Creative Enzymes - Products
Enzyme manufacturing for life science research and medicines, food, alcohol, fabric, paper etc. Uses include: drug discovery, cancer and infectious disease research, microbiology and personalized medicine.
| Product | Description | |
|---|---|---|
| Native Human Cathepsin S | Cathepsin S is a lysosomal cysteine protease found primarily in the spleen and in lung macrophages. Its level is elevated in the brain tissue of those with Alzheimer's disease and Down syndrome. Cathepsin S may function in the processing of amyloid precursor protein to amyloid beta peptides. Applications: Cathepsin s from human spleen has been used in a study to assess the sequence identification, tissue distribution and polymorphism of the porcine cathepsin d (ctsd) gene. cathepsin s from human spleen has also been used in a study to investigate a new promising camptothecin analogue-polysaccharide conjugate. Group: Enzymes. Synonyms: CTSS; cathepsin S; EC 3.4.22.27; FLJ50259; MGC3886. Enzyme Commission Number: EC 3.4.22.27. CTSS. Storage: -70°C. Form: lyophilized powder. Lyophilized from 100 mM sodium acetate, pH 5.5, and 1 mM EDTA. Source: Human spleen. Species: Human. CTSS; cathepsin S; EC 3.4.22.27; FLJ50259; MGC3886. Cat No: NATE-0178. |  |
| Native Human Creatine Kinase BB | Creatine Kinase BB is concentrated in the brain and lungs Because the CKBB isoenzyme, CPK-1 isoenzyme is predominately found in the brain and lungs, injury to either of these organs (for example, stroke or lung injury due to a pulmonary embolism) are associated with elevated levels of this isoenzyme. Group: Enzymes. Synonyms: CPK-1; CKBB isoenyzme; CK-BB; CKB; creatine kinase, brain; CKBB; creatine kinase B-type; creatine kinase-B; creatine kinase B chain; B-CK; Brain-type creatine kinase; Creatine Kinase BB; BB-CK. Enzyme Commission Number: EC 2.7.3.2. CAS No. 9001-15-4. Purity: CK-BB: > 99%. CK-MM: < 1%. CK-MB: < 1%. Activity:> 500 U/mL. Storage: Store at -20° C. Form: Liquid, 50% Glycerol, 25 mM Imidazole, 1 mM DTE, pH 6.5. Source: Human Brain. Species: Human. CPK-1; CKBB isoenyzme; CK-BB; CKB; creatine kinase, brain; CKBB; creatine kinase B-type; creatine kinase-B; creatine kinase B chain; B-CK; Brain-type creatine kinase; Creatine Kinase BB; BB-CK. Cat No: NATE-1885. | |
| Native Human Creatine Kinase MB Fraction | In the cells, the "cytosolic" CK enzymes consist of two subunits, which can be either B (brain type) or M (muscle type). There are, therefore, three different isoenzymes:CK-MM, CK-BB and CK-MB. The genes for these subunits are located on different chromosomes:B on 14q32 and M on 19q13. In addition to those three cytosolic CK isoforms, there are two mitochondrial creatine kinase isoenzymes, the ubiquitous and sarcomeric form. The functional entity of the latter two mitochondrial CK isoforms is an octamer consisting of four dimers each. Applications: The mb isoenzyme of creatine kinase (mbck) can be used as a diagnostic marker for acute myocardial infarction. Group: Enzymes. Synonyms: CK-MB; CKMB; Creatine Kinase MB Fraction; Creatine Kinase MB. Purity: > 70% (SDS-PAGE). Activity: > 1,000 U/mL. Form: liquid. Source: Human heart. Species: Human. CK-MB; CKMB; Creatine Kinase MB Fraction; Creatine Kinase MB. Cat No: NATE-0141. | |
