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| Product | Description | |
|---|---|---|
| Triton X-100 | 100ml Pack Size. Group: Detergents. Formula: (C2H4O)nC14H22O. CAS No. 9002-93-1. Prepack ID 11084669-100ml. See USA prepack pricing. |  |
| Triton X-100 | 1lt Pack Size. Group: Detergents. Formula: (C2H4O)nC14H22O. CAS No. 9002-93-1. Prepack ID 11084669-1lt. See USA prepack pricing. | |
| Triton X-100 | 2.5lt Pack Size. Group: Detergents. Formula: (C2H4O)nC14H22O. CAS No. 9002-93-1. Prepack ID 11084669-2.5lt. See USA prepack pricing. | |
| Triton X-100 | Triton X-100. Grades: Product ID: 1-01412. |  |
| Triton X-100 | Widely used non-ionic surfactant for recovery of membrane components under mild non-denaturing conditions. Group: Biochemicals. Alternative Names: 4- (1, 1, 3, 3-Tetramethylbutyl) phenyl-polyethylene glycol; t-Octyl phenoxypoly ethoxyethanol; Polyethylene glycol tert-octylphenyl ether. Grades: Molecular Biology Grade. CAS No. 9002-93-1. Pack Sizes: 100ml, 500ml, 1L, 4L. Molecular Formula: (C2H4O)nC14H22O. US Biological Life Sciences. |  Worldwide |
| Triton(R)x-100 | Triton(R)x-100. Uses: Designed for use in research and industrial production. Additional or Alternative Names: DECA(ETHYLENE GLUCOL) MONOOCTYLPHENYL ETHER;IGEPAL(R) CA-630;IGEPAL CA-630;ISO-OCTYLPHENOXYPOLYETHOXYETHANOL;ALKYLARYL POLYETHER ALCOHOL;4-(1,1,3,3-TETRAMETHYLBUTYL)PHENYL-POLYETHYLENE GLYCOL;4-(1,1,3,3-TETRAMETHYLBUTYL)CYCLOHEXYL-POLYETHYLENE GLYCOL;SURF. Product Category: Polymer/Macromolecule. CAS No. 92046-34-9. Molecular formula: C34H62O11. Mole weight: 646.84948. Product ID: ACM92046349. Alfa Chemistry ISO 9001:2015 Certified. Categories: Triton X-100. |  |
| Triton(R)x-100,hydrogenated | Triton(R)x-100,hydrogenated. Uses: Designed for use in research and industrial production. Additional or Alternative Names: TRX-100;TRX-100, HYDROGENATED;TRITON(R) X-100, REDUCED FORM;TRITON X-100 HYDROGENATED;TRITON(R) X-100, HYDROGENATED;OCTYLPHENOXYPOLYETHOXYETHANOL;OCTYLPHENOXYPOLYETHOXYETHANOL, HYDROGENATED;polyethylene glycol mono-p-octylphenyl ether, reduced. Product Category: Heterocyclic Organic Compound. Appearance: Viscous, colorless liquid. CAS No. 101013-07-4. Molecular formula: C28H56O8. Mole weight: 520.74. Density: 1.030 g/mL at 20 °C(lit.). Product ID: ACM101013074. Alfa Chemistry ISO 9001:2015 Certified. | |
| Acl I | One unit of the enzyme is the amount required to hydrolyze 1 μg of Lambda DNA in 1 hour at 37°C in a total reaction volume of 50 μl. Applications: After 2-fold overdigestion with enzyme 90% of the dna fragments can be ligated and recut. Group: Restriction Enzymes. Purity: 200U. AA↑CGTT TTGC↓AA. Activity: 3000-5000u.a./ml. Appearance: 10 X SE-buffer Y, BSA. Storage: -20°C. Form: Liquid. Source: Acinetobacter calcoaceticus. Pack: 10 mM Tris-HCl (pH 7.5); 100 mM NaCl; 0.1 mM EDTA; 7 mM 2-mercaptoethanol; 200 μg/ml BSA; 0.05% Triton X-100; 50% glycerol. Cat No: RE-1009EN. |  |
| Bsu I | One unit of the enzyme is the amount required to hydrolyze 1 μg of Lambda DNA in 1 hour at 37°C in a total reaction volume of 50 μl. Applications: After 5-fold overdigestion with enzyme ~10% of dna fragments can be ligated with t4 dna ligase and recut. Group: Restriction Enzymes. Purity: 200U; 1000U. GTATCC(N)6↑ CATAGG(N)5&darr. Activity: 2000-5000u.a./ml. Appearance: 10 X SE-buffer Y. Storage: -20°C. Form: Liquid. Source: Bacillus sphaericus. Pack: 10 mM Tris-HCl (pH 7.5); 100 mM NaCl; 0.1 mM EDTA; 7 mM 2-mercaptoethanol; 200 μg/ml BSA, 0.05% Triton X-100, 50% glycerol. Cat No: ET-1091RE. | |
