorescent substance resorufin to measure the content of d-lactate in food products. Group: Enzymes. Synonyms: EC 1.1.1.28, D-Lactic Dehydrogenase; 9028-36-8; lactic acid dehydrogenase; D-specific lactic dehydrogenase; D-(-)-lactate dehydrogenase (NAD); D-lactic acid dehydrogenase; D-lactic dehydrogenase; (R)-Lactate:NAD+ oxidoreductase; D-LDH. Enzyme Commission Number: EC 1.1.1.28. CAS No. 9028-36-8. D-LDH. Activity: > 30 units/mg protein; ~1000 U/mL; 250-500 units/mg protein (biuret); 150-300 units/mg protein; 1,000-3,000 units/mg protein (biuret). Storage: 2-8°C. Form: Suspension in 3.2 M (NH4)2SO4, 0.1 M potassium phosphate, pH 7.0. Source: Lactobacillus leichmanii. EC 1.1.1.28, D-Lactic Dehydrogenase; 9028-36-8; lactic acid dehydrogenase; D-specific lactic dehydrogenase; D-(-)-lactate dehydrogenase (NAD); D-lactic acid dehydrogenase; D-lactic dehydrogenase; (R)-Lactate:NAD+ oxidoreductase; D-LDH. Cat No: NATE-0195. | |
| Native Lactobacillus reuteri Glucansucrase (α-glucanotransferase) | A moderately thermostable Glucansucrase (4,6-Alpha-Glucanotransferase, reuteransucrase). The enzyme transfers glucose units from sucrose to make a highly branched, high molecular weight alpha-D-Glucan with α (1?4) glucosidic linkages and also some α (1?6) linked glucosyl units. Group: Enzymes. Synonyms: Alpha-glucanotransferase; glucosyltransferase; 4,6-alpha-Glucanotransferase; EC 2.4.1.-. Enzyme Commission Number: EC 2.4.1.-. Glucansucrase. Source: Lactobacillus reuteri strain 121. Species: Lactobacillus reuteri. Alpha-glucanotransferase; glucosyltransferase; 4,6-alpha-Glucanotransferase; EC 2.4.1.-. Cat No: NATE-0304. | |
| Native Lactobacillus sp. Maltose Epimerase | Maltose 1-epimerase (MER), is an enzyme that catalyzes the interconversion of αand β anomers of maltose. Maltose 1-epimerase (mer), is an enzyme that catalyzes the interconversion of α and β anomers of maltose. Applications: Maltose epimerase has been used in a study to assess metabolite gene regulation. it has also been used in a study to investigate saccharogenic determination of α-amylase in serum and urine. Group: Enzymes. Synonyms: maltose epimerase; EC 5.1.3.21; maltose 1-epimerase; MER. Enzyme Commission Number: EC 5.1.3.21. MER. Mole weight: mol wt ~45 kDa by SDS-PAGE. Storage: -20°C. Source: Lactobacillus sp. maltose epimerase; EC 5.1.3.21; maltose 1-epimerase; MER. Cat No: NATE-0450. | |
| Native Leuconostoc mesenteroides 6-Phosphogluconolactonase | 6-Phosphogluconolactonase is an enzyme in the pentose phosphate pathway. It converts 6-phosphogluconolactone to 6-phosphogluconate. Hydrolase that catalyzes the conversion of 6-phosphogluconolactone to 6-phosphogluconate. increase the sensitivity of your creatine kinase assay. Applications: Use 6-phosphogluconolactonase in diagnostic tests for the determination of creatine kinase or glucose in the combination with hexokinase, glucose-6-phosphate dehydrogenase and phosphogluconate dehydrogenase. Group: Enzymes. Synonyms: 6-Phosphogluconolactonase. 6-Phosphogluconolactonase. Mole weight: 38 kD (SDS). Activity: >50 U/mg. Stability: At -15 to -25°C within specification range for 12 months. Appearance: White lyophilizate. Source: Leuconostoc mesenteroides. Species: Leuconostoc mesenteroides. 6-Phosphogluconolactonase. Cat No: NATE-0889. | |