| Native Human Creatine Kinase MB/MM Mix | Creatine kinase plays a key role in the energy metabolism of cells with intermittently high and fluctuating energy requirements. Examples of such cells include cardiac or skeletal muscle cells and neural tissues of brain and retina. The enzyme catalyzes the reversible transfer of the phosphoryl group from phosphorylcreatine to ADP, in order to generate ATP. The molecular mass of the protein is found to be approximately 80 kDa. It is made up of 2 subunits, each having a molecular weight of 40 kDa ± 2000. The lighter subunit is present in larger amounts. Applications: Diagnostic controls, calibrators & standards; immunoassays; clinical chemistry; testing/assay validation; life science; cardiac markers; manufacturing. Group: Enzymes. Synonyms: Creatine Kinase MB/MM Mix; CK-MB/MM; ATP:creatine phosphotransferase; Creatine Kinase; CK; CPK; MM-CK; MB-CK; creatine phosphokinase; creatine phosphot. CAS No. 9001-15-4. CK. Activity: > 500 U/mL. Stability: 2 years. Storage: Store at -20°C. Form: Glycerol solution. Source: Human Heart. Species: Human. Creatine Kinase MB/MM Mix; CK-MB/MM; ATP:creatine phosphotransferase; Creatine Kinase; CK; CPK; MM-CK; MB-CK; creatine phosphokinase; creatine phosphotransferase; phosphocreatine kinase; adenosine triphosphate-creatine transphosphorylase; Mi-CK; CK-MM; CK-MB; CKMiMi; MiMi-CK; 9001-15-4. Cat No: NATE-0957. | |
| Native Human Creatine Kinase mix | Creatine kinase plays a key role in the energy metabolism of cells with intermittently high and fluctuating energy requirements. Examples of such cells include cardiac or skeletal muscle cells and neural tissues of brain and retina. The enzyme catalyzes the reversible transfer of the phosphoryl group from phosphorylcreatine to ADP, in order to generate ATP.1 The molecular mass of the protein is found to be approximately 80 kDa Da. It is made up of 2 subunits, each having a molecular weight of 40 kDa ± 2000. The lighter subunit is present in larger amounts. Applications: Research life science elisa assay clinical chemistry. Group: Enzymes. Synonyms: EC 2.7.3.2; ATP:creatine phosphotransferase; CK; CPK; MM-CK; MB-CK; BB-CK; creatine phosphokinase; creatine phosphotransferase; phosphocreatine kinase; adenosine triphosphate-creatine transphosphorylase; Mi-CK; CK-BB; CK-MM; CK-MB; CKMiMi; MiMi-CK; 9001-15-4. Enzyme Commission Number: EC 2.7.3.2. CAS No. 9001-15-4. CK. Activity: >10%. Storage: -20°C. Source: Human Cardiac Tissue. Species: Human. EC 2.7.3.2; ATP:creatine phosphotransferase; CK; CPK; MM-CK; MB-CK; BB-CK; creatine phosphokinase; creatine phosphotransferase; phosphocreatine kinase; adenosine triphosphate-creatine transphosphorylase; Mi-CK; CK-BB; CK-MM; CK-MB; CKMiMi; MiMi-CK; 9001-15-4. Cat No: NATE-0137. | |
| Native Human Creatine Kinase MM | Human CK-MM isoenzyme also known as human CPK-3 isoenzyme is normally responsible for almost all human CPK enzyme activity in healthy people. When human (CK-MM) CKMM isoenzyme is elevated, this usually indicates injury or stress to skeletal muscle. Group: Enzymes. Synonyms: CKM; creatine kinase, muscle; CKMM; creatine kinase M-type; creatine kinase-M; creatine kinase M chain; CK-MM. Enzyme Commission Number: EC 2.7.3.2. CAS No. 9001-15-4. Purity: CK-MM: > 99% CK-MB: < 1%CK-BB: < 1%. CK. Activity:> 100 U/mg. Stability: 3 years. Appearance: White to off-white powder. Storage: Store at -20° C. Form: Lyophilized from tris chloride, EDTA and DTT, pH 7.5. Source: Human Skeletal Muscle. Species: Human. CKM; creatine kinase, muscle; CKMM; creatine kinase M-type; creatine kinase-M; creatine kinase M chain; CK-MM. Cat No: NATE-1883. | |
