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| Product | Description | |
|---|---|---|
| 1-pyrroline-2-carboxylate reductase [NAD(P)H] | The enzyme from the bacterium Colwellia psychrerythraea is involved in trans-3-hydroxy-L-proline metabolism. In contrast to EC 1.5.1.1, 1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase [NAD(P)H], which shows similar activity with 1-piperideine-2-carboxylate and 1-pyrroline-2-carboxylate, this enzyme is specific for the latter. While the enzyme is active with both NADH and NADPH, activity is higher with NADPH. Group: Enzymes. Enzyme Commission Number: EC 1.5.1.49. 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-1530; 1-pyrroline-2-carboxylate reductase [NAD(P)H]; EC 1.5.1.49. Cat No: EXWM-1530. |  |
| 2-methylcitrate dehydratase (2-methyl-trans-aconitate forming) | Catalyses the dehydration of (2S,3S)-2-methylcitrate, forming the trans isomer of 2-methyl-aconitate (unlike EC 4.2.1.79, which forms only the cis isomer). Part of a propionate degradation pathway. The enzyme from Shewanella oneidensis can also accept citrate and cis-aconitate, but activity with (2S,3S)-2-methylcitrate was approximately 2.5-fold higher. 2-methylisocitrate and isocitrate were not substrates. An iron-sulfur protein. Group: Enzymes. Enzyme Commission Number: EC 4.2.1.117. 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-4957; 2-methylcitrate dehydratase (2-methyl-trans-aconitate forming); EC 4.2.1.117. Cat No: EXWM-4957. | |
| 2-oxoglutarate reductase | The enzyme catalyses a reversible reaction. The enzyme from the bacterium Peptoniphilus asaccharolyticus is specific for (R)-2-hydroxyglutarate. The SerA enzyme from the bacterium Escherichia coli can also accept (S)-2-hydroxyglutarate with a much higher Km, and also catalyses the activity of EC 1.1.1.95, phosphoglycerate dehydrogenase. Group: Enzymes. Synonyms: serA (gene name). Enzyme Commission Number: EC 1.1.1.399. 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-0319; 2-oxoglutarate reductase; EC 1.1.1.399; serA (gene name). Cat No: EXWM-0319. | |
| 3,8-divinyl protochlorophyllide a 8-vinyl-reductase (NADPH) | The enzyme, found in higher plants, green algae, and some phototrophic bacteria, is involved in the production of monovinyl versions of (bacterio)chlorophyll pigments from their divinyl precursors. It can also act on 3,8-divinyl chlorophyllide a. cf. EC 1.3.7.13, 3,8-divinyl protochlorophyllide a 8-vinyl-reductase (ferredoxin). Group: Enzymes. Synonyms: DVR (gene name); bciA (gene name); [4-vinyl]chlorophyllide a reductase; 4VCR; chlorophyllide-a:NADP+ oxidoreductase; divinyl chlorophyllide a 8-vinyl-reductase; plant-type divinyl chlorophyllide a 8-vinyl-reductase. Enzyme Commission Number: EC 1.3.1.75. 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-1344; 3,8-divinyl protochlorophyllide a 8-vinyl-reductase (NADPH); EC 1.3.1.75; DVR (gene name); bciA (gene name); [4-vinyl]chlorophyllide a reductase; 4VCR; chlorophyllide-a:NADP+ oxidoreductase; divinyl chlorophyllide a 8-vinyl-reductase; plant-type divinyl chlorophyllide a 8-vinyl-reductase. Cat No: EXWM-1344. | |
| 3-Acetylpyridine-Adenine Dinucleotide, Oxidized (APAD) | 3-Acetylpyridine adenine dinucleotide is an NAD analog with higher oxidation potential than NAD. It can substitute for NAD as a hydrogen-accepting cofactor in many dehydrogenase reactions. For example lactate dehydrogenase from Toxoplasma, Clonorchis, and Plasmodium, bacterial lipoamide dehydrogenase, as well as mammalian dehydrogenases. This compound can also act as a proton acceptor in various transhydrogenation reactions with NADH or NADPH. Group: Coenzymes. Synonyms: aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NA. Enzyme Commission Number: EC 1.1.1.1. CAS No. 1986-8-8. Purity: Determined by increase in absorbance at 363 nm on enzymatic reduction with ADH* at pH 10.0 > 92% *ADH = Alcohol dehydrogenase (Horse liver) (EC 1.1.1.1.). APAD. Mole weight: 662.44. Storage: Keep tightly stoppered in the dark below 5°C. Moisture will reduce the purity. For prolonged storage, keep below-20°C. aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1; APAD. Cat No: NATE-0077. | |
| 4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside β-D-glucosidase | The enzyme from Triticum aestivum (wheat) has a higher affinity for DIMBOA glucoside than DIBOA glucoside. With Secale cereale (rye) the preference is reversed. Group: Enzymes. Synonyms: DIMBOAGlc hydrolase; DIMBOA glucosidase. Enzyme Commission Number: EC 3.2.1.182. 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-3866; 4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside β-D-glucosidase; EC 3.2.1.182; DIMBOAGlc hydrolase; DIMBOA glucosidase. Cat No: EXWM-3866. | |
| Alanine Racemase (Crude Enzyme) | This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. This enzyme participates in alanine and aspartatemetabolism and D-alanine metabolism. It employs one cofactor, pyridoxal phosphate. At least two compounds, 3-Fluoro-D-alanine and D-Cycloserine are known to inhibit this enzyme. The D-alanine produced by alanine racemase is used for peptidoglycan biosynthesis. Peptidoglycan is found in the cell walls of all bacteria, including many which are harmful to humans. The enzyme is absent in higher eukaryotes but found everywhere in prokaryotes, making alanine racemase a great target for antimicrobial drug...udies have shown that without the alr gene being expressed, the bacteria would need an external source of D-alanine in order to survive. Therefore, the alr gene is a feasible target for antimicrobial drugs. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Drug development; pharmacology; medicine; pharmacology. Group: Enzymes. Synonyms: L-alanine racemase. Enzyme Commission Number: EC 5.1.1.1. CAS No. 9024-06-0. Alanine Racemase. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. L-alanine racemase. Pack: 100ml. Cat No: NATE-1854. | |