| Casein Kinase II from Human, Recombinant | The Casein kinase 2 (EC 2.7.11.1) is a serine/threonine-selective protein kinase that is a tetramer of two alpha subunits and two beta subunits. The alpha subunits have the catalytic kinase domain. Casein kinase 2 has been implicated in cell cycle control, DNA repair, regulation of the circadian rhythm and other cellular processes. Casein kinase ii (ck2) is a constitutively active serine/threonine protein kinase composed of two 44 kda catalytic α-subunits and two 26 kda regulatory β-subunits in an α2β2 configuration to form stable heterotetramers. ck2 holoenzyme undergoes autophosphorylation at two serine residues (s2/s3) of its β-subunit. recen... ck2 is able to phosphorylate, under special circumstances, tyrosyl residues in proteins. ck2 is implicated in a variety of cellular functions. Group: Enzymes. Synonyms: EC 2.7.11.1; Casein Kinase II; CK2; CK II; Casein Kinase 2. CAS No. 9026-43-1. CK. Mole weight: a-subunit (45 kDa), b-subunit (25 kDa). The apparent molecular weight of the a-subunit estimated by SDS-PAGE is about 42 kDa. Activity: 859,000 units/mg. Storage: at -80°C. Avoid repeated freeze/thaw cycles. Form: 350 mM NaCl, 20 mM Tris-HCl (pH 7.5 25°C), 1 mM Na2EDTA, 2 mM DTT and 0.1% Triton X-100. Source: E. coli. Species: Human. EC 2.7.11.1; Casein Kinase II; CK2; CK II; Casein Kinase 2. Cat No: NATE-1271. | |
| Native E. coli PreScission Protease | PreScission Protease is a fusion protein of glutathione S-transferase (GST) and human rhinovirus (HRV) type 14 3C protease. The protease specifically recognizes a subset of sequences which include the core amino acid sequence Leu-Phe-Gln/Gly-Pro cleaving between the Gln and Gly residues. Substrate recognition and cleavage are likely to be dependent not only upon primary structural signals, but also upon the secondary and tertiary structures of the fusion protein as well. Applications: During cleavage reactions, it is recommended that samples be removed at various time points and analyzed by sds-page to estimate the yield, purity, and extent of digestion. the amount of prescission protease, temperature and length of incubation required for complete digestion of a given gst fusion partner may vary depending on the fusion partner. optimal conditions for each fusion should be determined in pilot experiments. digestion may be improved by adding triton x-100, tween 20, nonidet, or np40 to a concentration of 0.01%. concentrations of these detergents up to 1% do not inhibit prescission protease. Group: Enzymes. Synonyms: . Purity: >90% by SDS-PAGE. PSP. Activity: >10000 IU/mg. Appearance: Sterile colorless liquid. Storage: Should be stored in small aliquots at -20°C to -80°C for long term. Source: E. coli. PreScission Protease; PSP. Cat No: NATE-0877. | |
| Native Human Cancer Antigen 15-3 | Native Human Cancer Antigen 15-3. Applications: Turbid, light yellow solution. Group: Others. Synonyms: CA 15-3; Tumor Marker 15-3; Mucin-1; MUC-1; Breast carcinoma-associated antigen DF3; Breast Tumor Antigen. CA 15-3. Activity: > 5,000 IU/mL. Stability: 2 years. Storage: at -20°C. Form: Solution in 1 M sodium chloride, 1% Triton(TM) X-100, 0.05% sodium azide, pH 7.4. Source: Human Ascites Fluid. CA 15-3; Tumor Marker 15-3; Mucin-1; MUC-1; Breast carcinoma-associated antigen DF3; Breast Tumor Antigen. Cat No: NATE-1929. | |
| 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 Porcine α-Ketoglutarate Dehydrogenase | The oxoglutarate dehydrogenase complex (OGDC) or α-ketoglutarate dehydrogenase complex is an enzyme complex, most commonly known for its role in the citric acid cycle. Group: Enzymes. Synonyms: 2-ketoglutarate dehydrogenase; 2-oxoglutarate dehydrogenase; 2-oxoglutarate:lipoate oxidoreductase; 2-oxoglutarate:lipoamide 2-oxidoreductase (decarboxylating and acceptor-succinylating); α-k. Enzyme Commission Number: EC 1.2.4.2. CAS No. 9031-2-1. AKGDH. Activity: 0.1-1.0 units/mg protein (Lowry). Storage: -20°C. Form: buffered aqueous glycerol solution. Supplied as a 50% glycerol solution containing ~9 mg per mL bovine serum albumin, 30% sucrose, 1.5 mM EDTA, 1.5 mM EGTA, 1.5 mM 2-mercaptoethanol, 0.3% TRITON(TM) X-100, 0.003% sodium azide, and 15 mM potassium phosphate, pH 6.8. Source: Porcine heart. Species: Porcine. 