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| Product | Description | |
|---|---|---|
| 10-[3-(2,2-Diimethyl-1,3-dioxolan-4-yl)-2,3-dihydroxypropyl]-7,8-dimethyl-isoalloxazine | 10-[3-(2,2-Diimethyl-1,3-dioxolan-4-yl)-2,3-dihydroxypropyl]-7,8-dimethyl-isoalloxazine is an intermediate uin the synthesis of Riboflavin 4',5'-Diphosphate which is a diphosphate derivative of Riboflavin (R414995); a nutritional factor found in milk, eggs, malted barley, liver, kidney, heart, and leafy vegetables. Richest natural source is yeast. Minute amounts present in all plant and animal cells. Vitamin (enzyme cofactor). Group: Biochemicals. Grades: Highly Purified. CAS No. 22854-81-5. Pack Sizes: 2.5mg, 5mg. Molecular Formula: C20H24N4O6. US Biological Life Sciences. |  Worldwide |
| 10- ( ( (4R, 5R, 6S) -6- ( ( (tert-Butyldiphenylsilyl) oxy) methyl) -5-hydroxy-2, 2-dimethyl-1, 3-dioxan-4-yl) methyl) -7, 8-dimethylbenzo [g]pteridine-2, 4 (3H, 10H) -dione | 10- ( ( (4R, 5R, 6S) -6- ( ( (Tert-butyldiphenylsilyl) oxy) methyl) -5-hydroxy-2, 2-dimethyl-1, 3-dioxan-4-yl) methyl) -7, 8-dimethylbenzo [g]pteridine-2, 4 (3H, 10H) -dioneis an intermediate uin the synthesis of Riboflavin 4',5'-Diphosphate which is a diphosphate derivative of Riboflavin (R414995); a nutritional factor found in milk, eggs, malted barley, liver, kidney, heart, and leafy vegetables. Richest natural source is yeast. Minute amounts present in all plant and animal cells. Vitamin (enzyme cofactor). Group: Biochemicals. Grades: Highly Purified. Pack Sizes: 5mg, 10mg. Molecular Formula: C36H42N4O6Si, Molecular Weight: 654.83. US Biological Life Sciences. | Worldwide |
| 1-Deoxy-1-[ (3-hydroxymethyl-4-methyl-6- (2-phenyldiazenyl) phenyl) amino]-D-ribitol | 1-Deoxy-1-[ (3-hydroxymethyl-4-methyl-6- (2-phenyldiazenyl) phenyl) amino]-D-ribitol is an intermediate in the synthesis of 8-Hydroxymethyl Riboflavin which is an impurity of Riboflavin (R414995), a nutritional factor found in milk, eggs, malted barley, liver, kidney, heart, leafy vegetables. Richest natural source is yeast. Minute amounts present in all plant and animal cells. Vitamin (enzyme cofactor). Group: Biochemicals. Grades: Highly Purified. Pack Sizes: 5mg, 10mg. Molecular Formula: C19H25N3O5. US Biological Life Sciences. | Worldwide |
| 1-Deoxy-1-[(3-hydroxymethyl-4-methylphenyl)amino]-D-ribitol | 1-Deoxy-1-[(3-hydroxymethyl-4-methylphenyl)amino]-D-ribitol is an intermediate in the synthesis of 8-Hydroxymethyl Riboflavin which is an impurity of Riboflavin (R414995), a nutritional factor found in milk, eggs, malted barley, liver, kidney, heart, leafy vegetables. Richest natural source is yeast. Minute amounts present in all plant and animal cells. Vitamin (enzyme cofactor). Group: Biochemicals. Grades: Highly Purified. Pack Sizes: 10mg, 25mg. Molecular Formula: C13H21NO5. US Biological Life Sciences. | Worldwide |
| 25-Hydroxy Vitamin D3 3,3-Aminopropyl Ether | Vitamin D3 analog. Calcifediol (INN), also known as calcidiol, 25-hydroxycholecalcifero l, or 25-hydroxyvitamin D (abbreviated 25(OH)D),[1] is a prehormone that is produced in the liver by hydroxylation of vitamin D3(cholecalciferol) by the enzyme cholecalciferol 25-hydroxylase which was isolated by Michael F. Holick. Physicians worldwide measure this metabolite to determine a patient's vitamin D status.[2] At a typical daily intake of vitamin D3, its full conversion to calcifediol takes approximately 7 days.[3] Calcifediol is then converted in the kidneys (by the enzyme 25(OH)D-1α-hydroxylase) into calcitriol (1,25-(OH)2D3), a secosteroid hormone that is the active form of vitamin D. It can also be converted into 24-hydroxycalcidiol in the kidneys via 24-hydroxylation.[4][5]. Group: Biochemicals. Alternative Names: ( ε R, 1R, 3aS, 4E, 7aR) -4- [ (2Z) -2- [ (5S) -5- (3-Aminopropoxy) -2- methyl enecyclohexylidene] ethylidene] octahydro- α , α , ε , 7a-tetra methyl -1H-indene-1-pentanol; (3 β,5Z,7E)-3-(3-Aminopropoxy)-9,10-secocholesta-5,7,10(19)-trien-25-ol; 3-O-(2-Aminoethyl)-25-hydroxyvitamin D3. Grades: Highly Purified. CAS No. 163018-26-6. Pack Sizes: 2.5mg. US Biological Life Sciences. | Worldwide |
| 25-Hydroxy Vitamin D3 3-Sulfate Sodium Salt | 25-Hydroxyvitamin D3 3-Sulfate is a metabolite of 24,25-Dihydroxyvitamin D3 and 25-Hydroxyvitamin D3. Calcifediol (INN), also known as calcidiol, 25-hydroxycholecalcifero l, or 25-hydroxyvitamin D (abbreviated 25(OH)D),is a prehormone that is produced in the liver by hydroxylation of vitamin D3(cholecalciferol) by the enzyme cholecalciferol 25-hydroxylase which was isolated by Michael F. Holick. Physicians worldwide measure this metabolite to determine a patient's vitamin D status.At a typical daily intake of vitamin D3, its full conversion to calcifediol takes approximately 7 days. Calcifediol is then converted in the kidneys (by the enzyme 25(OH)D-1α-hydroxylase) into calcitriol (1,25-(OH)2D3), a secosteroid hormone that is the active form of vitamin D. It can also be converted into 24-hydroxycalcidiol in the kidneys via 24-hydroxylation. Group: Biochemicals. Alternative Names: (3 β,5Z,7E)-9,10-Secocholesta-5,7,10(19)-triene-3,25-diol 3-(Hydrogen Sulfate) Sodium Salt; 25-Hydroxyvitamin D3 3-Sulfate Sodium Salt; 25-Hydroxyvitamin D3 3 β-Sulfate Sodium Salt; Calcifediol 3-Sulfate Sodium Salt. Grades: Purified. Pack Sizes: 2.5mg. Molecular Formula: C??H??NaO?S, Molecular Weight: 502.68. US Biological Life Sciences. | Worldwide |
| 3-epi-25-Hydroxy Vitamin D3 | The epimer metabolite of Calcifediol or 25-hydroxyvitamin D3. Calcifediol (INN), also known as calcidiol, 25-hydroxycholecalcifero l, or 25-hydroxyvitamin D (abbreviated 25(OH)D),[1] is a prehormone that is produced in the liver by hydroxylation of vitamin D3(cholecalciferol) by the enzyme cholecalciferol 25-hydroxylase which was isolated by Michael F. Holick. Physicians worldwide measure this metabolite to determine a patient's vitamin D status.[2] At a typical daily intake of vitamin D3, its full conversion to calcifediol takes approximately 7 days.[3] Calcifediol is then converted in the kidneys (by the enzyme 25(OH)D-1α-hydroxylase) into calcitriol (1,25-(OH)2D3), a secosteroid hormone that is the active form of vitamin D. It can also be converted into 24-hydroxycalcidiol in the kidneys via 24-hydroxylation.[4][5]. Group: Biochemicals. Alternative Names: ( ε R, 1R, 3aS, 4E, 7aR) -Octahydro-4- [ (2Z) -2- [ (5R) -5-hydroxy-2- methyl enecyclohexylidene] ethylidene] - α , α , ε , 7a-tetra methyl -H-indene-1-pentanol; (3α,5Z,7E)-9,10-Seco-cholesta-5,7,10(19)-triene-3,25-diol; 3-epi-25-Hydroxyvitamin D3. Grades: Highly Purified. CAS No. 73809-05-9. Pack Sizes: 250ug. US Biological Life Sciences. | Worldwide |
| 4-Bromo-3-hydroxybenzoic acid | 4-Bromo-3-hydroxybenzoic acid is a metabolite of Brocresine and a histidine decarboxylase (HDC) inhibitor with IC 50 s of 1 mM for both rat fetal and rat gastric HDC. 4-Bromo-3-hydroxybenzoic acid also inhibits aromatic-L-amino acid decarboxylase from hog kidney and rat gastric mucosa in vitro with IC 50 s of 1 mM for both enzymes [1] [2]. Uses: Scientific research. Group: Natural products. CAS No. 14348-38-0. Pack Sizes: 10 mM * 1 mL; 100 mg; 500 mg. Product ID: HY-W003445. |  |