| Aldehyde Dehydrogenase 2 from Human, Recombinant | ALDH2 is part of the aldehyde dehydrogenase family of proteins which catalyze the chemical transformation from acetaldehyde to acetic acid. ALDH2 is the second enzyme of the major oxidative pathway of alcohol metabolism. ALDH2 has 2 major liver isoforms: cytosolic and mitochondrial, which differ by their electrophoretic mobilities, kinetic properties, and subcellular localizations. Nearly all Caucasians have 2 major isozymes, whereas roughly 50% of Orientals have only the cytosolic isozyme, omitting the mitochondrial isozyme. The extremely higher rate of acute alcohol intoxication with Orientals compared to Caucasians is due to the fact of the absence of mitochondrial... & having a molecular mass of 54.5 kda. the aldh2 is purified by proprietary chromatographic techniques. Group: Enzymes. Synonyms: ALDM; ALDHI; ALDH-E2; MGC1806; ALDH2; Aldehyde dehydrogenase mitochondrial; ALDH class 2. Purity: Greater than 90.0% as determined by SDS-PAGE. ALDH2. Mole weight: 54.5 kDa. Activity: > 0.14 units/ml. Stability: Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months. Please prevent freeze-thaw cycles. Appearance: Sterile Filtered clear solution. Source: E. coli. Species: Human. ALDM; ALDHI; ALDH-E2; MGC1806; ALDH2; Aldehyde dehydrogenase mitochondrial; ALDH class 2. Cat No: NATE-0804. | |
| α(2?3,6,8,9) Neuraminidase from Arthrobacter ureafaciens, Recombinant | Neuraminidase is the common name for Acetyl-neuraminyl hydrolase (Sialidase). α2-3,6,8,9 Neuraminidase catalyzes the hydrolysis of all linear and branched non-reducing terminal sialic acid residues from glycoproteins and oligosaccharides. The enzyme releases α2-3 and α2-6 linkages at a slightly higher rate than α2-8 and α2-9 linkages. Group: Enzymes. Synonyms: neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6; α2-3,6,8,9 Neuraminidase A; α2-3,6,8,9 Neuraminidase; α(2?3,6,8,9) Neuraminidase. Enzyme Commission Number: EC 3.2.1.18. CAS No. 9001-67-6. Neuraminidase. Mole weight: 100,000 daltons. Activity: ~316,000 units/mg. Storage: at -20°C. Form: Supplied in: 50 mM NaCl, 20 mM Tris-HCl (pH 7.5 @ 25°C) and 1 mM EDTA. Source: E. coli. Species: Arthrobacter ureafaciens. neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6; α2-3,6,8,9 Neuraminidase A; α2-3,6,8,9 Neuraminidase; α(2?3,6,8,9) Neuraminidase. Cat No: NATE-0758. | |
| angiotensin-converting enzyme 2 | A transmembrane glycoprotein with an extracellular catalytic domain. Angiotensin-converting enzyme 2 functions as a carboxypeptidase, cleaving a single C-terminal residue from a distinct range of substrates. Catalytic efficiency is 400-fold higher with angiotensin II (1-8) as a substrate than with angiotensin I (1-10). Angiotensin-converting enzyme 2 also efficiently hydrolyses des-Arg9-bradykinin, but it does not hydrolyse bradykinin. In peptidase family M2. Group: Enzymes. Synonyms: ACE-2; ACE2; hACE2; angiotensin converting enzyme 2; angiotensin converting enzyme-2; Tmem27. Enzyme Commission Number: EC 3.4.17.23. 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-4076; angiotensin-converting enzyme 2; EC 3.4.17.23; ACE-2; ACE2; hACE2; angiotensin converting enzyme 2; angiotensin converting enzyme-2; Tmem27. Cat No: EXWM-4076. | |
| arogenate dehydrogenase (NADP+) | Arogenate dehydrogenases may utilize NAD+ (EC 1.3.1.43), NADP+ (EC 1.3.1.78), or both (EC 1.3.1.79). NADP+-dependent enzymes usually predominate in higher plants.The enzyme from the cyanobacterium Synechocystis sp. PCC 6803 and the TyrAAT1 isoform of the plant Arabidopsis thaliana cannot use prephenate as a substrate, while the Arabidopsis isoform TyrAAT2 can use it very poorly. Group: Enzymes. Synonyms: arogenic dehydrogenase (ambiguous); pretyrosine dehydrogenase (ambiguous); TyrAAT1; TyrAAT2; TyrAa. Enzyme Commission Number: EC 1.3.1.78. CAS No. 64295-75-6. 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-1347; arogenate dehydrogenase (NADP+); EC 1.3.1.78; 64295-75-6; arogenic dehydrogenase (ambiguous); pretyrosine dehydrogenase (ambiguous); TyrAAT1; TyrAAT2; TyrAa. Cat No: EXWM-1347. | |
| aspartate dehydrogenase | The enzyme is strictly specific for L-aspartate as substrate. Catalyses the first step in NAD biosynthesis from aspartate. The enzyme has a higher affinity for NAD+ than NADP+. Group: Enzymes. Synonyms: NAD-dependent aspartate dehydrogenase; NADH2-dependent aspartate dehydrogenase; NADP+-dependent aspartate dehydrogenase. Enzyme Commission Number: EC 1.4.1.21. CAS No. 37278-97-0. 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-1455; aspartate dehydrogenase; EC 1.4.1.21; 37278-97-0; NAD-dependent aspartate dehydrogenase; NADH2-dependent aspartate dehydrogenase; NADP+-dependent aspartate dehydrogenase. Cat No: EXWM-1455. | |
| aspartate-semialdehyde dehydrogenase | In enzymology, an aspartate-semialdehyde dehydrogenase (EC 1.2.1.11) is an enzyme that is very important in the biosynthesis of amino acids in prokaryotes, fungi, and some higher plants. It forms an early branch point in the metabolic pathway forming lysine, methionine, leucine and isoleucine from aspartate. This pathway also produces diaminopimelate which plays an essential role in bacterial cell wall formation. There is particular interest in ASADH as disabling this enzyme proves fatal to the organism giving rise to the possibility of a new class of antibiotics, fungicides, and herbicides aimed at inhibiting it. Group: Enzymes. Synonyms: aspartate semialdehyde dehydrogenase; aspartic semialdehyde dehydrogenase; L-aspartate-β-semialdehyde:NADP+ oxidoreductase (phosphorylating); aspartic β-semialdehyde dehydrogenase; ASA dehydrogenase. Enzyme Commission Number: EC 1.2.1.11. CAS No. 9000-98-0. 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-1117; aspartate-semialdehyde dehydrogenase; EC 1.2.1.11; 9000-98-0; aspartate semialdehyde dehydrogenase; aspartic semialdehyde dehydrogenase; L-aspartate-β-semialdehyde:NADP+ oxidoreductase (phosphorylating); aspartic β-semialdehyde dehydrogenase; ASA dehydrogenase. Cat No: EXWM-1117. | |