2-ketoglutarate dehydrogenase; 2-oxoglutarate dehydrogenase; 2-oxoglutarate:lipoate oxidoreductase; 2-oxoglutarate:lipoamide 2-oxidoreductase (decarboxylating and acceptor-succinylating); α-ketoglutarate dehydrogenase; αketoglutaric acid dehydrogenase; α-ketoglutaric dehydrogenase; α-oxoglutarate dehydrogenase; AKGDH; OGDC; ketoglutaric dehydrogenase; oxoglutarate decarboxylase; oxoglutarate dehydrogenase; oxoglutarate dehydrogenase (lipoamide); EC 1.2.4.2; 9031-02-1. Cat No: NATE-0495. | |
| Native Porcine Trehalase | Trehalase is a glycoside hydrolase enzyme located in on the brush border of the small intestine that catalyzes the conversion of trehalose to glucose. It is found in most animals. The non-reducing disaccharide trehalose (α-D-glucopyranosyl-1,1-α-D-glucopyranoside) is one of the most important storage carbohydRates, which is present in almost all forms of life except mammals. The disaccharide is hydrolyzed into two molecules of glucose by the enzyme trehalase. There are two types of trehalases found in Saccharomyces cerevisiae, viz. neutral trehalase (NT) and acid trehalase (AT) classified according to their pH optima. NT has an optimum pH of 7.0, while that of AT is 4...mopara viticola-infected grapevine leaves. trehalase has also been used in a study to investigate growth arrest by trehalose-6-phosphate. Group: Enzymes. Synonyms: α,α-Trehalose glucohydrolase; Trehalase; EC 3.2.1.28; 9025-52-9; α,α-trehalase. Enzyme Commission Number: EC 3.2.1.28. CAS No. 9025-52-9. Trehalase. Activity: > 1.0 units/mg protein. Storage: -20°C. Form: buffered aqueous glycerol solution; Solution in 50% glycerol containing 1% Triton(TM) X-100 and 25 mM potassium phosphate, pH 6.5. Source: Porcine kidney. Species: Porcine. α,α-Trehalose glucohydrolase; Trehalase; EC 3.2.1.28; 9025-52-9; α,α-trehalase. Cat No: NATE-0717. | |
| Native Streptomyces chromofuscus Phospholipase D | Phospholipase D is a phospholipid hydrolyzing enzyme and an important component of receptor-mediated signal transduction responses and regulated secretion. Hydrolyzes the phosphate bonds of phospholipids and sphingomyelin to give the corresponding phosphatidic acid. Phospholipase D is involved in conferring drought susceptibility in peanuts, which increases the risk of aflatoxin contamination. Group: Enzymes. Synonyms: Phospholipase D; EC 3.1.4.4; lipophosphodiesterase II; lecithinase D; choline phosphatase; PLD; 9001-87-0. Enzyme Commission Number: EC 3.1.4.4. CAS No. 9001-87-0. PLD. Mole weight: mol wt ~60 kDa. Activity: Type I, > 50,000 units/mL; Type II, > 150 units/mg solid. Storage: -20°C. Form: Type I, buffered aqueous glycerol solution; Solution in 100 mM Tris/HCl, pH 8.0, 10% glycerol (v/v), and 0.1% Triton X-100 (w/v); Type II, lyophilized powder. Source: Streptomyces chromofuscus. Phospholipase D; EC 3.1.4.4; lipophosphodiesterase II; lecithinase D; choline phosphatase; PLD; 9001-87-0. Cat No: NATE-0596. | |