| Aldolase A from Human, Recombinant | Fructose bisphosphate aldolase A, also known as Aldolase A is a glycolytic enzyme that catalyzes the reversible conversion of fructose-1,6-bisphosphate to glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. It is found in the developing embryo and is produced in even greater amounts in adult muscle. Aldolase A expression is repressed in adult liver, kidney and intestine and similar to aldolase C levels in brain and other nervous tissue. Deficiency has been associated with myopathy and hemolytic anemia. Recombinant human Aldolase A, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. Group: Enzymes. Synonyms: Fructose bisphosphate Aldolase A; ALDOA; ALDA; GSD12. Enzyme Commission Number: EC 4.1.2.13. Purity: > 95% by SDS-PAGE. Aldolase. Mole weight: 41.5 kDa (384 aa, 1-364 aa + His Tag), confirmed by MALDI-TOF. Activity: > 1.5 units/mg. Storage: Can be stored at 4°C short term (1-2 weeks). For long term storage, aliquot and store at -20°C or -70°C. Avoid repeated freezing and thawing cycles. Form: Liquid. Source: E. coli. Species: Human. Fructose bisphosphate Aldolase A; ALDOA; ALDA; GSD12; Aldolase A; Aldolase. Cat No: NATE-1663. |  |
| Amrinone | Amrinone is a selective cAMP phosphodiesterase (PDE-3) inhibitor with positive inotropic and vasodilatory activity. It is a simple, non-glycoside cardiotonic agent. It provides protection against ischemia-reperfusion injury in kidney, liver, and heart. It has the ability to stimulate calcium ion influx into the cardiac cell. It is used in the treatment of congestive heart failure. It increases cardiac contractility as a vasodilator. It acts by inhibiting the breakdown of both cAMP and cGMP by the phosphodiesterase (PDE3) enzyme. It is a drug that may improve the prognosis in patients with congestive heart failure. It has been shown to increase the contractions initiated in the heart by high gain calcium induced calcium release (CICR). It was developed by Sanofi and has been listed. Uses: Amrinone is a simple, non-glycoside cardiotonic agent. it provides protection against ischemia-reperfusion injury in kidney, liver, and heart. it is used in the treatment of congestive heart failure. it increases cardiac contractility as a vasodilator. Synonyms: Inamrinone; Wincoram; Inocor; Cordemcura; Win-40680; Win40680; 3-Amino-5-pyridin-4-yl-1H-pyridin-2-one. Grades: 98%. CAS No. 60719-84-8. Molecular formula: C10H9N3O. Mole weight: 187.20. |  |
| Angiotensin I (human, rat, mouse) trifluoroacetate salt | Angiotensin I is formed from angiotensinogen by the action of renin, which is released from the kidney juxtaglomerular cells. Angiotensin I is further cleaved to angiotensin II by angiotensin converting enzyme. Angiotensin is a protein hormone that causes blood vessels to become narrower. It helps to maintain blood pressure and fluid balance in the body. It binds to angiotensin receptors in human myometrium membrane preparations with Kd of 11.2 nM and increases renal vascular resistance in isolated rat kidney with EC50 of 10.5 nM. Grades: ≥95%. Molecular formula: C62H89N17O14·xCF3COOH. Mole weight: 1296.48. | |
| Aspartate Transaminase (Crude Enzyme) | (AST) or aspartate aminotransferase, also known as AspAT/ASAT/AAT or serum glutamic oxaloacetic transaminase(SGOT), is a pyridoxal phosphate (PLP)-dependent transaminase enzyme (EC 2. 6. 1. 1) that was first described by Arthur Karmen and colleagues in 1954. AST catalyzes the reversible transfer of an α-amino group between aspartate and glutamate and, as such, is an important enzyme in amino acid metabolism. AST is found in the liver, heart, skeletal muscle, kidneys, brain, and red blood cells. Serum AST level, serum ALT (alanine transaminase) level, and their ratio (AST/ALT ratio) are commonly measured clinically as biomarkers for liver health. The tests are part of blood panels. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Synthesis; medicine; biotechnology. Group: Enzymes. Synonyms: glutamic-oxaloacetic transaminase; glutamic-aspartic transaminase; transaminase A; AAT; AspT; 2-oxoglutarate-glutamate aminotransferase; aspartate α-ketoglutarate transaminase; aspartate aminotransferase; aspartate-2-oxoglutarate transaminase; aspartic a. Enzyme Commission Number: EC 2.6.1.1. CAS No. 9000-97-9. AST. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. glutamic-oxaloacetic transamina | |
| Atto 590 nhs ester | ATTO 590 is a novel fluorescent label belonging to the class of Rhodamine dyes. The dye is designed for application in the area of life science, e.g. labeling of DNA, RNA or proteins. The ATTO dyes are a series of fluorescent dyes that provide all the crucial properties required for modern fluorescent technologies, such as fluorescence microscopy, flow-cytometry, fluorescence in situ hybridization (FISH), receptor binding assays or enzyme assays. The dye is highly suitable for single-molecule detection applications and high-resolution microscopy. The NHS-esters are used in common conjugation protocols.ATTO 590 is a novel fluorescent label belonging to the class of Rhodamine dyes, which has an absorption maximum of 594 nm and an emission maximum of 624 nm. ATTO 590-N-hydroxysuccinimide (NHS) is membrane permeable. Uses: Molar absorption 120,000 1/m cm, abs: 593 nm, em: 620 nm, qy=0.93, tfl 4.0 ns (unpublished data)atto 590 nhs ester may be suitable for use in site-specific labeling of human embryonic kidney (hek293t) cell lysates for western blotting, fluorescence, and widefield microscopy studies. Synonyms: 2-(6, 20-diethyl-7, 7, 9, 17, 19, 19-hexamethyl-2-oxa-20-aza-6-azoniapentacyclo[12.8.0.03, 12.05, 10.016, 21; docosa-1(14),3,5,8,10,12,15,17,21-nonaen-13-yl)-4-(2,5-dioxopyrrolidin-1-yl)oxycarbonylbenzoic acid;perchlorate; 6-(2-Carboxy-5-{[(2,5-dioxopyrrolidin-1-yl)oxy]carbonyl}phenyl)-1,11-diethyl-2,2,4,8,10,10-hexamethyl-10,11-dihydro-2H-pyrano[3,2-g:5,6-g']diquinolin-1-ium perchlorate. Grades: ≥60% (coupling to amines). CAS No. 670269-33-7. Molecular formula: C41H42ClN3O11. Mole weight: 788.24. | |
| Bovine Superoxide dismutase-polyethylene glycol | Superoxide dismutases (SOD) are enzymes that alternately catalyze the dismutation (or partitioning) of the superoxide (O2-) radical into either ordinary molecular oxygen (O2) or hydrogen peroxide (H2O2). Superoxide is produced as a by-product of oxygen metabolism and, if not regulated, causes many types of cell damage. Hydrogen peroxide is also damaging, but less so, and is degraded by other enzymes such as catalase. Thus, SOD is an important antioxidant defense in nearly all living cells exposed to oxygen. One exception is Lactobacillus plantarum and related lactobacilli, which use a different mechanism to prevent damage from reactive (O2-). Group: Enzymes. Synonyms: PEG-SOD; Superoxide dismutase-polyethylene glycol; SOD-PEG. SOD. Activity: 11,000 units/mg SOD before conjugation; SOD/PEG ratio: 10-20 PEG with each SOD enzyme. Appearance: Off-white. Storage: Store at -20°C. Form: Lyophilized powder. Source: Bovine Kidney. Species: Bovine. PEG-SOD; Superoxide dismutase-polyethylene glycol; SOD-PEG. Cat No: NATE-0682. | |
| Calcifediol monohydrate | Calcifediol monohydrate is a prehormone that is produced in the liver by hydroxylation of vitamin D3 (cholecalciferol) by the enzyme cholecalciferol 25-hydroxylase. It can be converted into 24-hydroxycalcidiol in the kidneys via 24-hydroxylation. Uses: Bone density conservation agents. Synonyms: 25-hydroxy Vitamin D3 monohydrate. Grades: >98%. CAS No. 63283-36-3. Molecular formula: C27H46O3. Mole weight: 418.65. | |
| Camostat Mesylate | Camostat (INN) or FOY-305 is a serine protease inhibitor. Serine protease enzymes have a variety of functions in the body, and so camostat has a diverse range of uses. It is used in the treatment of some forms of cancer and is also effective against some viral infections, as well as inhibiting fibrosis in liver or kidney disease orpancreatitis. Uses: Trypsin inhibitors. Synonyms: 4-(2-(2-(dimethylamino)-2-oxoethoxy)-2-oxoethyl)phenyl 4-guanidinobenzoate methanesulfonate; Camostat Mesilate; Camostat Mesylate; FOY 305; FOY-305; FOY305. Grades: >98%. CAS No. 59721-29-8. Molecular formula: C20H22N4O5.CH4O3S. Mole weight: 494.52. | |