| benzyl alcohol O-benzoyltransferase | The enzyme is involved in volatile benzenoid and benzoic acid biosynthesis. The enzyme from Petunia hybrida also catalyses the formation of 2-phenylethyl benzoate from benzoyl-CoA and 2-phenylethanol. The apparent catalytic efficiency of the enzyme from Petunia hybrida with benzoyl-CoA is almost 6-fold higher than with acetyl-CoA. Group: Enzymes. Synonyms: benzoyl-CoA:benzyl alcohol benzoyltransferase; benzoyl-CoA:benzyl alcohol/phenylethanol benzoyltransferase; benzoyl-coenzyme A:benzyl alcohol benzoyltransferase; benzoyl-coenzyme A:phenylethanol benzoyltransferase. Enzyme Commission Number: EC 2.3.1.196. 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-2139; benzyl alcohol O-benzoyltransferase; EC 2.3.1.196; benzoyl-CoA:benzyl alcohol benzoyltransferase; benzoyl-CoA:benzyl alcohol/phenylethanol benzoyltransferase; benzoyl-coenzyme A:benzyl alcohol benzoyltransferase; benzoyl-coenzyme A:phenylethanol benzoyltransferase. Cat No: EXWM-2139. | |
| β-1,2-mannosidase | The enzyme, characterized from multiple bacterial species, catalyses the hydrolysis of terminal, non-reducing D-mannose residues from β-1,2-mannotriose and β-1,2-mannobiose. The mechanism involves anomeric inversion, resulting in the release of α-D-mannopyranose. Activity with β-1,2-mannotriose or higher oligosaccharides is higher than that with β-1,2-mannobiose. Group: Enzymes. Enzyme Commission Number: EC 3.2.1.197. 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-3881; β-1,2-mannosidase; EC 3.2.1.197. Cat No: EXWM-3881. | |
| β-Amylase (Food Grade) | β-amylase is a kind of high efficiency enzyme obtained from plant by a series of scientific methods. Enzyme system of this product is pure, activity higher, good tolerance to high temperature and no peculiar smel. It is widely used in high maltose syrup, crystalline maltitol etc. Applications: Enzyme for starch sugar. Group: Enzymes. Synonyms: saccharogen amylase; glycogenase; β amylase; 1,4-α-D-glucan maltohydrolase; EC 3.2.1.2; 9000-91-3; Starch Sugar. CAS No. 9000-91-3. β-Amylase. Activity: 700,000u/ml. Storage: Should be stored in a cool place avoiding high temperature. Liquid: 3 months at 25°C, activity remain >90%; 6 months, activity remains >80%. Increase dosage after shelf life. Form: Liquid. saccharogen amylase; glycogenase; β amylase; 1,4-α-D-glucan maltohydrolase; EC 3.2.1.2; 9000-91-3; Starch Sugar. Pack: 25kgs/drum, 1.125kgs/drum. Cat No: SUG-005. | |
| β-cubebene synthase | Isolated from the fungus Coprinus cinereus. The enzyme also forms (+)-Δ-cadinene, β-copaene, (+)-sativene and traces of several other sequiterpenoids. It is found in many higher plants such as Magnolia grandiflora (Southern Magnolia) together with germacrene A. See EC 4.2.3.13, (+)-Δ-cadinene synthase, EC 4.2.3.127, β-copaene synthase, EC 4.2.3.129, (+)-sativene synthase, and EC 4.2.3.23, germacrene A synthase. Group: Enzymes. Synonyms: cop4; Mg25. Enzyme Commission Number: EC 4.2.3.128. 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-5141; β-cubebene synthase; EC 4.2.3.128; cop4; Mg25. Cat No: EXWM-5141. | |
| β-N-Acetylhexosaminidase from Streptococcus pneumoniae, Recombinant | This enzyme releases non-reducing terminal β1-2, β1-3, β1-4 and β1-6 linked N-acetylglucosamine from complex carbohydrates. When incubated with oligosaccharides at low concentrations (<50 mU/ml) the enzyme can differentiate between GlcNAcβ1-2Man, GlcNAcβ1-4Man and GlcNAcβ1-6Man linkages. Under such conditions, the enzyme cleaves essentially only β1-2 linked GlcNAc, with two provisos. Firstly, β1-2 GlcNAc is not hydrolyzed if the mannose to which it is substituted has a substitution at C-6. Thus, the enzyme is useful for the analysis of tri-antennary oligosaccharides. Secondly, if the β-linked mannose of the conserved pentasaccharide core is substituted with a "bisecting" GlcNAc then only the β1-2 linked GlcNAc linked to mannose on the α1-3 arm is cleaved. At higher concentrations of the enzyme, β1-4 and β1-6 linked GlcNAc may also be hydrolyzed. Group: Enzymes. Synonyms: β-N-Acetylhexosaminidase; N-Acetyl-β-D-glucosaminidase, β-N-Acetylglucosaminidase. β-N-Acetylhexosaminidase. Source: E. coli. Species: Streptococcus pneumoniae. β-N-Acetylhexosaminidase; N-Acetyl-β-D-glucosaminidase, β-N-Acetylglucosaminidase. Cat No: NATE-0784. | |
| c[G(2',5')pS-A(3',5')pS], isomer 1 and isomer 2 | c[G(2',5')pS-A(3',5')pS] is an isomeric di-thiophosphate analogue of c[G(2',5')pA(3',5')p], the metazoan cyclic dinucleotide second messenger. It is resistant against the 2'3'-cGAMP hydrolysing enzyme ENPP1, and compared to natural 2'3'-cGAMP, it exhibits higher potency in inducing IFN-β secretion from human THP1 monocytes. Grades: ≥ 95% by HPLC. CAS No. 1638242-56-4 / 1638243-00-1. Molecular formula: C20H24N10O11P2S2 (free acid). Mole weight: 706.6 (free acid). |  |
| cobyrinate a,c-diamide synthase | This enzyme is the first glutamine amidotransferase that participates in the anaerobic (early cobalt insertion) biosynthetic pathway of adenosylcobalamin, and catalyses the ATP-dependent synthesis of cobyrinate a,c-diamide from cobyrinate using either L-glutamine or ammonia as the nitrogen source. It is proposed that the enzyme first catalyses the amidation of the c-carboxylate, and then the intermediate is released into solution and binds to the same catalytic site for the amidation of the a-carboxylate. The Km for ammonia is substantially higher than that for L-glutamine. Group: Enzymes. Synonyms: cobyrinic acid a,c-diamide synthetase; CbiA. Enzyme Commission Number: EC 6.3.5.11. 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-5804; cobyrinate a,c-diamide synthase; EC 6.3.5.11; cobyrinic acid a,c-diamide synthetase; CbiA. Cat No: EXWM-5804. | |
| D-galactarolactone cycloisomerase | The enzyme, characterized from the bacterium Agrobacterium fabrum strain C58, is involved in degradation of D-galacturonate and D-glucuronate. Activity with D-galactaro-1,4-lactone is 4-fold higher than with D-glucaro-1,4-lactone. Group: Enzymes. Synonyms: GCI. Enzyme Commission Number: EC 5.5.1.27. 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-5628; D-galactarolactone cycloisomerase; EC 5.5.1.27; GCI. Cat No: EXWM-5628. | |