| Native Leuconostoc mesenteroides Dextran Sucrase | Dextransucrases are glucansucrases that are able to produce dextran, a glucose polymer linked mainly through α1-6 bonds. However, α1-3, α1-6, α1-4 and α1-2 bonds are also found, in both the main chain and the branching linkages. The peptide has approximately 1600 amino acids. The aspartic acid in position 551 is essential for catalytic activity, while glutamic acid 589 and aspartic acid 662 complement the catalytic triad. The activity of dextransucrase is decreased by EDTA, and is restored by the addition of calcium ions. Zinc, cadmium, lead, mercury and copper ions are inhibitory to various degrees. Applications: Dextran sucrase from leu... immobilized sphere for the production of dextran from sucrose. Group: Enzymes. Synonyms: EC 2.4.1.5, sucrose 6-glucosyltransferase; SGE; CEP; sucrose-1,6-α-glucan glucosyltransferase; sucrose:1,6-α-D-glucan 6-α-D-glucosyltransferase; 9032-14-8. Enzyme Commission Number: EC 2.4.1.5. CAS No. 9032-14-8. SGE. Activity: > 100 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing dextran, MES buffer salts and CaCl2. Source: Leuconostoc mesenteroides. EC 2.4.1.5, sucrose 6-glucosyltransferase; SGE; CEP; sucrose-1,6-α-glucan glucosyltransferase; sucrose:1,6-α-D-glucan 6-α-D-glucosyltransferase; 9032-14-8. Cat No: NATE-0669. | |
| Native Leuconostoc mesenteroides D-Lactic Dehydrogenase | In enzymology, a D-lactate dehydrogenase is an enzyme that catalyzes the chemical reaction: (D)-lactate + 2 ferricytochrome c<-> pyruvate + 2 ferrocytochrome c. Thus, the two substrates of this enzyme are (D)-lactate and ferricytochrome c, whereas its two products are pyruvate and ferrocytochrome c. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with a cytochrome as acceptor. This enzyme participates in pyruvate metabolism. It employs one cofactor, FAD. Group: Enzymes. Synonyms: EC 1.1.1.28; D-Lactic Dehydrogenase; 9028-36-8; (D)-lactate:ferricytochrome-c 2-oxidoreductase; lactic acid dehydrogenase; D-lactate (cytochrome) dehydrogenase; cytochrome-dependent D-(-)-lactate dehydrogenase; D-lactate-cytochrome c reductase; D-(-)-lactic cytochrome c reductase. Enzyme Commission Number: EC 1.1.1.28. CAS No. 9028-36-8. D-LDH. Activity: 1,000-3,000 units/mg protein (biuret). Stability: 2-8°C. Form: ammonium sulfate suspension. Source: Leuconostoc mesenteroides. EC 1.1.1.28; D-Lactic Dehydrogenase; 9028-36-8; (D)-lactate:ferricytochrome-c 2-oxidoreductase; lactic acid dehydrogenase; D-lactate (cytochrome) dehydrogenase; cytochrome-dependent D-(-)-lactate dehydrogenase; D-lactate-cytochrome c reductase; D-(-)-lactic cytochrome c reductase. Cat No: NATE-0196. | |
| Native Leuconostoc mesenteroides Glucose-6-phosphate Dehydrogenase | Glucose-6-phosphate dehydrogenase (G6PD or G6PDH) (EC 1.1.1.49) is a cytosolic enzyme that catalyzes the chemical reaction:D-glucose 6-phosphate + NADP+ ? 6-phospho-D-glucono-1,5-lactone + NADPH + H+. This enzyme is in the pentose phosphate pathway, a metabolic pathway that supplies reducing energy to cells (such as erythrocytes) by maintaining the level of the co-enzyme nicotinamide adenine dinucleotide phosphate (NADPH). Applications: Glucose-6-phosphate dehydrogenase was used as a model to test the effect of seed protein fractions on enzyme protection during dehydration. g-6-pdh has been utilized in assays for nicotinamide adenine dinucleotide and tissue pyridine nucleotides. Group: Enzymes. Synonyms: EC 1.1.1.49; NADP-glucose-6-phosphate dehydrogenase; Zwischenferment; D-glucose 6-p. Enzyme Commission Number: EC 1.1.1.49. CAS No. 9001-40-5. Activity: 20U/mg-solid or more. Storage: 2-8°C. Form: Freeze dried powder. Source: Leuconostoc mesenteroides. EC 1.1.1.49; NADP-glucose-6-phosphate dehydrogenase; Zwischenferment; D-glucose 6-phosphate dehydrogenase; glucose 6-phosphate dehydrogenase (NADP); NADP-dependent glucose 6-phosphate dehydrogenase; 6-phosphoglucose dehydrogenase; Entner-Doudoroff enzyme; glucose-6-phosphate 1-dehydrogenase; G6PDH; GPD; glucose-6-phosphate dehydrogenase; 9001-40-5. Cat No: DIA-321. | |