| CAY10462 | 20-HETE is an important metabolite of arachidonic acid in the vasculature, especially in the kidney, where it is synthesized by cytochrome P450 (CYP450) enzymes of the 4A family. CAY10462 is the hydrochloride salt form of CAY10434. It is a selective inhibitor of the 20-HETE synthase CYP4A11, which exhibits an IC50 of 8.8 nM when tested in human renal microsomes. Synonyms: CAY 10462; CAY-10462. Grades: ≥98%. CAS No. 502656-68-0. Molecular formula: C17H25N3O·2HCl. Mole weight: 360.3. | |
| Cholesterol Esterase from Candida Rugosa | Cholesterol esterase (CE) is also known as cholesterol ester hydrolase. This enzyme catalyzes the following reaction: Sterol Ester --------> Sterol + Fatty Acid. Cholesterol esterase activity has been demonstrated in pancreas, intestine, liver and kidney. The enzyme is inactivated by proteolytic enzymes but stabilized by proteolytic enzyme inhibitors and by bile salts. Group: Enzymes. Synonyms: cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; sterol esterase; CE. Enzyme Commission Number: EC 3.1.1.13. CAS No. 9026-00-0. Purity: 0.9. Activity: 25-100 U/mg. Storage: Store at -20° C. Form: Freeze dried powder. Source: Candida Rugosa. cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; sterol esterase; CE. Cat No: NATE-1679. | |
| Cholesterol Esterase from Microorganism | Cholesterol esterase (CE) is also known as cholesterol ester hydrolase. This enzyme catalyzes the following reaction: Sterol Ester --------> Sterol + Fatty Acid. Cholesterol esterase activity has been demonstrated in pancreas, intestine, liver and kidney. The enzyme is inactivated by proteolytic enzymes but stabilized by proteolytic enzyme inhibitors and by bile salts. Group: Enzymes. Synonyms: cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; EC 3.1.1.13; Sterol esterase. Enzyme Commission Number: EC 3.1.1.13. CAS No. 9026-00-0. Activity: 5.0U/mg-solid or more. Form: Freeze dried powder. Source: Microorganism. cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; EC 3.1.1.13; Sterol esterase. Cat No: DIA-135. | |
| Cholesterol Esterase from Pseudomonas sp. | Cholesterol esterase (CE) is also known as cholesterol ester hydrolase. This enzyme catalyzes the following reaction: Sterol Ester --------> Sterol + Fatty Acid. Cholesterol esterase activity has been demonstrated in pancreas, intestine, liver and kidney. The enzyme is inactivated by proteolytic enzymes but stabilized by proteolytic enzyme inhibitors and by bile salts. Group: Enzymes. Synonyms: cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; EC 3.1.1.13; Sterol esterase. Enzyme Commission Number: EC 3.1.1.13. CAS No. 9026-00-0. Activity: 100U/mg-solid or more (containing approx. 40% of stabilizers). Form: Freeze dried powder. Source: Pseudomonas sp. cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; EC 3.1.1.13; Sterol esterase. Cat No: DIA-134. | |
| Cholesterol Esterase from Schizophyllum commune | Cholesterol esterase (CE) is also known as cholesterol ester hydrolase. This enzyme catalyzes the following reaction: Sterol Ester --------> Sterol + Fatty Acid. Cholesterol esterase activity has been demonstrated in pancreas, intestine, liver and kidney. The enzyme is inactivated by proteolytic enzymes but stabilized by proteolytic enzyme inhibitors and by bile salts. Group: Enzymes. Synonyms: cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; EC 3.1.1.13; Sterol esterase. Enzyme Commission Number: EC 3.1.1.13. CAS No. 9026-00-0. Activity: 2.0 U/mg-solid or more (containing approx. 20% of stabilizers). Form: Freeze dried powder. Source: Schizophyllum commune. cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; EC 3.1.1.13; Sterol esterase. Cat No: DIA-133. | |
| Cilastatin Ammonium Salt | Cilastatin Ammonium Salt is the ammonium salt of Cilastatin, which is a dipeptidase inhibitor of renal enzyme dehydropeptidase-I and leukotriene D4 peptidase. It inhibits metabolism of LTD4 to LTE4 and the hydrolysis of β-lactam antibiotics. It reduces toxic accumulation of cyclosporin A in kidney proximal tubule epithelial cells. It can be combined intravenously with imipenem in order to protect it from dehydropeptidase. It suppresses both host and target metabolism of the broad-spectrum antibiotic imipenem, improving its efficacy. It usually confers antibiotic resistance to certain bacteria because itself does not have antibiotic activity. It has nephroprotective effects. Synonyms: (2Z)-7-[[(2R)-2-amino-2-carboxyethyl]thio]-2-[[[(1S)-2,2-dimethylcyclopropyl]carbonyl]amino]-2-heptenoic Acid Ammonium Salt; MK-791 Ammonium Salt. Grades: > 95%. CAS No. 877674-82-3. Molecular formula: C16H29N3O5S. Mole weight: 375.48. | |
| Cilastatin sodium | Cilastatin sodium is the sodium salt of cilastatin, which is a dipeptidase inhibitor of renal enzyme dehydropeptidase-I and leukotriene D4 peptidase. It inhibits metabolism of LTD4 to LTE4 and the hydrolysis of β-lactam antibiotics. It reduces toxic accumulation of cyclosporin A in kidney proximal tubule epithelial cells. It can be combined intravenously with imipenem in order to protect it from dehydropeptidase. It suppresses both host and target metabolism of the broad-spectrum antibiotic imipenem, improving its efficacy. It usually confers antibiotic resistance to certain bacteria because itself does not have antibiotic activity. It has nephroprotective effects. Synonyms: L 642957; MK 791; L642957; MK791; L-642957; MK-791; [R-[R*,S*-(Z)]]-7-[(2-Amino-2-carboxyethyl)thio]-2-[[(2,2-dimethylcyclopropyl)carbonyl]amino]-2-heptenoic Acid Monosodium Salt; (2Z) ?-7- [ [ (2R) ?-2-Amino-2-carboxyethyl] ?thio] ?-2- [ [ [ (1S) ?-2, ?2-dimethylcyclopropyl] ?carbonyl] ?amino] ?-2-heptenoic Acid Sodium Salt; sodium S-((Z)-6-carboxy-6-((S)-2,2-dimethylcyclopropane-1-carboxamido)hex-5-en-1-yl)-L-cysteinate. Grades: ≥99% by HPLC. CAS No. 81129-83-1. Molecular formula: C16H25N2NaO5S. Mole weight: 380.43. | |
| Creatine monohydrate | Creatine is a nitrogenous compound that acts as a high-energy reservoir for the rapid regeneration of ATP. Approximately 95% of creatine is found in skeletal muscle, primarily as phosphocreatine. Creatine can be acquired through dietary consumption or formed from L-arginine, glycine, and L-methionine in a multi-step reaction that occurs in the kidneys and liver. Creatine is then transported to muscle tissue. Creatine is also being investigated as a treatment of neuromuscular diseases, where it may aid in neuroprotection and by improving the cellular bioenergetic state. Applications: Involved with rapid atp production primarily in skeletal muscle tissue via the action of creatine kinase(s). Group: Coenzymes. Synonyms: N-Amidinosarcosine monohydrate. CAS No. 6020-87-7. Mole weight: 149.15. Form: Solid. N-Amidinosarcosine monohydrate; Creatine monohydrate; 6020-87-7. Cat No: COEC-096. | |
| Cyclosporin | It is produced by the strain of Polypocladiurn inflatum. It has a strong immunosuppressive action, but also has anti-inflammatory and weak antifungal effects. The mechanism of immunosuppression is the combination of cyclosporin A and cyclosporin-binding protein in T cells, which inhibits the activity of Calcineurin, and then impedes the transposition of intracellular transcription factors into the nucleus, and inhibits the interleukin-2 transcription, resulting in immunosuppression. It is mainly used for kidney transplantation, bone marrow and heart transplantation, and is one of the most important immunosuppressive agents in clinical application. Uses: Enzyme inhibitors. Synonyms: Restasis; Cyclosporine; Gengraf; Sandimmune; SangCyA; Atopica. Grades: >98%. CAS No. 79217-60-0. Molecular formula: C62H111N11O12. Mole weight: 1202.61. | |