| Native Human Creatine Kinase MM Fraction | Creatine kinase, muscle also known as CKM is a creatine kinase that in humans is encoded by the CKM gene. In the figure to the right, the crystal structure of the muscle-type M-CK monomer is shown. In vivo, two such monomers arrange symmetrically to form the active MM-CK enzyme. In heart, in addition to the MM-CK homodimer, also the heterodimer MB-CK consisting of one muscle (M-CK) and one brain-type (B-CK) subunit is expressed. The latter may be an important serum marker for myocardial infarction, if released from damaged myocardial cells into the blood where it can be detected by clinical chemistry. Applications: May be used as a control or calibrator in monitoring myoc...stoperative cardiac medical therapy in emergency coronary artery bypass grafting for acute myocardial infarction. creatine kinase mm fraction from human heart has also been used in a study to investigate the circadian dependence of infarct size and left ventricular function after st slevation myocardial infarction. Group: Enzymes. Synonyms: CKM; creatine kinase, muscle; CKMM; creatine kinase M-type; creatine kinase-M; creatine kinase M chain; M-CK; MM-CK. Activity: > 200 U/mg. Form: lyophilized powder. Source: Human heart. Species: Human. CKM; creatine kinase, muscle; CKMM; creatine kinase M-type; creatine kinase-M; creatine kinase M chain; M-CK; MM-CK. Cat No: NATE-0142. | |
| Native Human Creatine Kinase Total | Creatine kinase plays a key role in the energy metabolism of cells with intermittently high and fluctuating energy requirements. Examples of such cells include cardiac or skeletal muscle cells and neural tissues of brain and retina. The enzyme catalyzes the reversible transfer of the phosphoryl group from phosphorylcreatine to ADP, in order to generate ATP. The molecular mass of the protein is found to be approximately 80 kDa. It is made up of 2 subunits, each having a molecular weight of 40 kDa ± 2000. The lighter subunit is present in larger amounts. Applications: Diagnostic controls, calibrators & standards; immunoassays; clinical chemistry; testing/assay validation; life science; elisa; blotting; cardiac markers; manufacturing. Group: Enzymes. Synonyms: EC 2.7.3.2; ATP:creatine phosphotransferase; CK; CPK; MM-CK; MB-CK; BB-CK; creatine phosphokinase; creatine phosphotransferase; ph. Enzyme Commission Number: EC 2.7.3.2. CAS No. 9001-15-4. CK. Activity: > 5 U/mg. Stability: 3 years. Storage: Store at -20°C. Form: Lyophilized. Source: Human Heart/Brain. Species: Human. EC 2.7.3.2; ATP:creatine phosphotransferase; CK; CPK; MM-CK; MB-CK; BB-CK; creatine phosphokinase; creatine phosphotransferase; phosphocreatine kinase; adenosine triphosphate-creatine transphosphorylase; Mi-CK; CK-BB; CK-MM; CK-MB; CKMiMi; MiMi-CK; 9001-15-4. Cat No: NATE-0961. | |
| Native Human Dipeptidyl Peptidase-4 | Native DPPIV is a ubiquitous type II transmembrane glycoprotein and a serine protease of the S9 prolyl-oligopeptidase family. In vivo, it is synthesized with a signal peptide, which functions as the membrane anchoring domain. There is an 88% sequence homology between the human and porcine kidney enzymes. Both exist as homodimers with a subunit molecular weight of ~30 kDa. The high mannose 100 kDa DPPIV precursor is processed in the Golgi to yield a 124 kDa heavily N-and O-linked mature glycoprotein. It is then sorted to the apical membrane through the concerted action of both N-and O-linked glycans and its association with lipid microdomains. The porcine enzyme contains 18....Store at -20°C. Form: Liquid. Source: Human Placenta. Species: Human. EC 3.4.14.5; 54249-88-6; DPPIV; DPP4; dipeptidyl aminopeptidase IV; Xaa-Pro-dipeptidyl-aminopeptidase; Gly-Pro naphthylamidase; postproline dipeptidyl aminopeptidase IV; lymphocyte antigen CD26; glycoprotein GP110; dipeptidyl peptidase IV; glycylproline aminopeptidase; glycylproline aminopeptidase; X-prolyl dipeptidyl aminopeptidase; pep X; leukocyte antigen CD26; glycylprolyl dipeptidylaminopeptidase; dipeptidyl-peptide hydrolase; glycylprolyl aminopeptidase; dipeptidyl-aminopeptidase IV; DPP IV/CD26; amino acyl-prolyl dipeptidyl aminopeptidase; T cell triggering molecule Tp103; X-PDAP. Cat No: NATE-0962. | |