| Native Leuconostoc mesenteroides Mannitol Dehydrogenase | In enzymology, a mannitol 2-dehydrogenase (EC 1.1.1.67) is an enzyme that catalyzes the chemical reaction:D-mannitol + NAD+<-> D-fructose + NADH + H+. Thus, the two substrates of this enzyme are D-mannitol and NAD+, whereas its 3 products are D-fructose, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in fructose and mannose metabolism. Applications: This preparation is useful in the determination of mannitol in urine. can be used for the production of d-mannitol. it has been used in a study to assess glucosylglycerol and glucosylglycerate as enzyme stabilizers. Group: Enzymes. Synonyms: mannitol dehydrogenase; D-mannitol dehydrogenase; mannitol dehydrogenase; mannitol 2-dehydrogenase; EC 1.1.1.67; 9001-65-4. Enzyme Commission Number: EC 1.1.1.67. CAS No. 9001-65-4. Mannitol Dehydrogenase. Mole weight: 136 kDa. Activity: > 60 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing buffer salts, potassium phosphate, and dithiothreitol. Source: Leuconostoc mesenteroides. mannitol dehydrogenase; D-mannitol dehydrogenase; mannitol dehydrogenase; mannitol 2-dehydrogenase; EC 1.1.1.67; 9001-65-4. Cat No: NATE-0435. | |
| Native Leuconostoc Mesenteroides Sucrose Phosphorylase | Sucrose phosphorylase (EC. 2.4.1.7) is an important enzyme in the metabolism of sucrose and regulation of other metabolic intermediates. Sucrose phosphorylase is in the class of hexosyltransferases. More specifically it has been placed in the retaining glycoside hydrolases family although it catalyzes a transglycosidation rather than hydrolysis. Sucrose phosphorylase catalyzes the conversion of sucrose to D-fructose and α-D-glucose-1-phosphate. It has been shown in multiple experiments that the enzyme catalyzes this conversion by a double displacement mechanism. Group: Enzymes. Synonyms: Sucrose Phosphorylase; EC 2.4.1.7; sucrose glucosyltransferase; disaccharide glucosyltransferase; Sucrose:orthophosphate α-D-glucosytransferase. Enzyme Commission Number: EC. 2.4.1.7. CAS No. 9074-06-0. Sucrose Phosphorylase. Activity: > 100 units/mg protein. Storage: Store at -20°C. Form: Lyophilized powder. Source: Leuconostoc Mesenteroides. Sucrose Phosphorylase; EC 2.4.1.7; sucrose glucosyltransferase; disaccharide glucosyltransferase; Sucrose:orthophosphate α-D-glucosytransferase. Cat No: NATE-0890. | |
| Native Lignin Peroxidase | Lignin peroxidase is a fungal enzyme which has a key role in the ligninolytic cycle, the process by which the structural component of plant walls, lignin, is degraded. Group: Enzymes. Synonyms: lignin peroxidase; diarylpropane oxygenase; ligninase I; diarylpropane peroxidase; diarylpropane:oxygen,hydrogen-peroxide oxidoreductase (C-C-bond-cleaving); LiP; 42613-30-9. CAS No. 42613-30-9. LiP. Activity: >0.1 units/mg. Storage: -20°C. Form: powder; slightly beige. lignin peroxidase; diarylpropane oxygenase; ligninase I; diarylpropane peroxidase; diarylpropane:oxygen,hydrogen-peroxide oxidoreductase (C-C-bond-cleaving); LiP; 42613-30-9. Pack: Bottomless glass bottle. Contents are inside inserted fused cone. Cat No: NATE-0396. | |