| Native Vaccinia virus 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. Applications: Enzyme activity is increased in the presence of 2.5 mm mg2+. topoisomerase i from vaccinia virus can be used for studying pivotal biological pr ocess such as-replication, transcription, recombination as well as dna structure and topology which includes chromatin reconstitution in vitro and the degree of supercoiling of dna. additionally, the product helps in relaxing the dna coils and exposes the restriction sites which...me; swivelase; ω-protein; deoxyribonucleate topoisomerase; topoisomerase; type I DNA topoisomerase; DNA topoisomerase; TOPO I. Enzyme Commission Number: EC 5.99.1.2. CAS No. 80449-01-0. TOPO I. Mole weight: mol wt 32 kDa. Storage: -20°C. Form: buffered aqueous solution; Solution in 50 mM Tris HCl, pH 7.5, containing 100 mM NaCl, 1 mM EDTA, 1 mM DTT, 0.1% Triton X-100, and 50% glycerol. Source: Vaccinia virus. 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-0708. | |
| Protein Kinase CβII isozyme from human, Recombinant | Protein Kinase C (PKC) is a serine/threonine kinase that is activated intracellularly by signal transduction pathways that produce DAG from phosphatidylinositol diphosphate (PIP2) and phosphatidylcholine (PC) through the action of various activated phospholipases. Phorbol esters also stimulate PKC. At least 11 PKC isozymes have been identified that differ in primary structure, tissue distribution, subcellular localization, response to extracellular signals, and substrate specificity. The isozymes can be grouped into three subfamilies. Members of the first family require Ca2+ and phospholipid and include PKCα, βI, βII, and &gamma. Members of the sec... esters and include PKCξ, μ, and &Iota. Group: Enzymes. Synonyms: PRKCB; PKCB; PRKCB1; PRKCB2; protein kinase C, beta 1; protein kinase C beta type; PKC-beta; EC 2.7.1.37. Enzyme Commission Number: EC 2.7.1.37. Purity: >95% (SDS-PAGE). PKC. Mole weight: calculated mol wt 76.9 kDa; mol wt 80 kDa by SDS-PAGE. Storage: -70°C. Form: buffered aqueous glycerol solution; Solution in 20 mM HEPES, pH 7.4; 2 mM EDTA, 2 mM EGTA, 5 mM DTT, 100 mM NaCl, 0.05% Triton X-100, and 50% glycerol. Source: Baculovirus infected insect cells. Species: Human. PRKCB; PKCB; PRKCB1; PRKCB2; protein kinase C, beta 1; protein kinase C beta type; PKC-beta; EC 2.7.1.37. Cat No: NATE-0622. | |
| Protein Kinase CβI isozyme from human, Recombinant | Protein Kinase C (PKC) is a serine/threonine kinase that is activated intracellularly by signal transduction pathways that produce DAG from phosphatidylinositol diphosphate (PIP2) and phosphatidylcholine (PC) through the action of various activated phospholipases. Phorbol esters also stimulate PKC. At least 11 PKC isozymes have been identified that differ in primary structure, tissue distribution, subcellular localization, response to extracellular signals, and substrate specificity. The isozymes can be grouped into three subfamilies. Members of the first family require Ca2+ and phospholipid and include PKCα, βI, βII, and &gamma. Members of the sec...ted by either DAG or phorbol esters and include PKCξ, μ, and &Iota. Group: Enzymes. Synonyms: PRKCB; PKCB; PRKCB1; PRKCB2; protein kinase C, beta 1; protein kinase C beta type; PKC-beta; EC 2.7.1.37. Enzyme Commission Number: EC 2.7.1.37. Purity: > 95% (SDS-PAGE). PKC. Mole weight: apparent mol wt 79-80 kDa. Storage: -70°C. Form: buffered aqueous glycerol solution; Solution in 20 mM HEPES, pH 7.4; 2 mM EDTA, 2 mM EGTA, 5 mM DTT, 100 mM NaCl, 0.05% Triton X-100, and 50% glycerol. Source: Baculovirus infected insect cells. Species: Human. PRKCB; PKCB; PRKCB1; PRKCB2; protein kinase C, beta 1; protein kinase C beta type; PKC-beta; EC 2.7.1.37. Cat No: NATE-0621. | |