| D-2-hydroxyacid dehydrogenase (quinone) | The enzyme from mammalian kidney contains one mole of FAD per mole of enzyme.(R)-lactate, (R)-malate and meso-tartrate are good substrates. Ubiquinone-1 and the dye 2,6-dichloroindophenol can act as acceptors; NAD+ and NADP+ are not acceptors. Group: Enzymes. Synonyms: (R)-2-hydroxy acid dehydrogenase; (R)-2-hydroxy-acid:(acceptor) 2-oxidoreductase; D-lactate dehydrogenase (ambiguous). Enzyme Commission Number: EC 1.1.5.10. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0428; D-2-hydroxyacid dehydrogenase (quinone); EC 1.1.5.10; (R)-2-hydroxy acid dehydrogenase; (R)-2-hydroxy-acid:(acceptor) 2-oxidoreductase; D-lactate dehydrogenase (ambiguous). Cat No: EXWM-0428. | |
| D-amino acid oxidase from Human, Recombinant | D-amino-acid oxidase (DAAO) is a peroxisomal enzyme which uses flavin adenine dinucleotide (FAD) as a cofactor and oxidizes D-amino acids to the corresponding imino acids, producing ammonia and hydrogen peroxide. Its substrates include a wide variety of D-amino acids, but it is inactive on the naturally occurring L-amino acids. It has been suggested that it is involved in acid base balance in the kidney or it could act as a detoxifying agent which removes D-amino acids accumulated during aging. Recombinant human daao protein, fused to his-tag at n-terminus, was expressed in e.coli and purified by using conventional chromatography. Group: Enzymes. Synonyms: DAAO; DAO; OXDA; DAMOX; D-Amino Acid Oxidase; EC 1.4.3.3; 9000-88-8; ophio-amino-acid oxidase; L-amino acid:O2 oxidoreductase. Enzyme Commission Number: EC 1.4.3.3. Purity: > 90% by SDS-PAGE. DAAO. Mole weight: 41.6 kDa. Activity: > 3.5 units/mg. Storage: Store at +4°C for short term (1-2 weeks). For long term storage, aliquot and store at -70°C. Avoid repeated freeze/thaw cycles. Form: Liquid. Source: E. coli. Species: Human. DAAO; DAO; OXDA; DAMOX; D-Amino Acid Oxidase; EC 1.4.3.3; 9000-88-8; ophio-amino-acid oxidase; L-amino acid:O2 oxidoreductase. Cat No: NATE-1653. | |
| DDMS | DDMS is a mechanism-based irreversible inhibitor with a 10-fold selectivity for CYP4A2 enzymes, which are mainly synthesized into 20-hete in mammalian kidneys. Synonyms: Dibromo-dodecenyl-methylsulfimide; 12,12-Dibromo-N-(methylsulfonyl)-11-dodecenamide. Grades: ≥98%. CAS No. 206052-03-1. Molecular formula: C13H23Br2NO3S. Mole weight: 433.2. | |
| Dipeptidyl Peptidase IV from Human, Recombinant | 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 contai...zyme from creative enzymes has been used to study the lc-ms (liquid chromatography-mass spectrometry) based assay method for dpp-iv inhibitor screening and substrate discovery. Group: Enzymes. Synonyms: 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; dipeptidy | |
| fructokinase | Fructokinase, also known as D-fructokinase or D-fructose (D-mannose) kinase, is an enzyme (EC 2.7.1.4) of the liver, intestine, and kidney cortex. Fructokinase is in a family of enzymes called transferases, meaning that this enzyme transfers functional groups; it is also considered a phosphotransferase (or, frequently, a kinase) since it specifically transfers a phosphate group. Fructokinase specifically catalyzes the transfer of a phosphate group from ATP (the substrate) to fructose as the initial step in its utilization. The main role of fructokinase is in carbohydrate metabolism, more specifically, sucrose and fructose metabolism. The reaction equation is as follows: ATP + D-fructose = ADP + D-fructose 6-phosphate. This is notable because in most tissues this reaction is catalyzed by hexokinase (EC 2.7.1.1). Group: Enzymes. Synonyms: fructokinase (phosphorylating); D-fructokinase; D-fructose(D-mannose)kinase. Enzyme Commission Number: EC 2.7.1.4. CAS No. 9030-51-7. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3069; fructokinase; EC 2.7.1.4; 9030-51-7; fructokinase (phosphorylating); D-fructokinase; D-fructose(D-mannose)kinase. Cat No: EXWM-3069. | |
| kallikrein 13 | The enzyme is specific for prorenin from the mouse submandibular gland, as prorenin from the mouse kidney (Ren1) and human prorenin are not substrates. Site-directed mutagenesis studies have shown that the enzyme will also cleave prorenin when Lys-Arg is replaced by Arg-Arg or Gln-Arg but the rate of reaction is much slower when Lys-Lys is used. This enzyme is also able to process pro-interleukin-1β (pro-IL-1β) in mouse submandibular gland to form IL-1&beta. Belongs in peptidase family S1A. Group: Enzymes. Synonyms: KLK13; kallikrein mK13; mGK-13; mK13; mKLK13; prorenin converting enzyme 1; PRECE-1; prorenin-converting enzyme; PRECE; proteinase P. Enzyme Commission Number: EC 3.4.21.119. CAS No. 342900-44-1. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4114; kallikrein 13; EC 3.4.21.119; 342900-44-1; KLK13; kallikrein mK13; mGK-13; mK13; mKLK13; prorenin converting enzyme 1; PRECE-1; prorenin-converting enzyme; PRECE; proteinase P. Cat No: EXWM-4114. | |
| Kallikrein-1 from Human, Recombinant | Kallikreins are serine protease enzymes having various physiological functions. Kallikreins are implicated in carcinogenesis and have potenital as novel cancer disease biomarkers. KLK1 is one of the fifteen kallikrein subfamily members located in a cluster on chromosome 19. KLK1 is functionally conserved in its ability to release the vasoactive peptide, Lys-bradykinin, from low molecular weight kininogen. Human Kallikrein-1, also called as Kallidinogenase, Kininogenase or Kininogenin, is an active protein enzyme present in saliva, pancreatic juices, and urine that catalyzes the proteolysis of bradykininogen to bradykinin. Kallikrein-1, which derived from human or porcine, h...ysis by RP-HPLC. (b) Analysis by SDS-PAGE. Kallikrein. Mole weight: 28-32 kDa. Activity: 5 Units/mg. Stability: Lyophilized KLK1although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution KLK1 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles. Appearance: Sterile Filtered white lyophilized powder. Source: Pichia Pastoris. Species: Human. KLK1; KLK-1; HK1; HK-1; KLKR; KLK6; Tissue Kallikrein; Hklk1; EC 3.4.21.35; Kidney/pancreas/salivary gland kallikrein; Kallikrein-1. Cat No: NATE-0851. | |
| L-Carnitine-13C Chloride | L-Carnitine-13C Chloride is an essential cofactor of fatty acid metabolism; required for the transport of fatty acids through the inner mitochondrial membrane. Synthetized primarily in the liver and kidney; highest concentrations found in heart and skeletal muscle. Applications: An essential cofactor of fatty acid metabolism. Group: Coenzymes. Synonyms: AG-B-72503. CAS No. 541-15-1 (unlabeled). Mole weight: 198.65. AG-B-72503; L-Carnitine-13C Chloride; 541-15-1 (unlabeled). Cat No: COEC-092. | |
| leucyl aminopeptidase | A zinc enzyme isolated from pig kidney and cattle lens; activated by heavy metal ions. Type example of peptidase family M17. Group: Enzymes. Synonyms: leucine aminopeptidase; leucyl peptidase; peptidase S; cytosol aminopeptidase; cathepsin III; L-leucine aminopeptidase; leucinaminopeptidase; leucinamide aminopeptidase; FTBL proteins; proteinates FTBL; aminopeptidase II; aminopeptidase III; aminopeptidase I. Enzyme Commission Number: EC 3.4.11.1. CAS No. 9001-61-0. LAP. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4007; leucyl aminopeptidase; EC 3.4.11.1; 9001-61-0; leucine aminopeptidase; leucyl peptidase; peptidase S; cytosol aminopeptidase; cathepsin III; L-leucine aminopeptidase; leucinaminopeptidase; leucinamide aminopeptidase; FTBL proteins; proteinates FTBL; aminopeptidase II; aminopeptidase III; aminopeptidase I. Cat No: EXWM-4007. | |