| Native Lignin Peroxidase from Phanerochaete chrysosporium | Lignin peroxidase is a fungal enzyme which has a key role in the ligninolytic cycle, the process by which the structural component of plant walls, lignin, is degraded. Applications: Demethoxylation cα-cβ cleavage benzylic alcohol oxidation degradation of lignins, polycyclic aromatic hydrocarbons and xenobiotic compounds. Group: Enzymes. Synonyms: lignin peroxidase; diarylpropane oxygenase; ligninase I; diarylpropane peroxidase; diarylpropane:oxygen,hydrogen-peroxide oxidoreductase (C-C-bond-cleaving); LiP; 42613-30-9. Enzyme Commission Number: EC 1.11.1.14. CAS No. 93792-13-3. LiP. Stability: 6 months. Storage: store at -20 °C. Form: Freeze-dried powder, no stabilizing agent added. Source: Phanerochaete chrysosporium. lignin peroxidase; diarylpropane oxygenase; ligninase I; diarylpropane peroxidase; diarylpropane:oxygen,hydrogen-peroxide oxidoreductase (C-C-bond-cleaving); LiP; 42613-30-9. Cat No: NATE-1579. | |
| Native Limpets (Patella vulgata) β-Glucuronidase | β-glucuronidase catalyzes the breakdown of complex carbohydrates. In humans it converts conjugated bilirubin into the unconjugated form, making bilirubin suitable for reabsorption. Type l-ii, lyophilized powder, 1 kda kda-3 kda kda units/g solid; aqueous solution, > 85 kda units/ml. Group: Enzymes. Synonyms: β-glucuronide glucuronohydrolase glucuronidase; exo-β-D-glucuronidase; ketodase; EC 3.2.1.31; 9001-45-0; β-D-glucuronoside glucuronosohydrolase; GUSB. Enzyme Commission Number: EC 3.2.1.31. CAS No. 9001-45-0. GUSB. Form: lyophilized powder or aqueous solution (Aqueous solution in 0.9% NaCl with 0.02% sodium azide as preservative). Source: Limpets (Patella vulgata). β-glucuronide glucuronohydrolase glucuronidase; exo-β-D-glucuronidase; ketodase; EC 3.2.1.31; 9001-45-0; β-D-glucuronoside glucuronosohydrolase; GUSB. Cat No: NATE-0332. | |
| Native Lysobacter enzymogenes Endoproteinase Lys-C | Endoproteinase Lys-C inactivates the enzyme inositol monophosphatase by cleaving it at a single site directly after Lys 36. Endoproteinase lys-c is an enzyme that preferentially cleaves at the carboxyl side of lysine residues. Applications: Endoproteinase lys-c from lysobacter enzymogenes is useful in the determination of primary structures of proteins. it has been used in a study to investigate the evidence for trisulfide bonds in a recombinant variant of a human igg2 mon oclonal antibody. endoproteinase lys-c has been used for the digestion mon oclonal antibodies for disulfide bond assignment. Group: Enzymes. Synonyms: EC 3.4.21.50; chromobacter proteinase I; Achromobacter lyticus alkaline proteinase I; protease I; achromopeptidase; lysyl bond specific proteinase; 72561-05-8; Achromobacter proteinase I; Endoproteinase Lys-C. Enzyme Commission Number: EC 3.4.21.50. CAS No. 72561-05-8. Achromopeptidase. Storage: 2-8°C. Form: lyophilized powder. Source: Lysobacter enzymogenes. EC 3.4.21.50; chromobacter proteinase I; Achromobacter lyticus alkaline proteinase I; protease I; achromopeptidase; lysyl bond specific proteinase; 72561-05-8; Achromobacter proteinase I; Endoproteinase Lys-C. Cat No: NATE-0220. | |