| Native Human Elastase | Neutrophil elastase is a serine proteinase in the same family as chymotrypsin and has broad substrate specificity. Secreted by neutrophils and macrophages during inflammation, it destroys bacteria and host tissue. It also localizes to Neutrophil extracellular traps (NETs), via its high affinity for DNA, an unusual property for serine proteases. Leuk ocyte elastase is a 29 kda serine endoprotease of the proteinase s1 family. it exists as a single 238 amino acid-peptide chain with four disulfide bonds. it contains two or thee n-linked glycans of variable composition which account for its three major isoforms. Applications: Elastase from creative enzymes has been used to digest fibro...mal models. Group: Enzymes. Synonyms: ELANE; elastase; EC 3.4.21.37; leukocyte elastase; ELA2; elastase 2; neutrophil elaszym; serine elastase; lysosomal elastase; neutrophil elastase; polymorphonuclear leukocyte elastase; elaszym; granulocyte elastase. Enzyme Commission Number: EC 3.4.21.37. CAS No. 9004-6-2. ELA2. Mole weight: 29 kDa. Activity: > 50 units/mg protein (Bradford). Storage: -20°C. Form: Lyophilized from 0.05 M sodium acetate (pH 5.5) and 0.6 M NaCl. Source: Human leuk ocytes. Species: Human. ELANE; elastase; EC 3.4.21.37; leukocyte elastase; ELA2; elastase 2; neutrophil elaszym; serine elastase; lysosomal elastase; neutrophil elastase; polymorphonuclear leukocyte ela | |
| Native Human Eosinophil Peroxidase | Eosinophil peroxidase is an enzyme found within the eosinophil granulocytes, innate immune cells of humans and mammals. This oxidoreductase protein is encoded by the gene EPX, expressed within these myeloid cells. EPO shares many similarities with its orthologous peroxidases, myeloperoxidase (MPO), lactoperoxidase (LPO), and thyroid peroxidase (TPO). The protein is concentrated in secretory granules within eosinophils. Eosinophil peroxidase is a heme peroxidase, its activities including the oxidation of halide ions to bacteriocidal reactive oxygen species, the cationic disruption of bacterial cell walls, and the post-translational modification of protein amino acid residues....8% (SDS-PAGE). Peroxidase. Mole weight: 77 kda (~53 kDa mw heavy chain, ~13 kDa mw light chain). Activity: > 1,000 U/mL (Enzymatic). Appearance: Clear, green to brown liquid. Storage: 2-8°C. Form: Liquid. Source: Human Eosinophils. Species: Human. EPX; eosinophil peroxidase; EPO; EPP; EPX PEN; EPX-PEN; EC 1.11.1.7; 9003-99-0; 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. Cat No: NATE-0228. | |
| Native Human erythrocytes Acetylcholinesterase | Acetylcholinesterase, also known as AChE or acetylhydrolase, is a hydrolase that hydrolyzes the neurotransmitter acetylcholine. AChE is found at mainly neuromuscular junctions and cholinergic brain synapses, where its activity serves to terminate synaptic transmission. It belongs to carboxylesterase family of enzymes. It is the primary target of inhibition by organophosphorus compounds such as nerve agents and pesticides. The activity obtained using acetylcholine as substrate is 30-100 times that obtained with butyrylcholine, using acetylcholinesterase from electric eel. Applications: Acetylcholinesterase (ache) from creative enzymes has been used in the structure-activity study of phosphoramido acid esters as inhibitors of ache. Group: Enzymes. Synonyms: true cholinesterase; choline esterase I; cholines. Enzyme Commission Number: EC 3.1.1.7. CAS No. 9000-81-1. Acetylcholinesterase. Mole weight: ~80 kDa. Activity: > 500 units/mg protein (BCA). Storage: 2-8°C. Form: buffered aqueous solution. Solution in 20 mM HEPES, pH 8.0, containing 0.1% TRITON X-100. Source: Human erythrocytes. Species: Human. true cholinesterase; choline esterase I; cholinesterase; acetylthiocholinesterase; acetylcholine hydrolase; acetyl; β-methylcholinesterase; AcCholE; EC 3.1.1.7; 9000-81-1; Acetylcholinesterase; AChE; acetylhydrolase. Cat No: NATE-0019. | |