| Lisinopril | Lisinopril is angiotensin-converting enzyme inhibitor, used in treatment of hypertension, congestive heart failure, and heart attacks. Uses: Lisinopril is used primarily in treatment of high blood pressure, heart failure, and after heart attacks. it is also used for preventing kidney and eye complications in people with diabetes. it is used to improve survival in certain individuals following myocardial infarction, and to prevent progression of renal disease in hypertensive patients with diabetes mellitus and microalbuminuria or overt nephropathy. Synonyms: (s)-1-(n(sup2)-(1-carboxy-3-phenylpropyl)-l-lysyl)-l-proline; lysinopril; mk0521; mk-0521; mk522; PRINIL; PRINIVIL; n-{n-[(s)-1-carboxy-3-phenylpropyl]-l-lysyl}-l-proline. Grades: > 95%. CAS No. 76547-98-3. Molecular formula: C21H31N3O5. Mole weight: 405.49. | |
| LY3522348 | KHK-IN-3 (Example 1) is a ketohexokinase ( KHK ) inhibitor. KHK-IN-3 can be used in the study of kidney disease, nonalcoholic steatohepatitis (NASH), diabetes and heart failure. KHK is a rate-limiting enzyme and fructokinase involved in fructose metabolism. KHK catalyzes the phosphorylation of fructose to fructose-1-phosphate (FIP) at the expense of ATP. The lack of feedback inhibition of fructose metabolism triggers the accumulation of downstream intermediates such as lipogenesis, gluconeogenesis, and oxidative phosphorylation [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: KHK-IN-3. CAS No. 2568608-48-8. Pack Sizes: 10 mM * 1 mL; 5 mg; 10 mg; 25 mg; 50 mg; 100 mg. Product ID: HY-149987. | |
| membrane dipeptidase | A membrane-bound, zinc enzyme with broad specificity. Abundant in the kidney cortex. Inhibited by bestatin and cilastatin. Type example of peptidase family M19. Group: Enzymes. Synonyms: renal dipeptidase; dehydropeptidase I (DPH I); dipeptidase (ambiguous); aminodipeptidase; dipeptide hydrolase (ambiguous); dipeptidyl hydrolase (ambiguous); nonspecific dipeptidase; glycosyl-phosphatidylinositol-anchored renal dipeptidase; MDP. Enzyme Commission Number: EC 3.4.13.19. CAS No. 9031-99-6. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4033; membrane dipeptidase; EC 3.4.13.19; 9031-99-6; renal dipeptidase; dehydropeptidase I (DPH I); dipeptidase (ambiguous); aminodipeptidase; dipeptide hydrolase (ambiguous); dipeptidyl hydrolase (ambiguous); nonspecific dipeptidase; glycosyl-phosphatidylinositol-anchored renal dipeptidase; MDP. Cat No: EXWM-4033. | |
| meprin A | A membrane-bound metalloendopeptidase of rat and mouse kidney and intestinal brush borders, and salivary ducts. Differences from neprilysin (EC 3.4.24.11 (astacin family). Formerly included in EC 3.4.24.11. Group: Enzymes. Synonyms: endopeptidase-2; meprin-a; meprin; N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase; PABA-peptide hydrolase; PPH. Enzyme Commission Number: EC 3.4.24.18. CAS No. 148938-24-3. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4299; meprin A; EC 3.4.24.18; 148938-24-3; endopeptidase-2; meprin-a; meprin; N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase; PABA-peptide hydrolase; PPH. Cat No: EXWM-4299. | |
| meprin B | A brush border membrane-bound metalloendopeptidase known from the intestine of all mouse strains that have been tested, and the kidney of certain inbred strains. A tetramer of meprin β subunits (in contrast to meprin A, which contains both α and β subunits). Occurs in the kidney as a proenzyme that can be activated by trypsin. Meprin B is inhibited by both EDTA and 1,10-phenanthroline, but not by phosphoramidon, captopril or thiorphan. In peptidase family M12 (astacin family). Group: Enzymes. Synonyms: meprin-b. Enzyme Commission Number: EC 3.4.24.63. CAS No. 150679-52-0. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4346; meprin B; EC 3.4.24.63; 150679-52-0; meprin-b. Cat No: EXWM-4346. | |
| Meropenem Sodium Carbonate | Meropenem with sodium carbonate is a salt form of Meropenem, a β-lactam antibiotic of the carbapenem subclass that has been shown to inhibit penicillinase-negative, -positive and methicillin-susceptible staphylococci. This compound demonstrates the ability to also affect strains of 11 species of streptococci. Mechanistic studies suggest that Meropenem's antimicrobial activity is based on its high affinity for the majority of penicillin-binding proteins, which are cell wall-synthesizing enzymes. Meropenem is very effective because it resists inactivation by the majority of microbial LACTB (β-lactamases) as well as kidney dehydropeptidase I. Experiments have shown Meropenem to have a low toxicity profile and, in contrast to similar compounds, no central nervous system toxicity. Synonyms: (4R, 5S, 6S)-3-[[(3S, 5S)5-[(Dimethylamino)carbonyl]-3-pyrrolidinyl]thio]-6-((1R)-1-hydroxyethyl)-4-methyl-7-oxo-1-azabicyclo[3, 2, 0]hept-2-ene-2-carboxyloc acid. CAS No. 96036-03-2 free acid. Product ID: PAP-0097. Molecular formula: C17H25N3O5S xNa2CO3. Mole weight: 383.46 (free acid). Product Keywords: Antibacterial, Anti-inflammatory and Antiviral Series; PAP-0097; Meropenem Sodium Carbonate; 96036-03-2 free acid; (4R, 5S, 6S)-3-[[(3S, 5S)5-[(Dimethylamino)carbonyl]-3-pyrrolidinyl]thio]-6-((1R)-1-hydroxyethyl)-4-methyl-7-oxo-1-azabicyclo[3, 2, 0]hept-2-ene-2-carboxyloc acid. Chemical Name: Meropenem with sodium carbona |  |
| Migalastat HCl | Migalastat HCl, also known as AT1001 or GR181413A, is a pharmacological chaperone that selectively binds, stabilizes, and increases cellular levels of α-Gal A. Oral administration of migalastat HCl reduces tissue GL-3 in Fabry transgenic mice, and in urine and kidneys of some FD patients. Migalastat HCl may provide a potential novel genotype-specific treatment for Fabry Disease (FD). Phase 3 studies are ongoing. Fabry disease (FD) is a genetic disorder resulting from deficiency of the lysosomal enzyme α-galactosidase A (α-Gal A) which leads to globotriaosylceramide (GL-3) accumulation in multiple tissues. Synonyms: 1,5-Dideoxy-1,5-imino-D-galactitol HCl; DGJ; (2R,3S,4R,5S)-2-methylolpiperidine-3,4,5-triol hydrochloride; Migalastat hydrochloride; Amigal. Grades: 98%. CAS No. 75172-81-5. Molecular formula: C6H13NO4.HCl. Mole weight: 199.63. | |
| N-[2-(4-oxo-4H-3,1-benzoxazin-2-yl)phenyl]-2-naphthalenesulfonamide | N-[2-(4-oxo-4H-3,1-benzoxazin-2-yl)phenyl]-2-naphthalenesulfonamide, a profound small molecule inhibitor designed to target Cancerous Enzyme Carbonic Anhydrase IX (CAIX). This molecule is capable of exhibiting its potential therapeutic efficacy against various malignancies in numerous body sites including Breast, Prostate, and Kidney. This inhibitor is highly recommended due to its ability to repress the CAIX activity, a pivotal catalyst responsible for tumor inception, advancement, and invasion, rendering it a glimmer of hope as a Cancer treatment. Synonyms: oxobenzoxazinyl naphthalene sulfoanilide; 2-Naphthalenesulfonamide, N-[2-(4-oxo-4H-3,1-benzoxazin-2-yl)phenyl]-. CAS No. 10128-55-9. Molecular formula: C24H16N2O4S. Mole weight: 428.46. | |
| N-Acetyltaurine | N-Acetyltaurine is a sulfonate that can serve as a carbon source or a nitrogen source, and an energy source for microbial growth (such as the NAT strain). Additionally, N-Acetyltaurine is also a substrate for the amidase enzyme, porcine kidney N-acetyl-β-alanine deacetylase [EC 3.5.1.21] [1]. Uses: Scientific research. Group: Signaling pathways. CAS No. 19213-70-8. Pack Sizes: 10 mM * 1 mL; 5 mg; 10 mg; 25 mg; 50 mg; 100 mg. Product ID: HY-W587486. | |