| D-glycero-α-D-manno-heptose 1,7-bisphosphate 7-phosphatase | The enzyme is involved in biosynthesis of GDP-D-glycero-α-D-manno-heptose, which is required for assembly of S-layer glycoprotein in some Gram-positive bacteria. The in vitro catalytic efficiency of the enzyme from Bacteroides thetaiotaomicron is 6-fold higher with the α-anomer than with the β-anomer. Group: Enzymes. Synonyms: gmhB (gene name). Enzyme Commission Number: EC 3.1.3.83. 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-3689; D-glycero-α-D-manno-heptose 1,7-bisphosphate 7-phosphatase; EC 3.1.3.83; gmhB (gene name). Cat No: EXWM-3689. | |
| dTDP-4-dehydro-6-deoxyglucose reductase | The enzymes from the Gram-negative bacteria Aggregatibacter actinomycetemcomitans and Escherichia coli O52 are involved in activation of fucose for incorporation into capsular polysaccharide O-antigens. The enzyme from the Gram-positive bacterium Anoxybacillus tepidamans (Geobacillus tepidamans) is involved in activation of fucose for incorporation into the organism's S-layer. The enzyme from Escherichia coli O52 has a higher catalytic efficiency with NADH than with NADPH. Group: Enzymes. Synonyms: dTDP-4-keto-6-deoxyglucose reductase; dTDP-D-fucose:NADP+ oxidoreductase; Fcf1; dTDP-6-deoxy-D-xylo-hex-4-ulopyranose reductase. Enzyme Commission Number: EC 1.1.1.266. 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-0172; dTDP-4-dehydro-6-deoxyglucose reductase; EC 1.1.1.266; dTDP-4-keto-6-deoxyglucose reductase; dTDP-D-fucose:NADP+ oxidoreductase; Fcf1; dTDP-6-deoxy-D-xylo-hex-4-ulopyranose reductase. Cat No: EXWM-0172. | |
| [fructose-bisphosphate aldolase]-lysine N-methyltransferase | The enzyme methylates a conserved lysine in the C-terminal part of higher plant fructose-bisphosphate aldolase (EC 4.1.2.13). The enzyme from pea (Pisum sativum) also methylates Lys-14 in the large subunits of hexadecameric higher plant ribulose-bisphosphate-carboxylase (EC 4.1.1.39), but that from Arabidopsis thaliana does not. Group: Enzymes. Synonyms: rubisco methyltransferase; ribulose-bisphosphate-carboxylase/oxygenase N-methyltransferase; ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit εN-methyltransferase; S-adenosyl-L-methionine:[3-phospho-D-glycerate-carboxy-lyase (dimerizing)]-lysine 6-N-methyltransferase. Enzyme Commission Number: EC 2.1.1.259. 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-1863; [fructose-bisphosphate aldolase]-lysine N-methyltransferase; EC 2.1.1.259; rubisco methyltransferase; ribulose-bisphosphate-carboxylase/oxygenase N-methyltransferase; ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit εN-methyltransferase; S-adenosyl-L-methionine:[3-phospho-D-glycerate-carboxy-lyase (dimerizing)]-lysine 6-N-methyltransferase. Cat No: EXWM-1863. | |
| galactan endo-1,6-β-galactosidase | The enzyme specifically hydrolyses 1,6-β-D-galactooligosaccharides with a degree of polymerization (DP) higher than 3, and their acidic derivatives with 4-O-methylglucosyluronate or glucosyluronate groups at the non-reducing terminals.1,3-β-D- and 1,4-β-D-galactosyl residues cannot act as substrates. The enzyme can also hydrolyse α-L-arabinofuranosidase-treated arabinogalactan protein (AGP) extracted from radish roots. AGPs are thought to be involved in many physiological events, such as cell division, cell expansion and cell death. Group: Enzymes. Synonyms: endo-1,6-β-galactanase. Enzyme Commission Number: EC 3.2.1.164. 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-3846; galactan endo-1,6-β-galactosidase; EC 3.2.1.164; endo-1,6-β-galactanase. Cat No: EXWM-3846. | |
| glucose/galactose 1-dehydrogenase | A zinc protein. The enzyme from the archaeon Picrophilus torridus is involved in glucose and galactose catabolism via the nonphosphorylative variant of the Entner-Doudoroff pathway. It shows 20-fold higher activity with NADP+ compared to NAD+. The oxidation of D-glucose and D-galactose is catalysed at a comparable rate (cf. EC 1.1.1.119, glucose 1-dehydrogenase (NADP+) and EC 1.1.1.120, galactose 1-dehydrogenase (NADP+)). Group: Enzymes. Synonyms: GdhA; dual-specific glucose/galactose dehydrogenase; glucose (galactose) dehydrogenase; glucose/galactose dehydrogenase. Enzyme Commission Number: EC 1.1.1.360. 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-0277; glucose/galactose 1-dehydrogenase; EC 1.1.1.360; GdhA; dual-specific glucose/galactose dehydrogenase; glucose (galactose) dehydrogenase; glucose/galactose dehydrogenase. Cat No: EXWM-0277. | |
| glutamate-prephenate aminotransferase | A pyridoxal-phosphate protein. Aspartate can also act as the amino donor, but more slowly (cf. EC 2.6.1.78, aspartate-prephenate aminotransferase). The enzyme from higher plants shows a marked preference for prephenate as substrate compared to pyruvate, phenylpyruvate or 4-hydroxyphenylpyruvate. Group: Enzymes. Synonyms: prephenate transaminase (ambiguous); PAT (ambiguous); L-glutamate:prephenate aminotransferase. Enzyme Commission Number: EC 2.6.1.79. 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-2919; glutamate-prephenate aminotransferase; EC 2.6.1.79; prephenate transaminase (ambiguous); PAT (ambiguous); L-glutamate:prephenate aminotransferase. Cat No: EXWM-2919. | |
| glutamyl-tRNA reductase | This enzyme forms part of the pathway for the biosynthesis of 5-aminolevulinate from glutamate, known as theC5 pathway.The route shown in the diagram is used in most eubacteria, and in all archaebacteria, algae and plants. However, in the α-proteobacteria, EC 2.3.1.37, 5-aminolevulinate synthase, is used in an alternative route to produce the product 5-aminolevulinate from succinyl-CoA and glycine. This route is found in the mitochondria of fungi and animals, organelles that are considered to be derived from an endosymbiotic α-proteobacterium. Although higher plants do not possess EC 2.3.1.37, the protistan Euglena gracilis possesses both the C5 pathway and EC 2.3.1.37. Group: Enzymes. Enzyme Commission Number: EC 1.2.1.70. CAS No. 119940-26-0. 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-1172; glutamyl-tRNA reductase; EC 1.2.1.70; 119940-26-0. Cat No: EXWM-1172. | |