| Native Human Factor α-XIIa | Human Factor α-XIIa is a serine protease responsible for the activation of Factor XI to XIa in the contact activation system. Human Factor XII and prekallikrein are thought to be involved in a reciprocal activation mechanism in which Factor XIIa activates prekallikrein to kallikrein, which in turn converts Factor XII to XIIa. Factor XIIa activates Factor XI to XIa thereby triggering the Contact Factor cascade. ERL offers Factor α-XIIa which is activated by the autoactivation process with Dextran Sulfate and re-purified to remove the activator. The protein purity is determined by SDS-PAGE and activity is determined via clotting assay. Group: Enzymes. Synonyms: Human Factor Alpha-XIIa; Factor Alpha-XIIa; Factor α-XIIa. Factor α-XIIa. Mole weight: 80 kDa. Activity: 69.51 PEU/mg. Storage: < -60°C. Source: Human. Species: Human. Human Factor Alpha-XIIa; Factor Alpha-XIIa; Factor α-XIIa. Cat No: NATE-0882. | |
| Native Human Factor IXa β | Prepared from Human Factor IX by activation with Bovine Factor XIa. This Bovine Factor XIa is removed after activation. Complete activation is observed by SDS-PAGE. The Factor XIa activates Factor IX in a two-step reaction. In the first step, an internal Arg-Ala bond is cleaved, and in the second step, an Arg-Val bond is cleaved. The second cleavage leads to the liberation of an activation peptide from the NH2-terminal portion of the heavy chain to produce Factor IXa&beta. Group: Enzymes. Synonyms: Human Factor IXa Beta; Factor IXa Beta; Factor IXa. Factor IXa Beta. Mole weight: 45 kDa. Activity: 12500.00 PEU/mg. Storage: < -60°C. Source: Human. Species: Human. Human Factor IXa Beta; Factor IXa Beta; Factor IXa. Cat No: NATE-0883. | |
| Native Human Factor VIIa | Prepared from purified Human Factor VII using Human Factor XIIa. The Factor Xlla is removed using affinity chromatography. Purity is determined by SDS-PAGE. Human Factor VIIa reduces to 29,500 and 23,500 with the addition of 2-mercaptoethanol. Activity is determined via clotting assay. Factor Vlla, in the presence of calcium ions and Tissue factor, activates Factors IX and X to their enzymatically active forms, Factor IXa and Xa. Group: Enzymes. Synonyms: Human Factor VII; Factor VII. Factor VIIa. Mole weight: 50 kDa. Activity: 53833.00 PEU/mg. Storage: < -60°C. Source: Human. Species: Human. Human Factor VII; Factor VII. Cat No: NATE-0884. | |
| Native Human Factor Xa | Human Factor Xa is prepared from Human Factor X by activation with Russell's Viper Venom. This RVV-X is removed after activation. Complete activation is observed by SDS-PAGE. Factor Xa along with cofactor Va, phospholipids and calcium ions, (the prothrombinase complex) catalyzes the rapid conversion of prothrombin to thrombin. Group: Enzymes. Synonyms: Human Factor Xa; Factor Xa. Factor Xa. Mole weight: 46 kDa. Activity: 218.00 IU/mg. Storage: < -60°C. Source: Human. Species: Human. Human Factor Xa; Factor Xa. Cat No: NATE-0885. | |
| Native Human Factor XIa | Prepared from Human Factor XI using Human Factor Xlla. This Xlla was removed using a corn trypsin inhibitor column. Complete activation is observed by SDS-PAGE. Factor XI, through the contact factor pathway cascade, is activated to Factor XIa via Factor Xlla and High Molecular Weight Kininogen. During activation by Factor Xlla and HK, FXI undergoes proteolytic cleavage in which the Mr=80,000 chain reportedly is cleaved to a heavy and light chain with Mr of about 48,000 and 33,000. This Factor XIa is responsible for the activation of Factor IX to Factor IXa. Unlike other examples of activation of Vitamin K-dependent blood-clotting proteins, Factor XIa proteolysis of Factor IX does not require membrane surfaces. Group: Enzymes. Synonyms: Human Factor XIa; Factor XIa. Factor XIa. Mole weight: 160 kDa. Storage: < -60°C. Source: Human. Species: Human. Human Factor XIa; Factor XIa. Cat No: NATE-0886. | |