| Native Bovine α (1-2,3,4,6) Fucosidase | Tissue alpha-L-fucosidase is an enzyme that in humans is encoded by the FUCA1 gene. Alpha-Fucosidase is an enzyme that breaks down fucose. Fucosidosis is an autosomal recessive lysosomal storage disease caused by defective alpha-L-fucosidase with accumulation of fucose in the tissues. Different phenotypes include clinical features such as neurologic deterioration, growth retardation, visceromegaly, and seizures in a severe early form; coarse facial features, angiokeratoma corporis diffusum, spasticity and delayed psychomotor development in a longer surviving form; and an unusual spondylometaphyseoepiphyseal dysplasia in yet another form. Group: Enzymes. Synonyms: α (1-2,3,4,6) Fucosidase; alpha-L-fucosidase; Alpha-Fucosidase; FUCA1; FUCA. FUCA. Source: Bovine kidney. Species: Bovine. α (1-2,3,4,6) Fucosidase; alpha-L-fucosidase; Alpha-Fucosidase; FUCA1; FUCA. Cat No: NATE-0261. | |
| Native Bovine α-L-Fucosidase | In enzymology, an alpha-L-fucosidase (EC 3.2.1.51) is an enzyme that catalyzes the chemical reaction:an alpha-L-fucoside + H2O<-> L-fucose + an alcohol. Thus, the two substrates of this enzyme are alpha-L-fucoside and H2O, whereas its two products are L-fucose and alcohol. This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O-and S-glycosyl compounds. This enzyme participates in n-glycan degradation and glycan structures-degradation. Group: Enzymes. Synonyms: α-L-Fucosidase; EC 3.2.1.51; α-fucosidase. Enzyme Commission Number: EC 3.2.1.51. CAS No. 9037-65-4. FUCA. Activity: > 2.0 units/mg protein (biuret). Storage: 2-8°C. Form: ammonium sulfate suspension. Suspension in 3.2 M (NH4)2SO4, 10 mM NaH2PO4 10 mM Citrate, pH 6.0. Source: Bovine kidney. Species: Bovine. α-L-Fucosidase; EC 3.2.1.51; α-fucosidase. Cat No: NATE-0266. | |
| Native Bovine Angiotensin Converting Enzyme | Angiotensin-converting enzyme (EC 3.4.15.1), or "ACE" indirectly increases blood pressure by causing blood vessels to constrict. It does that by converting angiotensin I to angiotensin II, which constricts the vessels. For this reason, drugs known as ACE inhibitors are used to lower blood pressure. ACE, angiotensin I and angiotensin II are part of the renin-angiotensin system (RAS), which controls blood pressure by regulating the volume of fluids in the body. ACE is secreted in the lungs and kidneys by cells in the endothelium (inner layer) of blood vessels. Applications: Positive control. Group: Enzymes. Synonyms: ACE; Angiotensin Converting Enzyme; EC 3.4.15.1; dipept...te buffer-300 mM NaCl, pH 8.3 at 37°C. Storage: Maintain at -20°C in undiluted aliquots for up to 12 months. Maintain at 4°C for up to one month. A decrease in activity may occur within prolonged storage at 4°C. Source: Bovine lung. Species: Bovine. ACE; Angiotensin Converting Enzyme; EC 3.4.15.1; dipeptidyl carboxypeptidase I; peptidase P; dipeptide hydrolase, peptidyl dipeptidase; angiotensin converting enzyme; kininase II; angiotensin I-converting enzyme; carboxycathepsin; dipeptidyl carboxypeptidase; "hypertensin converting enzyme" peptidyl dipeptidase I; peptidyl-dipeptide hydrolase; peptidyldipeptide hydrolase; endothelial cell peptidyl dipeptidase; peptidyl dipept | |
| Native Bovine Auto-Activated Protein Kinase | Auto-Activated Protein Kinase phosphorylates and inactivates protein phosphatase 2A. The funtion appears to be related to the catalytic domain of p21-activated p65 (PAK) protein kinase which is produced in apoptotic cells. AK is also involved in cytoskeleton organization and other signal transduction processes. Group: Enzymes. Synonyms: AK; Auto-Activated Protein Kinase. AK. Activity: ~17,000 units/mg protein. Stability: -70°C. Form: aqueous solution. Source: bovine kidney. Species: Bovine. AK; Auto-Activated Protein Kinase. Cat No: NATE-0042. | |
| Native Bovine β-N-Acetylglucosaminidase | This enzyme, 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. Applications: Bovine ki...idase A; N-acetylhexosaminidase; β-D-hexosaminidase; 9012-33-3; EC 3.2.1.52. Enzyme Commission Number: EC 3.2.1.52. CAS No. 9012-33-3. β-N-Acetylhexosaminidase. Activity: 10-50 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension. Suspension in 3.2 M (NH4)2SO4, pH approx. 6.0. Source: Bovine kidney. Species: Bovine. 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; | |
| Native Bovine 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 ...transferase; 9046-27-9; GGTP. Enzyme Commission Number: EC 2.3.2.2. CAS No. 9046-27-9. Purity: Purified. γ-GT. Activity: > 30 U/mg (Dimension Clinical Chemistry System). Appearance: Tan Powder. Storage: -20°C. Form: Lyophilized. Source: Bovine Kidney. Species: Bovine. 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-0790. | |
| Native Bovine Kidney Alkaline Phosphatase | Alkaline Phosphatase is a hydrolase enzyme responsible for removing phosphate groups in the 5- and 3- positions from many types of molecules, including nucleotides, proteins, and alkaloids. In humans, alkaline phosphatase is present in all tissues throughout the entire body, but is particularly concentrated in liver, bile duct, kidney, bone, and the placenta. The optimal pH for the enzyme activity is 10.0 in standard conditions. 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. Activity: > 750 U/mg solid. Storage: Store at -20°C. Form: Freeze dried powder. Source: Bovine Kidney. Species: Bovine. Alkaline phosphatase; ALP; ALKP; ALPase; Alk Phos; EC 3.1.3.1; Alkaline phosphomonoesterase; Glycerophosphatase; Phosphomonoesterase. Cat No: NATE-0946. | |
| Native Bovine Protamine Kinase, Cytosolic | Cytosolic protamine kinase is involved in the regulation of protein synthesis and is indirectly associated with numerous cellular processes. Cytosolic protamine kinase is a distinct insulin-stimulated kinase involved in the phosphorylation of eukaryotic Initiation Factor 4E (eIF4E) which is key to initiating translation by mRNA. This protein appears to be inactivated by protein phosphatase 2A family members and may also be inhibited by microcystin, okadeic acid, and ATP. The phosphorylation process is reversible and MBPK1 and MBPK2 (Myelin Basic Protein Kinase 1 and 2) may reactivate cytosolic protamine kinase. Applications: Cytosolic protamine kinase (cpk) is isolated from bovine kidney and has a molecular mass of approximately 45 kda. it phosphorylates the eukaryotic initiation factor 4e (eif4e), which initiates translation by mrna. it is used to study protein synthesis and various cellular processes. Group: Enzymes. Synonyms: Protamine Kinase, Cytosolic; Cytosolic protamine kinase; CPK; Cpk. Purity: >90% (SDS-PAGE). CPK. Activity: > 15,000 units/mg protein. Form: buffered aqueous glycerol solution. Source: Bovine kidney. Species: Bovine. Protamine Kinase, Cytosolic; Cytosolic protamine kinase; CPK; Cpk. Cat No: NATE-0155. | |
| Native Bovine Protein Phosphatase 2A2 | Protein phosphatase 2A (PP2A) is a specific protamine-kinase-inactivating phosphatase, one common physiological form of which is PP2A2. Protein Phosphatase 2A2 from bovine kidney was shown to be a unique inhibitor of protamine kinase while other phosphatases in the same family including PP1, PP2B, PP2C did not show any inhibition. Protein phosphatase 2a (pp2a) is a specific protamine-kinase-inactivating phosphatase, one common physiological form of which is pp2a2. Applications: Protein phosphatase 2a2 has been used in a study to investigate two heat-stable protein inhibitors. it has also been used in a study to describe the purification and properties of a protamine kinase from bovine kidney microsomes. Group: Enzymes. Synonyms: Protein Phosphatase 2A2; PP2A2. Protein Phosphatase. Activity: ~2.0 U/vial. Stability: -70°C. Form: buffered aqueous glycerol solution. Source: Bovine kidney. Species: Bovine. Protein Phosphatase 2A2; PP2A2. Cat No: NATE-0617. | |