| glycerol-3-phosphate 2-O-acyltransferase | A membrane-associated enzyme required for suberin or cutin synthesis in plants. Active with a wide range of acyl-CoA substrates (C16:0-C24:0). The enzyme from some sources has much higher activity with ω-oxidized acyl-CoAs. Some enzymes are bifunctional and have an additional phosphatase activity producing sn-2-monoacylglycerols. Group: Enzymes. Synonyms: sn-2-glycerol-3-phosphate O-acyltransferase; glycerol-3-phosphate O-acyltransferase (ambiguous). Enzyme Commission Number: EC 2.3.1.198. 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-2141; glycerol-3-phosphate 2-O-acyltransferase; EC 2.3.1.198; sn-2-glycerol-3-phosphate O-acyltransferase; glycerol-3-phosphate O-acyltransferase (ambiguous). Cat No: EXWM-2141. | |
| glycine N-phenylacetyltransferase | Not identical with EC 2.3.1.13 (glycine N-acyltransferase).This enzyme was purified from bovine liver mitochondria. L-asparagine, L-glutamine and L-arginine are alternative substrates to glycine, but have higher Km values. Group: Enzymes. Synonyms: arylacetyl-CoA N-acyltransferase; arylacetyltransferase; GAT (gene name). Enzyme Commission Number: EC 2.3.1.192. 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-2135; glycine N-phenylacetyltransferase; EC 2.3.1.192; arylacetyl-CoA N-acyltransferase; arylacetyltransferase; GAT (gene name). Cat No: EXWM-2135. | |
| Glycine Oxidase H244K from Bacillus subtilis, recombinant | Glycine oxidase (GO) from Bacillus subtilis (EC 1.4.3.19) is a homotetrameric flavin-dependent oxidoreductase. Each GO monomer is non-covalently bound to flavin adenine dinucleotide. GO catalyzes oxidative deamination of various primary and secondary amines (e.g. glycine, sarcosine, N-ethylglycine) and some D-amino acids (e.g. D -alanine, D -proline, D -valine) to the corresponding α-keto acids and hydrogen peroxide. Primarily, glycine oxidase catalyzes the oxidation of glycine in the biosynthesis of thiamine. The variant H244K shows a higher substrate specificity ratio for glycine versus sarcosine and a 5-fold improved specific activity in comparison to the wild-type. Group: Enzymes. Synonyms: Glycine oxidase; glycine oxygen oxidoreductase (deaminating); GO; EC 1.4.3.19; 39307-16-9. Enzyme Commission Number: EC 1.4.3.19. CAS No. 39307-16-9. Purity: > 90% by SDS-PAGE. Mole weight: 43.1 kDa (1-369 aa, NT His Tag). Activity: 1200 mU/mg. Storage: Store at -20°C. Stable for at least 1 year as supplied. Avoid repeated freeze and thaw cycles. Form: Liquid. Source: E. coli. Species: Bacillus subtilis. Glycine oxidase; glycine oxygen oxidoreductase (deaminating); GO; EC 1.4.3.19; 39307-16-9. Cat No: NATE-1674. | |
| Hemorphin-7 | Hemorphin-7, a hemorphin peptide with antinociceptive and antihypertensive effects, is an endogenous opioid peptide derived from the β-chain of hemoglobin. Hemorphin peptides activates opioid receptors and inhibiting angiotensin-converting enzyme (ACE). The much lower affinity of hemorphin- 7 for μ-receptors as compared to other opioid peptides may be compensated by its much higher plasma concentration, resulting in biological effects of comparable magnitude. Synonyms: H-Tyr-Pro-Trp-Thr-Gln-Arg-Phe-OH; L-tyrosyl-L-prolyl-L-tryptophyl-L-threonyl-L-glutaminyl-L-arginyl-L-phenylalanine; L-Phenylalanine, N-(N2-(N2-(N-(N-(1-L-tyrosyl-L-prolyl)-L-tryptophyl)-L-threonyl)-L-glutaminyl)-L-arginyl)-. Grades: ≥97%. CAS No. 152685-85-3. Molecular formula: C49H64N12O11. Mole weight: 997.11. | |
| Heparinase I from Bacteroides eggerthii, Recombinant | Heparin-degrading lyase that recognizes heparin sulfate proteoglycan as its primary substrate. Heparinase I and III plays vital role in various biological processes: modulate cell-growth factor interactions, cell-lipoprotein interactions, neovascularization. It cleaves highly sulphated polysaccharide chains in presence of 2-O-sulfated α-L-idopyranosyluronic acid and β-D-glucopyranosyluronic acid residues of polysaccharides. Bacteroides heparinase i cloned from bacteroides eggerthii, also called heparin lyase i, is active on heparin and the highly sulfated domains of heparan sulfate. the reaction yields oligosaccharide products containing unsaturated uroni...heparinase i has a much higher rate of cleavage for 2-o sulfated iduronic acid residues. limited digest of porcine mucosal heparin with flavobacterium heparinum heparinase i results in sulfated heparin oligosaccharides structures previously reported. limited digest of porcine mucosal heparin with the bacteroides heparinase i results in heparin oligosaccharides with a lower extent of sulfation as reported. Group: Enzymes. Synonyms: Heparinase; Heparin lyase; Heparin eliminase; Heparin-sulfate lyase; Heparin-sulfate eliminase; Heparitin-sulfate lyase; Heparinase I; Heparinase III; Heparin lyase II; Heparinase II. CAS No. 9025-39-2. Purity: > 95% determined by SDS-PAGE | |
| H-Glu(EDANS)-Pro-Leu-Phe-Ala-Glu-Arg-Lys(DABCYL)-OH | H-Glu(EDANS)-Pro-Leu-Phe-Ala-Glu-Arg-Lys(DABCYL)-OH is an internally quenched substrate for calpain-1 (μ-calpain) with optimal cleavage motifs flanking the scissile bond. The turnover rate of the enzyme to hydrolysis of this FRET substrate based on the PLFAER amino acid sequence is more than 18 times higher than that of EVYGMM derived from the natural substrate α-spectrin cleavage site. Synonyms: N- ({5-[ (2-Aminoethyl) amino]-1-naphthyl}sulfonyl) -L-α -glutamyl-L-prolyl-L-leucyl-L-phenylalanyl-L-alanyl-L-α -glutamyl-L-arginyl-N6- (4-{[4- (dimethylamino) phenyl]diazenyl}benzoyl) -L-lysine. Grades: ≥95%. CAS No. 1914987-47-5. Molecular formula: C72H97N17O16S. Mole weight: 1488.71. | |