| Native Human Factor XIIIa | Human Factor XIII is cleaved with human alpha thrombin. The thrombin is subsequently removed via chromatography. The above protein was purified from Human plasma that was tested and found negative by FDA accepted methods fro Anti-HIV1/2, Anti-HTLV I & II, HBsAg, Anti-HCV, Syphilis, ABC ab, HIV-1 p24 Ag or HIV-1 RNA, HCV RNA and HBV RNA. Donors are screened for CJD (Creutzfeldt-Jakob Disease). Group: Enzymes. Synonyms: Human Factor XIIIa; Factor XIIIa. Factor XIIIa. Mole weight: 312 kDa. Activity: 1968.00 Loewy u/mg. Storage: -20°C. Source: Human. Species: Human. Human Factor XIIIa; Factor XIIIa. Cat No: NATE-0887. | |
| Native Human Gamma-Glutamyl Transferase | γ-glutamyl transferase is an enzyme that transfers gamma-glutamyl functional groups. It is found in many tissues, the most notable one being the liver, and has significance in medicine as a diagnostic marker. GGT catalyzes the transfer of the gamma-glutamyl moiety of glutathione to an acceptor that may be an amino acid, a peptide or water (forming glutamate). GGT plays a key role in the gamma-glutamyl cycle, a pathway for the synthesis and degradation of glutathione and drug and xenobiotic detoxification. Other lines of evidence indicate that GGT can also exert a prooxidant role, with regulatory effects at various levels in cellular signal transduction and cellular pathophysiology. Applications: Research life science elisa assay clinical chemistry. Group: Enzymes. Synonyms: EC 2.3.2.2; glutamyl tr. Enzyme Commission Number: EC 2.3.2.2. CAS No. 9046-27-9. γ-GT. Activity: >50 U/mg. Storage: 4°C. Source: Human Liver. Species: Human. EC 2.3.2.2; glutamyl transpeptidase; α-glutamyl transpeptidase; γ-glutamyl peptidyltransferase; γ-glutamyl transpeptidase (ambiguous); γ-GPT; γ-GT; γ-GTP; L-γ-glutamyl transpeptidase; L-γ-glutamyltransferase; L-glutamyltransferase; GGT (ambiguous); γ-glutamyltranspeptidase (ambiguous); γ-glutamyltransferase; 9046-27-9; GGTP. Cat No: NATE-0792. | |
| Native Human Glutathione Peroxidase | Glutathione peroxidase is an enzyme which reduced lipid hydroperoxides into their corresponding alcohols. It also reduces free hydrogen peroxide in to water. In vivo it is responsible for protecting hemoglobin from oxidative breakdown. At the reported ph optimum of 8.8, we have found the activity to be approx. 10 times that at ph 7.0. however, to remain consistent with literature and avoid complications arising from non-enzymatic oxidation of gsh, our unit is defined at ph 7.0. Group: Enzymes. Synonyms: EC 1.11.1.9; GSH peroxidase; selenium-glutathione peroxidase; reduced glutathione peroxidase; 9013-66-5; GSH-Px, Glutathione:hydrogen-peroxide oxido-reductase; Glutathione Peroxidase. Enzyme Commission Number: EC 1.11.1.9. CAS No. 9013-66-5. GSH-Px. Activity: > 30 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing 25% sucrose, 3% dithiothreitol, and sodium phosphate buffer salts. Source: Human erythr ocytes. Species: Human. EC 1.11.1.9; GSH peroxidase; selenium-glutathione peroxidase; reduced glutathione peroxidase; 9013-66-5; GSH-Px, Glutathione:hydrogen-peroxide oxido-reductase; Glutathione Peroxidase. Cat No: NATE-0323. | |