| Native Bovine Protein Phosphatase 2Ac | Divalent cation-independent catalytic subunit of protein phosphatase 2A. Useful for functional studies of the A and B subunit of the phosphatase. Group: Enzymes. Synonyms: Protein Phosphatase 2Ac; PP2Ac. Protein Phosphatase. Activity: ~2 U/vial. Stability: -70°C. Form: buffered aqueous glycerol solution. Source: Bovine kidney. Species: Bovine. Protein Phosphatase 2Ac; PP2Ac. Cat No: NATE-0618. | |
| Native Bovine Protein Phosphatase 2C | Protein Phosphatase 2C is a Mg2+-dependent serine/threonine protein phosphatase with a molecular mass of 42-45 kDa, involved in regulating numerous cellular processes. It is ubiquitously expressed and has been isolated from many mammalian tissues including liver, brain, skeletal muscle, retina, and blood platelets. There are two major isotypes associated with this enzyme, 2C1 and 2C2, also known as 2Ca and 2Cb, respectively. Both isozymes appear to be equally Mg2+-dependent and respond similarly to specific substrates. Both are monomers that demonstrate ~75% sequence homology. The molecular masses are similar; 44 kDa and 42 kDa for 2C1 and 2C2, respectively. Additional Type 2C serine/threonine protein phosphatases include 2Cg, 2Cd, Wip1, and NERPP2C, many of which have multiple isozyme members. Group: Enzymes. Synonyms: Protein Phosphatase 2C; PP2C. Protein Phosphatase. Activity: ~1000 units/mg protein. Stability: -70°C. Form: buffered aqueous glycerol solution. Source: Bovine kidney. Species: Bovine. Protein Phosphatase 2C; PP2C. Pack: vial of 1 μg. Cat No: NATE-0619. | |
| Native Bovine Tautomerase | In enzymology, phenylpyruvate tautomerase or Macrophage migration inhibitory factor (EC 5.3.2.1) is an enzyme that catalyzes the chemical reaction:keto-phenylpyruvate<-> enol-phenylpyruvate. Phenylpyruvate tautomerase has also been found to exhibit the same keto-enol tautomerism for 4-Hydroxyphenylpyruvic acid, which is structurally similar to phenylpyruvate but contains an additional hydroxyl moiety in the para position of the aromatic ring. This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting keto-and enol-groups. This enzyme participates in tyrosine metabolism and phenylalanine metabolism. Applications: Tautomerase from bovine kidney has been used in a study to assess tritium isotope effects in the reaction catalyzed by 4-hydroxyphenylpyruvate dioxygenase. tautomerase from bovine kidney has also been used in a study to investigate human macrophage migration inhibitory factor. Group: Enzymes. Synonyms: Tautomerase; phenylpyruvate tautomerase; EC 5.3.2.1; phenylpyruvic keto-. Enzyme Commission Number: EC 5.3.2.1. CAS No. 9023-54-5. Tautomerase. Activity: 1-4 units/mg protein (Lowry), ~10 units/mL. Storage: -20°C. Form: aqueous solution. Source: Bovine kidney. Species: Bovine. Tautomerase; phenylpyruvate tautomerase; EC 5.3.2.1; phenylpyruvic keto-enol isomerase; 9023-54-5. Cat No: NATE-0691. | |
| Native Candida Rugosa Cholesterol Esterase | Cholesterol esterase (CE) is also known as cholesterol ester hydrolase. This enzyme catalyzes the following reaction: Sterol Ester --------> Sterol + Fatty Acid.Cholesterol esterase activity has been demonstrated in pancreas, intestine, liver and kidney. The enzyme is inactivated by proteolytic enzymes but stabilized by proteolytic enzyme inhibitors and by bile salts. CE from rat pancreas has a molecular weight of 65,000-69,000. In the presence of bile salts, it aggregates to a hexamer which is possibly the active form of the enzyme. Group: Enzymes. Synonyms: cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; sterol esterase; CE. Enzyme Commission Number: EC 3.1.1.13. CAS No. 9026-00-0. Purity: 0.9. Cholesterol Esterase. Activity: 25-100 U/mg. Storage: Store at -20° C. Form: Freeze-dried powder. Source: Candida Rugosa. cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; sterol esterase; CE. Cat No: NATE-1679. | |
| Native Equine γ-Glutamyltranspeptidase | 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. Group: Enzymes. Synonyms: EC 2.3.2.2; glutamyl transpeptidase; α-glutamyl transpeptidase; . Enzyme Commission Number: EC 2.3.2.2. CAS No. 9046-27-9. γ-GT. Activity: 5-12 units/mg solid. Storage: -20°C. Source: Equine kidney. Species: Equine. 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-0791. | |
| 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 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 Mouse Endoproteinase Arg-C | An Endoglycosidase is an enzyme that releases oligosaccharides from glycoproteins or glycolipids. It may also cleave polysaccharide chains between residues that are not the terminal residue, although releasing oligosaccharides from conjugated protein and lipid molecules is more common. It breaks the glycosidic bonds between two sugar monomer in the polymer. It is different from exoglycosidase that it does not do so at the terminal residue. Hence, it is used to release long carbohydrates from conjugated molecules. If an exoglycosidase were used, every monomer in the polymer would have to be removed, one by one from the chain, taking a long time. An endoglycosidase cleaves, giving a polymeric product. Group: Enzymes. Synonyms: EC 3.4.21.35; glandular kallikrein; pancreatic kallikrein; submandibular. Enzyme Commission Number: EC 3.4.21.35. CAS No. 82047-85-6. Kallikrein. Storage: -20°C. Form: lyophilized powder. Source: Mouse submaxillary gland. Species: Mouse. EC 3.4.21.35; glandular kallikrein; pancreatic kallikrein; submandibular kallikrein; submaxillary kallikrein; kidney kallikrein; urinary kallikrein; kallikrein; salivary kallikrein; kininogenin; kininogenase; callicrein; glumorin; padreatin; padutin; kallidinogenase; bradykininogenase; depot-padutin; urokallikrein; dilminal D; onokrein P; 82047-85-6. Pack: vial of 5 μg. Cat No: NATE-0218. | |
| Native Porcine Acylase I | In enzymology, an aminoacylase (EC 3.5.1.14) is an enzyme that catalyzes the chemical reaction:N-acyl-L-amino acid + H2O<-> carboxylate + L-amino acid. Thus, the two substRates of this enzyme are N-acyl-L-amino acid and H2O, whereas its two products are carboxylate and L-amino acid. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. This enzyme participates in urea cycle and metabolism of amino groups. Protein determined by biuret. Applications: Acylase i from porcine kidney has been used to study the acylase i-catalyzed deacetylation of various s-alkyl-n-acetyl-l-cysteines and their carb...ort acyl amidoacylase; ACY1 (gene name); N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14; 9012-37-7. Enzyme Commission Number: EC 3.5.1.14. CAS No. 9012-37-7. ACY1. Activity: > 2,000 units/mg protein; 500-1,500 units/mg protein. Storage: -20°C. Form: lyophilized powder. Source: Porcine kidney. Species: Porcine. aminoacylase 1; aminoacylase I; dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; acylase; aminoacylase; L-amino-acid acylase; α-N-acylaminoacid hydrolase; long acyl amidoacylase; short acyl amidoacylase; ACY1 (gene name); N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14; 9012-37-7. Cat No: NATE-0031. | |
| Native Porcine 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. Applications: Alkaline phosphatase is used for conjugation to antibodies and other proteins for elisa, western blotting, and hist ochemical detection. alkaline phosphatase is also used to prevent dna self ligation and for radiolabeling. 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. Activity: >100U/mg. Storage: -20°C. Form: Freeze dried powder. Source: Porcine kidney. Species: Porcine. Alkaline phosphatase; ALP; ALKP; ALPase; Alk Phos; EC 3.1.3.1; Alkaline phosphomonoesterase; Glycerophosphatase; Phosphomonoesterase. Pack: Package size based on DEA units. Cat No: NATE-0059. | |