| homogentisate geranylgeranyltransferase | Requires Mg2+ for activity. Involved in the biosynthesis of the vitamin E, tocotrienols. While the enzyme from the bacterium Synechocystis PCC 6803 has higher activity with phytyl diphosphate (EC 2.5.1.115, homogentisate phytyltransferase), the enzymes from barley, rice and wheat have only a low activity with that substrate. Group: Enzymes. Synonyms: HGGT; slr1736 (gene name). Enzyme Commission Number: EC 2.5.1.116. 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-2732; homogentisate geranylgeranyltransferase; EC 2.5.1.116; HGGT; slr1736 (gene name). Cat No: EXWM-2732. | |
| indole-3-acetaldehyde oxidase | A hemoprotein. This enzyme is an isoform of aldehyde oxidase (EC 1.2.3.1). It has a preference for aldehydes having an indole-ring structure as substrate. It may play a role in plant hormone biosynthesis as its activity is higher in the auxin-overproducing mutant, super-root1, than in wild-type Arabidopsis thaliana. While (indol-3-yl)acetaldehyde is the preferred substrate, it also oxidizes indole-3-carbaldehyde and acetaldehyde, but more slowly. The enzyme from maize contains FAD, iron and molybdenum. Group: Enzymes. Synonyms: indoleacetaldehyde oxidase; IAAld oxidase; AO1; indole-3-acetaldehyde:oxygen oxidoreductase. Enzyme Commission Number: EC 1.2.3.7. CAS No. 66082-22-2. 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-1214; indole-3-acetaldehyde oxidase; EC 1.2.3.7; 66082-22-2; indoleacetaldehyde oxidase; IAAld oxidase; AO1; indole-3-acetaldehyde:oxygen oxidoreductase. Cat No: EXWM-1214. | |
| L-2-hydroxycarboxylate dehydrogenase [NAD(P)+] | The enzyme from the archaeon Methanocaldococcus jannaschii catalyses the reversible oxidation of (2R)-3-sulfolactate and (S)-malate to 3-sulfopyruvate and oxaloacetate, respectively (note that (2R)-3-sulfolactate has the same stereochemical configuration as (2S)-2-hydroxycarboxylates). The enzyme can use both NADH and NADPH, although activity is higher with NADPH. The oxidation of (2R)-3-sulfolactate was observed only in the presence of NADP+. The same organism also possesses an NAD+-specific enzyme with similar activity, cf. EC 1.1.1.337, L-2-hydroxycarboxylate dehydrogenase (NAD+). Group: Enzymes. Synonyms: MdhII; lactate/malate dehydrogenase. Enzyme Commission Number: EC 1.1.1.375. 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-0293; L-2-hydroxycarboxylate dehydrogenase [NAD(P)+]; EC 1.1.1.375; MdhII; lactate/malate dehydrogenase. Cat No: EXWM-0293. | |
| limonene-1,2-diol dehydrogenase | While the enzyme from the Gram-positive bacterium Rhodococcus erythropolis DCL14 can use both (1S,2S,4R)- and (1R,2R,4S)-menth-8-ene-1,2-diol as substrate, activity is higher with (1S,2S,4R)-menth-8-ene-1,2-diol as substrate. Group: Enzymes. Synonyms: NAD+-dependent limonene-1,2-diol dehydrogenase. Enzyme Commission Number: EC 1.1.1.297. 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-0206; limonene-1,2-diol dehydrogenase; EC 1.1.1.297; NAD+-dependent limonene-1,2-diol dehydrogenase. Cat No: EXWM-0206. | |
| long-chain-3-hydroxyacyl-CoA dehydrogenase | This enzyme was purified from the mitochondrial inner membrane. The enzyme has a preference for long-chain substrates, and activity with a C16 substrate was 6- to 15-fold higher than with a C4 substrate (cf. EC 1.1.1.35 3-hydroxyacyl-CoA dehydrogenase). Group: Enzymes. Synonyms: β-hydroxyacyl-CoA dehydrogenase; long-chain 3-hydroxyacyl coenzyme A dehydrogenase; 3-hydroxyacyl-CoA dehydrogenase; LCHAD. Enzyme Commission Number: EC 1.1.1.211. CAS No. 84177-52-6. 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-0116; long-chain-3-hydroxyacyl-CoA dehydrogenase; EC 1.1.1.211; 84177-52-6; β-hydroxyacyl-CoA dehydrogenase; long-chain 3-hydroxyacyl coenzyme A dehydrogenase; 3-hydroxyacyl-CoA dehydrogenase; LCHAD. Cat No: EXWM-0116. | |
| L-ornithine N5-monooxygenase [NAD(P)H] | A flavoprotein (FAD). The enzyme from the pathogenic fungus Aspergillus fumigatus catalyses a step in the biosynthesis of the siderophores triacetylfusarinine and desferriferricrocin, while the enzyme from the bacterium Kutzneria sp. 744 is involved in the biosynthesis of piperazate, a building block of the kutzneride family of antifungal antibiotics. Activity of the fungal enzyme is higher with NADPH, due to the fact that following the reduction of the flavin, NADP+ (but not NAD+) stabilizes the C4a-hydroperoxyflavin intermediate that oxidizes the substrate. cf. EC 1.14.13.195, L-ornithine N5-monooxygenase (NADPH). Group: Enzymes. Synonyms: SidA (ambiguous). Enzyme Commission Number: EC 1.14.13.196. 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-0796; L-ornithine N5-monooxygenase [NAD(P)H]; EC 1.14.13.196; SidA (ambiguous). Cat No: EXWM-0796. | |
| methylxanthine N1-demethylase | A non-heme iron oxygenase. The enzyme from the bacterium Pseudomonas putida shares an NAD(P)H-FMN reductase subunit with EC 1.14.13.179, methylxanthine N3-demethylase, and has a 5-fold higher activity with NADH than with NADPH. Also demethylate 1-methylxantine with lower efficiency. Forms part of the degradation pathway of methylxanthines. Group: Enzymes. Synonyms: ndmA (gene name). Enzyme Commission Number: EC 1.14.13.178. 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-0776; methylxanthine N1-demethylase; EC 1.14.13.178; ndmA (gene name). Cat No: EXWM-0776. | |
| methylxanthine N3-demethylase | A non-heme iron oxygenase. The enzyme from the bacterium Pseudomonas putida shares an NAD(P)H-FMN reductase subunit with EC 1.14.13.178, methylxanthine N1-demethylase, and has higher activity with NADH than with NADPH. Also demethylates caffeine and theophylline with lower efficiency. Forms part of the degradation pathway of methylxanthines. Group: Enzymes. Synonyms: ndmB (gene name). Enzyme Commission Number: EC 1.14.13.179. 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-0777; methylxanthine N3-demethylase; EC 1.14.13.179; ndmB (gene name). Cat No: EXWM-0777. | |