| Native Lysozyme Biotin-Caproyl | Total activity of conjugate against immobilized avidin >95%. Contains approx. two moles biotin to one mole of lysozyme. Group: Enzymes. Synonyms: Lysozyme Biotin-Caproyl. Lysozyme. Activity: >20,000 U/mg. Storage: Store at 2-8°C. Form: Lyophilized powder containing potassium phosphate and sodium chloride. Lysozyme Biotin-Caproyl. Pack: 0.2 mg in glass bottle. Cat No: NATE-0891. | |
| Native Malate dehydrogenase (Decarboxylating) from Thermophillic bacteria | Malate dehydrogenase 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 malate to pyruvate producing 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 ...; malate NAD dehydrogenase; NAD-dependent malate dehydrogenase; NAD-sp; ECific malate dehydrogenase; NAD-linked malate dehydrogenase; MDH; L-malate-NAD+ oxidoreductase; S-malate: NAD+ oxidoreductase; EC 1.1.1.38; Malate Dehydrogenase. Enzyme Commission Number: EC 1.1.1.38. CAS No. 9080-52-8. MDH. Storage: Store at -20°C. Form: Frozen Liquid. Source: Thermophillic bacteria. malic dehydrogenase; L-malate dehydrogenase; NAD-L-malate dehydrogenase; malic acid dehydrogenase; NAD-dependent malic dehydrogenase; NAD-malate dehydrogenase; NAD-malic dehydrogenase; malate NAD dehydrogenase; NAD-dependent malate dehydrogenase; NAD-sp; ECific malate dehydrogenase; NAD- | |
| Native Malate dehydrogenase from Thermophillic bacteria | Malate dehydrogenase 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 malate to pyruvate producing 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...e dehydrogenase; NAD-sp; ECific malate dehydrogenase; NAD-linked malate dehydrogenase; MDH; L-malate-NAD+ oxidoreductase; S-malate: NAD+ oxidoreductase; EC 1.1.1.37; Malate Dehydrogenase. Enzyme Commission Number: EC 1.1.1.37. CAS No. 9001-64-3. MDH. Storage: Store at -20°C. Form: Frozen Liquid. Source: Thermophillic bacteria. malic dehydrogenase; L-malate dehydrogenase; NAD-L-malate dehydrogenase; malic acid dehydrogenase; NAD-dependent malic dehydrogenase; NAD-malate dehydrogenase; NAD-malic dehydrogenase; malate NAD dehydrogenase; NAD-dependent malate dehydrogenase; NAD-sp; ECific malate dehydrogenase; NAD-linked malate dehydrogenase; MDH; L-malate-NAD+ oxidored | |
| Native Mammalian Ubiquitin Conjugating Enzyme Fractions | Ubiquitin-conjugating enzymes perform the second step in the ubiquitination reaction that targets a protein for degradation via the proteasome. The ubiquitination process covalently attaches ubiquitin, a short protein of 76 amino acids, to a lysine residue on the target protein. Once a protein has been tagged with one ubiquitin molecule, additional rounds of ubiquitination form a polyubiquitin chain that is recognized by the proteasome's 19S regulatory particle, triggering the ATP-dependent unfolding of the target protein that allows passage into the proteasome's 20S core particle, where proteases degrade the target into short peptide fragments for recycling by the cell. Applications: Ubiquitin conjugating enzyme fractions mammalian may be used in transferring the activated ubiquitin from e1 to the substrate through an additional high energy thiol ester intermediate e2-s-ubiquitin. ubiquitin-conjugating enzymes, also known as e2 enzymes and more rarely as ubiquitin-carrier enzymes, perform the second step in the ubiquitination reaction that targets a protein for degradation via the proteasome. Group: Enzymes. Synonyms: Ubiquitin con. Ubiquitin Conjugating Enzyme. Storage: -70°C. Source: Mammalian. Ubiquitin conjugating enzymes; Ubiquitin Conjugating Enzyme Fractions; E2 enzymes; ubiquitin-carrier enzymes. Cat No: NATE-0727. | |