| Native Porcine Aminopeptidase M | Native amino peptidase M from porcine kidney. Metalloprotease that hydrolyzes N-terminal amino acids from almost all unsubstituted oligopeptides. Does not cleave X-Pro bonds or N-blocked amino acids. Useful in peptide sequencing. Inhibited by EDTA, bestatin, and amastatin. Group: Enzymes. Synonyms: Aminopeptidase M. Enzyme Commission Number: EC 3.4.11.2. CAS No. 9054-63-1. Aminopeptidase M. Activity: > 50 units/ml. Stability: Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 4 months at -20°C. Appearance: White crystalline suspension. Storage: 2 - 8°C. Source: Porcine kidney. Species: Porcine. Aminopeptidase M. Cat No: NATE-1912. | |
| Native Porcine Angiotensin Converting Enzyme | Angiotensin-converting enzyme (EC 3.4.15.1), or "ACE" indirectly increases blood pressure by causing blood vessels to constrict. It does that by converting angiotensin I to angiotensin II, which constricts the vessels. For this reason, drugs known as ACE inhibitors are used to lower blood pressure. ACE, angiotensin I and angiotensin II are part of the renin-angiotensin system (RAS), which controls blood pressure by regulating the volume of fluids in the body. ACE is secreted in the lungs and kidneys by cells in the endothelium (inner layer) of blood vessels. Ace is a monomer with molecular weight of ~170 kda ph range for activity: 7-8.5 temperature optimum: 37°c zinc is...-82-1. Angiotensin Converting Enzyme. Activity: > 10 units/mg protein (Bradford). Storage: -20°C. Form: Lyophilized powder containing Tris buffer salts. Source: Porcine kidney. Species: Porcine. ACE; Angiotensin Converting Enzyme; EC 3.4.15.1; dipeptidyl carboxypeptidase I; peptidase P; dipeptide hydrolase, peptidyl dipeptidase; angiotensin converting enzyme; kininase II; angiotensin I-converting enzyme; carboxycathepsin; dipeptidyl carboxypeptidase; "hypertensin converting enzyme" peptidyl dipeptidase I; peptidyl-dipeptide hydrolase; peptidyldipeptide hydrolase; endothelial cell peptidyl dipeptidase; peptidyl dipeptidase-4; PDH; peptidyl dipeptide hydrolase; DCP. Cat N | |
| Native Porcine Apo D-Amino Acid Oxidase | Apo-D-amino acid oxidase is entirely present as a monomeric protein, while the reconstituted holoenzyme is a dimer of 79 kDa. Group: Enzymes. Synonyms: Apo D-Amino Acid Oxidase; D-Amino Acid Oxidase; DAAO; Apo DAAO. Enzyme Commission Number: EC 1.4.3.3. CAS No. 9000-88-8. Purity: 0.9. DAAO. Activity: 25-30 U/mg protein. Storage: Store at -20° C. Form: Freeze-dried powder. Source: Porcine Kidney. Species: Porcine. Apo D-Amino Acid Oxidase; D-Amino Acid Oxidase; DAAO; Apo DAAO. Cat No: NATE-1872. | |
| Native Porcine D-Amino Acid Oxidase | D-Amino Acid Oxidase isolated from porcine kidney is used in the measurement of D-alanine and FAD, and in the preparation of L-amino acids from racemic mixtures. Creative Enzymes products are not intended for use in pharmaceutical applications. Applications: The measurement of d-alanine and fad, and in the preparation of l-amino acids from racemic mixtures. life science. Group: Enzymes. Synonyms: DAAO; DAO; OXDA; DAMOX; D-Amino Acid Oxidase; EC 1.4.3.3; 9000-88-8; ophio-amino-acid oxidase; L-amino acid:O2 oxidoreductase; new yellow enzyme. Enzyme Commission Number: EC 1.4.3.3. CAS No. 9000-88-8. DAAO. Activity: > 6000 U/g. Storage: Store at <-15°C. Form: A freeze-dried material. Source: Porcine kidney. Species: Porcine. DAAO; DAO; OXDA; DAMOX; D-Amino Acid Oxidase; EC 1.4.3.3; 9000-88-8; ophio-amino-acid oxidase; L-amino acid:O2 oxidoreductase; new yellow enzyme. Cat No: NATE-0180. | |
| Native Porcine Diamine Oxidase | Diamine oxidase from porcine kidney is a homodimer consisting of 2 equal subunits with a molecular weight of 87 kDa each. Each subunit contains one molecule of pyridoxal phosphate and one atom of copper. The molecular mass of the enzyme is found to be 170 kDa. The enzyme is a glycoprotein containing 5% hexose, 3.3% glucosamine, 2.6% N-acetylglucosamine, and 0.25% N-acetylneuraminic acid. The enzyme exhibits a high affinity for concanavalin A. It catalyzes the oxidation of monoamines, diamines, and histamine to aldehydes, ammonia, and hydrogen peroxide. Optimum pH with cadverine and histamine as substrates is found to be 6.3-7.4.2 The enzyme is classified as a copper amine oxid...a luminescence-based test for determining ornithine decarboxylase activity. diamine oxidase from porcine kidney has also been used in a study to investigate n-linked oligosaccharide structures in diamine oxidase. Group: Enzymes. Synonyms: EC 1.4.3.6; 9001-53-0; Amine:oxygen oxidoreductase (deaminating) (pyridoxal-containing); Diamine Oxidase; Amine oxidase (copper-containing). Enzyme Commission Number: EC 1.4.3.6. CAS No. 9001-53-0. Diamine Oxidase. Activity: > 0.05 unit/mg solid. Storage: -20°C. Source: Porcine kidney. Species: Porcine. EC 1.4.3.6; 9001-53-0; Amine:oxygen oxidoreductase (deaminating) (pyridoxal-containing); Diamine Oxidase; Amine oxidase (copper-containing). | |
| Native Porcine Dipeptidyl Peptidase IV | 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...ukocyte 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. Enzyme Commission Number: EC 3.4.14.5. CAS No. 54249-88-6. Purity: >94% by SDS-PAGE. DPP IV. Activity: 1.0 U/mg; Specific Activity >40 U/mg protein. Storage: at -70°C, Avoid freeze/thaw. Form: Liquid. In 20 mM Tris-HCl, 5 mM CaCl?, 1 uM ZnCl?, 0.05% NaN?, pH 8.0. Source: Porcine Kidney. Species: Porcine. EC 3.4.14.5; 54249-88-6; DPPIV; DPP4; dipeptidyl aminopeptidase IV; Xaa-Pro-dipeptidyl-aminopeptidase; Gly-Pro naphthylamidas | |
| Native Porcine γ-Glutamyltranspeptidase | 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 cellul...ase; GGT (ambiguous); γ-glutamyltranspeptidase (ambiguous); γ-glutamyltransferase; 9046-27-9; GGTP. Enzyme Commission Number: EC 2.3.2.2. CAS No. 9046-27-9. γ-GT. Activity: 2.0-6.0 units/mg solid. Storage: -20°C. Source: Porcine kidney. Species: Porcine. 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-0793. | |
| Native Porcine Glutamic-Oxalacetic Transaminase | Aspartate transaminase (AST) or aspartate aminotransferase, also known as AspAT/ASAT/AAT or serum glutamic oxaloacetic transaminase (SGOT), is a pyridoxal phosphate (PLP)-dependent transaminase enzyme (EC 2.6.1.1). AST catalyzes the reversible transfer of an α-amino group between aspartate and glutamate and, as such, is an important enzyme in amino acid metabolism. AST is found in the liver, heart, skeletal muscle, kidneys, brain, and red blood cells. Serum AST level, serum ALT (alanine transaminase) level, and their ratio (AST/ALT ratio) are commonly measured clinically as biomarkers for liver health. The tests are part of blood panels. Group: Enzymes. Synonyms: EC 2.6.1.1; glutamic-oxaloacetic transaminase; glutamic-aspartic transaminase; transaminase A; AAT; AspT; 2-oxoglutaRate-glutamate aminotransferase; aspartate α-ketoglutaRate transaminase; aspartate aminotransferase; aspartate-2-oxoglutaRate transaminase; aspartic acid aminotr. Enzyme Commission Number: EC 2.6.1.1. CAS No. 9000-97-9. Activity: > 100 U/mg. Storage: 2-8°C. Source: Porcine heart. Species: Porcine. EC 2.6.1.1; glutamic-oxaloacetic transaminase; glutamic-aspartic transaminase; transaminase A; AAT; AspT; 2-oxoglutaRate-glutamate aminotransferase; aspartate α-ketoglutaRate transaminase; aspartate aminotransferase; aspartate-2-oxoglutaRate transa | |
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