| Native Aspergillus sp. Lipase (API) | This product is a lipase (TLL) from Thermomyces lanuginosus and it is produced by a submerged fermentation of Aspergillus sp.In opposition to most enzymes, lipases exhibit a wide specificity, recognizing very different substrates. This permits to use a determined lipases as a catalyst for very different reactions, and makes that lipases may be used in pharmaceuticals and drugs production, in energy (biodiesel) or food manufacture, etc. TLL enzyme is a basophilic and noticeably thermostable enzyme. Initially oriented toward the food industry, TLL has been used in many different industrial areas such as modification of fats and oils, production of biodiesel, production of fine chemicals (mainly in enatio/regioselective or specific processes), etc. This product is optimally designed for production of API. Group: Enzymes. Synonyms: EC 3.1.1.3; 9001-62-1; Lipase; Triacylglycerol acylhydrolase; Triacylglycerol lipase; butyrinase; . Enzyme Commission Number: EC 3.1.1.3. CAS No. 9001-62-1. Lipase. Activity: 100,000 unit/g. Appearance: dark brown liquid. Storage: Enzymes gradually lose activity over time depending on storage temperature and humidity. Cool and dry conditions are recommended. At lower temperatures the storage stability is increased. Extended storage and/or adverse conditions, including higher temperatures or high humidity, may lead to a | |
| Native Human Plasmin | Plasmin functions as a key enzyme of the fibrinolytic cascade, and is also important in inflammation processes. Plasmin exhibits preferential cleavage at the carboxyl side of lysine and arginine residues with higher selectivity than trypsin. Converts polymerized fibrin into soluble products. Plasmin functions as a key enzyme of the fibrinolytic cascade, and is also important in inflammation processes. Applications: A complex between plasmin and an inhibitor has been isolated in a study via affinity chromatography from urokinase-activated human plasma. it has also been used in a study to investigate activation of human epithelial sodium channel (enac) by plasmin and chymotrypsin. Group: Enzymes. Synonyms: fibrinase; fibrinolysin; actase; serum tryptase; thrombolysin; plasmin; EC 3.4.21.7; 9001-90-5; PLG. Enzyme Commission Number: EC 3.4.21.7. CAS No. 9001-90-5. PLG. Activity: > 2.0 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing sodium phosphate, mannitol, and NaCl. Source: Human plasma. Species: Human. fibrinase; fibrinolysin; actase; serum tryptase; thrombolysin; plasmin; EC 3.4.21.7; 9001-90-5; PLG. Cat No: NATE-0598. | |
| Native Streptococcus pneumoniae β(1-4)-Galactosidase | The enzyme releases non-reducing terminal β(1-4)-linked galactose from oligosaccharides and glycoproteins. This specificity is only evident at enzyme concentrations < 100mU/ml. At higher concentrations, hydrolysis of β(1-3)-linked galactose occurs. Applications: Due to its high selectivity the enzyme is an extremely useful reagent for the identification of non-reducing terminal β(1-4)-linked galactose residues. as such the enzyme has been extensively used for detailed structural analysis in conjunction with broader specificity bovine testes β-galactosidase or jack bean β-galactosidase. Group: Enzymes. Synonyms: β-galactosidase; beta-gal; β-gal; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat; β-D-galactoside galactohydrolase. β-gal. Mole weight: 220-247 kD. Form: 20 mM Tris-HCl, 25 mM NaCl (pH 7.5). Source: Streptococcus pneumoniae. β(1-4)-Galactosidase; β-galactosidase; beta-gal; β-gal; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat; β-D-galactoside galactohydrolase. Cat No: NATE-0974. | |
| Native Streptomyces griseus Protease | Protease from Streptomyces griseus is a mixture of at least three proteolytic activities including an extracellular serine protease. In general, serine proteases display a wide range of substrate specificities, which are believed to be mediated by an active site composed of one Asp, one His, and a Ser residue in the molecule. This enzyme prefers to hydrolyze peptide bonds on the carboxyl side of glutamic or aspartic acid. Collected from culture broth of s. griseus and purified by successive column procedures. a mixture of at least three proteolytic activities including an extracellular serine protease. in general, serine proteases display a wide range of substrate specifici...de aldehydes and serine proteases. protease is typically used in nucleic acid isolation procedures in incubations of 0.5-3.0 hours supplemented with 0.2% sodium dodecyl sulfate and 10 mm edta. the enzyme from creative enzymes has been used for the digestion and analysis of antithrombin-heparin complexes. it has also been used for the isolation of enzyme-resistant starch. this enzyme is more active at a higher ph range than the known alkaline protease, showing the proteolytic activity even in 0.2n naoh solution. this enzyme is useful for proteolysis of insoluble protein and for structure investigation of protein. Group: Enzymes. Synonyms: Protease; 9036-06-0; Actinase E, Pro | |
| Nicotianamine | Phytosiderophores are produced in higher plants as iron chelating amino acids that promote uptake of iron from soil. Nicotianamine is a metal chelator and phytosiderophore precursor produced in plants that has a role in the uptake, translocation, and intracellular transport of metals.1 Treating lettuce (L. sativa) with a Cu(OH)2-based pesticide raises nicotianamine levels 12- to 27-fold compared to non-pesticide treated plants.2 Nicotianamine also inhibits rabbit angiotensin-coverting enzyme (ACE) (IC50 = 0.26 μM) and human recombinant ACE2 (IC50 = 84 nM).3,4. Group: Biochemicals. Alternative Names: (αS,2S)-α-[[(3S)-3-Amino-3-carboxypropyl]amino]-2-carboxy-1-azetidinebutanoic Acid; [2S-[1[αR*(R*)], 2R*]]-α-[(3-Amino-3-carboxypropyl)amino]-2-carboxy- 1-azetidinebutanoic Acid. Grades: Highly Purified. CAS No. 34441-14-0. Pack Sizes: 1mg. Molecular Formula: C12H21N3O6, Molecular Weight: 303.31. US Biological Life Sciences. |  Worldwide |