| Native Microbial α-phosphoglucomutase | Phosphoglucomutase (EC 5.4.2.2) is an enzyme that transfers a phosphate group on an α-D-glucose monomer from the 1' to the 6' position in the forward direction or the 6' to the 1' position in the reverse direction. More precisely, it facilitates the interconversion of glucose 1-phosphate and glucose 6-phosphate. High purity recombinant α-phosphoglucomutase (microbial) for use in research, biochemical enzyme assays and in vitro diagnostic analysis. Group: Enzymes. Synonyms: α-phosphoglucomutase; Phosphoglucomutase; EC 5.4.2.2; Phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent); Glucose phosphomutase; Phosphoglucose mutase. Enzyme Commission Number: EC 5.4.2.2. CAS No. 9001-81-4. Phosphoglucomutase. Mole weight: MW ~ 59.2 kDa. Source: Microbial. α-phosphoglucomutase; Phosphoglucomutase; EC 5.4.2.2; Phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent); Glucose phosphomutase; Phosphoglucose mutase. Cat No: DIA-265. | |
| Native Microbial Creatinine Deiminase | In enzymology, a creatinine deaminase (EC 3.5.4.21) is an enzyme that catalyzes the chemical reaction: creatinine + H2O <-> N-methylhydantoin + NH3. Thus, the two substrates of this enzyme are creatinine and H2O, whereas its two products are N-methylhydantoin and NH3. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is creatinine iminohydrolase. Applications: Creatinine deiminase has been used in a study to assess the application of a creatinine-sensitive biosensor for hemodialysis control. creatinine deiminase has also been used in a study to investigate the bioelectronic tongue for the simultaneous determination of urea, creatinine and alkaline ions in clinical samples. Group: Enzymes. Synonyms: EC 3.5.4.21, creatinine hydrolase; creatinine desiminase; creatinine deaminase; 37289-15-9. Enzyme Commission Number: EC 3.5.4.21. CAS No. 37289-15-9. Creatinine Deiminase. Mole weight: mol wt ~260 kDa. Activity: > 25 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing mannitol as stabilizer. Source: Microbial. EC 3.5.4.21, creatinine hydrolase; creatinine desiminase; creatinine deaminase; 37289-15-9. Cat No: NATE-0164. | |
| Native Microbial Xanthine Oxidase | Xanthine oxidase is a molybdenum-containing enzyme that is found in the cytosol, and may be strongly inhibited by flavonoids. It plays a vital role in the metabolism of some drugs, as well as purines and pyrimidines. It is also known to be a biological source of reactive oxygen species. Xanthine oxidase was shown to be involved in the reduction of cytochrome c by the generation of superoxide anions following the oxidation of xanthine. These free radicals are responsible for reducing cytochrome c. Allopurinol is a synthetic drug show to inhibit xanthine oxidase. Applications: This enzyme is useful for enzymatic determination of inorganic phosphorus, 5?-nucleotidase and adenosine deaminase when coupled with purine-nucleoside phosphorylase and uricase. Group: Enzymes. Synonyms: Xanthine oxidase; XO; xanthine oxidoreductase; EC 1.17. Enzyme Commission Number: EC 1.17.3.2. CAS No. 9002-17-9. XAO. Mole weight: mol wt ~160 kDa. Activity: > 7 units/mg solid. Storage: -20°C. Form: Lyophilized powder containing BSA and sodium glutamate as stabilizers. Source: Microbial. Xanthine oxidase; XO; xanthine oxidoreductase; EC 1.17.3.2; 9002-17-9; XOD; Xanthine:oxygen oxidoreductase; hypoxanthine oxidase; hypoxanthine:oxygen oxidoreductase; Schardinger enzyme; hypoxanthine-xanthine oxidase; xanthine:O2 oxidoreductase; xanthine:xanthine oxidase. Cat No: NATE-0733. | |