| Native Human Glutathione S-Transferase | Glutathione S-transferases are a family of proteins that catalyze the conjugation of reduced glutathione with a variety of hydrophobic chemicals containing electrophilic centers. Group: Enzymes. Synonyms: EC 2.5.1.18; glutathione S-transferase; glutathione S-alkyltransferase; glutathione S-aryltransferase; S-(hydroxyalkyl)glutathione lyase; glutathione S-aralkyltransferase; glutathione S-alkyl transferase; GST; 50812-37-8. Enzyme Commission Number: EC 2.5.1.18. CAS No. 50812-37-8. Glutathione S-Transferase. Activity: 25-125 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing Tris buffer salts, reduced glutathione and EDTA. Source: Human placenta. Species: Human. EC 2.5.1.18; glutathione S-transferase; glutathione S-alkyltransferase; glutathione S-aryltransferase; S-(hydroxyalkyl)glutathione lyase; glutathione S-aralkyltransferase; glutathione S-alkyl transferase; GST; 50812-37-8. Cat No: NATE-0326. | |
| Native Human Glyceraldehyde-3-phosphate Dehydrogenase | Glyceraldehyde-3-phosphate dehydrogenase catalyzes the conversion of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate as part of glycolysis. It has also been shown to have roles in initiation of apoptosis, transcription activation and the shuttling of ER to Golgi vesicles. Group: Enzymes. Synonyms: EC 1.2.1.12; GAPDH; glyceraldehyde-3-phosphate dehydrogenase (phosphorylating); triosephosphate dehydrogenase; dehydrogenase, glyceraldehyde phosphate; phosphoglyceraldehyde dehydrogenase; 3-phosphoglyceraldehyde dehydrogenase; NAD+-dependent glyceraldehyde phosphate dehydrogenase; glyceralde. Enzyme Commission Number: EC 1.2.1.12. CAS No. 9001-50-7. Glyceraldehyde-3-phosphate Dehydrogenase. Activity: 50-150 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing sodium Citrate buffer salts. Source: Human erythrocytes. Species: Human. EC 1.2.1.12; GAPDH; glyceraldehyde-3-phosphate dehydrogenase (phosphorylating); triosephosphate dehydrogenase; dehydrogenase, glyceraldehyde phosphate; phosphoglyceraldehyde dehydrogenase; 3-phosphoglyceraldehyde dehydrogenase; NAD+-dependent glyceraldehyde phosphate dehydrogenase; glyceraldehyde phosphate dehydrogenase (NAD+); glyceraldehyde-3-phosphate dehydrogenase (NAD+); NADH-glyceraldehyde phosphate dehydrogenase; glyceraldehyde-3-P-dehydrogenase; 9001-50-7. Cat No: NATE-0280. | |
| Native Human Kallikrein | Plasma kallikrein is an enzyme. This enzyme catalyses the following chemical reaction:Selective cleavage of some Arg-and Lys-bonds, including Lys-Arg and Arg-Ser in (human) kininogen to release bradykinin. This enzyme is formed from plasma prokallikrein (Fletcher factor) by factor XIIa. Group: Enzymes. Synonyms: serum kallikrein; kininogenin; kallikrein I; kallikrein II; kininogenase; kallikrein; callicrein; glumorin; padreatin; padutin; kallidinogenase; bradykininogenase; panceatic kallikrein; onokrein P; dilminal D; depot-Padutin; urokallikrein; urinary kallikrein; 9001-01-8; EC 3.4.21.34; plasma kallikrein. Enzyme Commission Number: EC 3.4.21.34. CAS No. 9001-1-8. Kallikrein. Activity: Type I, > 5 units/mg protein; Type II, 1-5 units/mg protein. Storage: -20°C. Form: Type I, buffered aqueous solution, Solution in 20 mM Tris-HCl, pH 7.8 with 100 mM NaCl; Type II, lyophilized powder. Source: Human plasma. Species: Human. serum kallikrein; kininogenin; kallikrein I; kallikrein II; kininogenase; kallikrein; callicrein; glumorin; padreatin; padutin; kallidinogenase; bradykininogenase; panceatic kallikrein; onokrein P; dilminal D; depot-Padutin; urokallikrein; urinary kallikrein; 9001-01-8; EC 3.4.21.34; plasma kallikrein. Cat No: NATE-0361. | |
| Native Human Lactate Dehydrogenase | 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-0380. | |
| Native Human Lactate Dehydrogenase 1 | 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-0384. | |
| 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 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. | |
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