| Protein Kinase Cδ isozyme from human, Recombinant | Protein Kinase C (PKC) is a serine/threonine kinase that is activated intracellularly by signal transduction pathways that produce DAG from phosphatidylinositol diphosphate (PIP2) and phosphatidylcholine (PC) through the action of various activated phospholipases. Phorbol esters also stimulate PKC. At least 11 PKC isozymes have been identified that differ in primary structure, tissue distribution, subcellular localization, response to extracellular signals, and substrate specificity. The isozymes can be grouped into three subfamilies. Members of the first family require Ca2+ and phospholipid and include PKCα, βI, βII, and &gamma. Members of the sec...DAG or phorbol esters and include PKCξ, μ, and &Iota. Group: Enzymes. Synonyms: PRKCD; protein kinase C, delta; protein kinase C delta type; ALPS3; CVID9; MAY1; PKCD; nPKC-delta; EC 2.7.1.37. Enzyme Commission Number: EC 2.7.1.37. Purity: >95% (SDS-PAGE). PKC. Mole weight: mol wt 74-79 kDa by SDS-PAGE. Storage: -70°C. Form: buffered aqueous glycerol solution; Solution in 20 mM HEPES, pH 7.4; 2 mM EDTA, 2 mM EGTA, 5 mM DTT, 100 mM NaCl, 0.05% Triton X-100, and 50% glycerol. Source: Baculovirus infected insect cells. Species: Human. PRKCD; protein kinase C, delta; protein kinase C delta type; ALPS3; CVID9; MAY1; PKCD; nPKC-delta; EC 2.7.1.37. Cat No: NATE-0623. | |
| Protein kinase Cγ isozyme from human, Recombinant | Protein Kinase C (PKC) is a serine/threonine kinase that is activated intracellularly by signal transduction pathways that produce DAG from phosphatidylinositol diphosphate (PIP2) and phosphatidylcholine (PC) through the action of various activated phospholipases. Phorbol esters also stimulate PKC. At least 11 PKC isozymes have been identified that differ in primary structure, tissue distribution, subcellular localization, response to extracellular signals, and substrate specificity. The isozymes can be grouped into three subfamilies. Members of the first family require Ca2+ and phospholipid and include PKCα, βI, βII, and &gamma. Members of the sec...vated by either DAG or phorbol esters and include PKCξ, μ, and &Iota. Group: Enzymes. Synonyms: PRKCG; protein kinase C, gamma; protein kinase C gamma type; PKC-gamma; PKCC; PKCG; SCA14; EC 2.7.1.37. Enzyme Commission Number: EC 2.7.1.37. Purity: >95% (SDS-PAGE). PKC. Mole weight: mol wt 77-84 kDa by SDS-PAGE. Storage: -70°C. Form: buffered aqueous glycerol solution; Solution in 20 mM HEPES, pH 7.4; 2 mM EDTA, 2 mM EGTA, 5 mM DTT, 250 mM NaCl, 0.05% Triton X-100, and 50% glycerol. Source: Baculovirus infected insect cells. Species: Human. PRKCG; protein kinase C, gamma; protein kinase C gamma type; PKC-gamma; PKCC; PKCG; SCA14; EC 2.7.1.37. Cat No: NATE-0624. | |
| Protein Kinase Cζ isozyme from human, Recombinant | Protein Kinase C (PKC) is a serine/threonine kinase that is activated intracellularly by signal transduction pathways that produce DAG from phosphatidylinositol diphosphate (PIP2) and phosphatidylcholine (PC) through the action of various activated phospholipases. Phorbol esters also stimulate PKC. At least 11 PKC isozymes have been identified that differ in primary structure, tissue distribution, subcellular localization, response to extracellular signals, and substrate specificity. The isozymes can be grouped into three subfamilies. Members of the first family require Ca2+ and phospholipid and include PKCα, βI, βII, and &gamma. Members of the seco...Members of the third family are not activated by either DAG or phorbol esters and include PKCξ, μ, and &Iota. Group: Enzymes. Synonyms: PRKCZ; protein kinase C, zeta; protein kinase C zeta type; PKC2; PKC-ZETA; EC 2.7.1.37. Enzyme Commission Number: EC 2.7.1.37. Purity: > 75% (SDS-PAGE). PKC. Mole weight: mol wt 76-80 kDa by SDS-PAGE. Storage: -70°C. Form: buffered aqueous solution; Solution in 20 mM HEPES, pH 7.5; 2 mM EDTA, 2 mM EGTA, 5 mM DTT, 250 mM NaCl, 0.05% Triton X-100, and 50% glycerol. Source: Baculovirus infected insect cells. Species: Human. PRKCZ; protein kinase C, zeta; protein kinase C zeta type; PKC2; PKC-ZETA; EC 2.7.1.37. Cat No: NATE-0625. | |
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