| Native Micrococcus lysodeikticus Catalase | Catalase activates the decomposition of hydrogen peroxide, a reactive oxygen species, into water and oxygen. It functions as a natural antioxidant, protecting cells against oxidative damage to proteins, lipids and nucleic acids. Catalase has also been used to study the role reactive oxygen species play in gene expression and apoptosis. Group: Enzymes. Synonyms: EC 1.11.1.6; Catalase; catalase; equilase; caperase; optidase; catalase-peroxidase; CAT; H2O2:H2O2 oxidoreductase; 9001-05-2. Enzyme Commission Number: EC 1.11.1.6. CAS No. 9001-5-2. CAT. Mole weight: Mr ~230 kDa. Storage: 2-8°C. Form: solution. Source: Micrococcus lysodeikticus. EC 1.11.1.6; Catalase; catalase; equilase; caperase; optidase; catalase-peroxidase; CAT; H2O2:H2O2 oxidoreductase; 9001-05-2. Cat No: NATE-0109. | |
| Native Microorganism Alkaline phosphatase | Alkaline phosphatase (ALP, ALKP, ALPase, Alk Phos) (EC 3.1.3.1) is a hydrolase enzyme responsible for removing phosphate groups from many types of molecules, including nucleotides, proteins, and alkaloids. The process of removing the phosphate group is called dephosphorylation. As the name suggests, alkaline phosphatases are most effective in an alkaline environment. It is sometimes used synonymously as basic phosphatase. Group: Enzymes. Synonyms: Alkaline phosphatase; ALP; ALKP; ALPase; Alk Phos; EC 3.1.3.1; Alkaline phosphomonoesterase; Glycerophosphatase; Phosphomonoesterase. Enzyme Commission Number: EC 3.1.3.1. CAS No. 9001-78-9. ALP. Storage: Storage at 2-8 centigrade. Source: Microorganism. Alkaline phosphatase; ALP; ALKP; ALPase; Alk Phos; EC 3.1.3.1; Alkaline phosphomonoesterase; Glycerophosphatase; Phosphomonoesterase. Cat No: DIA-181. | |
| Native Microorganism α-Glucosidase (MALTASE) | Glycoside hydrolases (also called glycosidases or glycosyl hydrolases) assist in the hydrolysis of glycosidic bonds in complex sugars. They are extremely common enzymes with roles in nature including degradation of biomass such as cellulose and hemicellulose, in anti-bacterial defense strategies (e.g., lysozyme), in pathogenesis mechanisms (e.g., viral neuraminidases) and in normal cellular function (e.g., trimming mannosidases involved in N-linked glycoprotein biosynthesis). Together with glycosyltransferases, glycosidases form the major catalytic machinery for the synthesis and breakage of glycosidic bonds. Applications: This enzyme is useful for structural investi...tase; alpha-D-glucosidase; alpha-glucoside hydrolase; alpha-1,4-glucosidase; alpha-D-glucoside glucohydrolase; glycosidases; glycosyl hydrolases; α-Glucosidase. Enzyme Commission Number: EC 3.2.1.20. CAS No. 9001-42-7. Activity: 20U/mg-solid or more. Appearance: White amorphous powder, lyophilized. Form: Freeze dried powder. Source: Microorganism. Alpha-glucosidase; EC 3.2.1.20; maltase; glucoinvertase; glucosidosucrase; maltase-glucoamylase; alpha-glucopyranosidase; glucosidoinvertase; alpha-D-glucosidase; alpha-glucoside hydrolase; alpha-1,4-glucosidase; alpha-D-glucoside glucohydrolase; glycosidases; glycosyl hydrolases; α-Glucosidase. Cat No: DIA-194. | |
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