| orotate phosphoribosyltransferase | The enzyme from higher eukaryotes also catalyses the reaction listed as EC 4.1.1.23, orotidine-5'-phosphate decarboxylase. Group: Enzymes. Synonyms: orotidylic acid phosphorylase; orotidine-5'-phosphate pyrophosphorylase; OPRTase; orotate phosphoribosyl pyrophosphate transferase; orotic acid phosphoribosyltransferase; orotidine 5'-monophosphate pyrophosphorylase; orotidine monophosphate pyrophosphorylase; orotidine phosphoribosyltransferase; orotidylate phosphoribosyltransferase; orotidylate pyrophosphorylase; orotidylic acid pyrophosphorylase; orotidylic phosphorylase; orotidylic pyrophosphorylase. Enzyme Commission Number: EC 2.4.2.10. CAS No. 9030-25-5. OPRTase. 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-2639; orotate phosphoribosyltransferase; EC 2.4.2.10; 9030-25-5; orotidylic acid phosphorylase; orotidine-5'-phosphate pyrophosphorylase; OPRTase; orotate phosphoribosyl pyrophosphate transferase; orotic acid phosphoribosyltransferase; orotidine 5'-monophosphate pyrophosphorylase; orotidine monophosphate pyrophosphorylase; orotidine phosphoribosyltransferase; orotidylate phosphoribosyltransferase; orotidylate pyrophosphorylase; orotidylic acid pyrophosphorylase; orotidylic phosphorylase; orotidylic pyrophosphorylase. Cat No: EXWM-2639. | |
| orotidine-5'-phosphate decarboxylase | The enzyme from higher eukaryotes is identical with EC 2.4.2.10 orotate phosphoribosyltransferase. Group: Enzymes. Synonyms: orotidine-5'-monophosphate decarboxylase; orotodylate decarboxylase; orotidine phosphate decarboxylase; OMP decarboxylase; orotate monophosphate decarboxylase; orotidine monophosphate decarboxylase; orotidine phosphate decarboxylase; OMP-DC; orotate decarboxylase; orotidine 5'-phosphate decarboxylase; orotidylic decarboxylase; orotidylic acid decarboxylase; orotodylate decarboxylase; ODCase; orotic decarboxylase; orotidine-5'-phosphate carboxy-lyase. Enzyme Commission Number: EC 4.1.1.23. CAS No. 9024-62-8. 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-4768; orotidine-5'-phosphate decarboxylase; EC 4.1.1.23; 9024-62-8; orotidine-5'-monophosphate decarboxylase; orotodylate decarboxylase; orotidine phosphate decarboxylase; OMP decarboxylase; orotate monophosphate decarboxylase; orotidine monophosphate decarboxylase; orotidine phosphate decarboxylase; OMP-DC; orotate decarboxylase; orotidine 5'-phosphate decarboxylase; orotidylic decarboxylase; orotidylic acid decarboxylase; orotodylate decarboxylase; ODCase; orotic decarboxylase; orotidine-5'-phosphate carboxy-lyase. Cat No: EXWM-4768. | |
| OXi-4503 | OXi-4503 is the diphosphate prodrug of the stilbenoid combretastatin A1, originally isolated from the plant Combretum caffrum, with vascular-disrupting and antineoplastic activities. Upon administration, combretastatin A1 diphosphate (CA1P) is dephosphorylated to the active metabolite combretastatin A1 (CA1), which promotes rapid microtubule depolymerization; endothelial cell mitotic arrest and apoptosis, destruction of the tumor vasculature, disruption of tumor blood flow and tumor cell necrosis may ensue. In addition, orthoquinone intermediates, metabolized from combretastatin A1 by oxidative enzymes found to be elevated levels in some tumor types, may bind to tumor cell thiol-specific antioxidant proteins and DNA, and stimulate oxidative stress by enhancing superoxide/hydrogen peroxide production. CA1 binds to tubulin at the same site as colchicine but with higher affinity. Synonyms: OXi4503; OXi 4503; CA1P; tetrasodium [3-methoxy-2-phosphonatooxy-6-[(Z)-2-(3,4,5-trimethoxyphenyl)ethenyl]phenyl] phosphate. Grades: >98%. CAS No. 288847-35-8. Molecular formula: C18H22O12P2. Mole weight: 492.31. | |
| peptidase Do | This serine endopeptidase is essential for the clearance of denatured or aggregated proteins from the inner-membrane and periplasmic space in Escherichia coli. Natural substrates of the enzyme include colicin A lysis protein, pilin subunits and MalS from E. coli. The enzyme has weak peptidase activity with casein and other non-native substrates. The peptidase acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. Molecular chaperones and peptidases control the folded state of proteins by recognizing hydrophobic stretches of polypeptide that become exposed by misfolding or unfolding. They then bind these hydrophobic substrates to prevent aggregation or assist in protein refolding. If attempts at refolding fail, then irreversibly damaged proteins are degraded by peptidases such as this enzyme. Belongs in peptidase family S1C. Group: Enzymes. Synonyms: DegP; DegP protease; HtrA; high temperature requirement protease A; HrtA heat shock p. Enzyme Commission Number: EC 3.4.21.107. CAS No. 161108-11-8. 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-4102; peptidase Do; EC 3.4.21.107; 161108-11-8; DegP; DegP protease; HtrA; high temperature requirement protease A; HrtA heat shock protein; protease Do; Do protease. Cat No: EXWM-4102. | |
| perakine reductase | The biosynthesis of raucaffrinoline from perakine is a side route of the ajmaline biosynthesis pathway. The enzyme is a member of the aldo-keto reductase enzyme superfamily from higher plants. Group: Enzymes. Enzyme Commission Number: EC 1.1.1.317. 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-0229; perakine reductase; EC 1.1.1.317. Cat No: EXWM-0229. | |
| pheophorbidase | This enzyme forms part of the chlorophyll degradation pathway, and is found in higher plants and in algae. In higher plants it participates in de-greening processes such as fruit ripening, leaf senescence, and flowering. The enzyme exists in two forms: type 1 is induced by senescence whereas type 2 is constitutively expressed. The enzyme is highly specific for pheophorbide as substrate (with a preference for pheophorbide a over pheophorbide b) as other chlorophyll derivatives such as protochlorophyllide a, pheophytin a and c, chlorophyll a and b, and chlorophyllide a cannot act as substrates. Another enzyme, called pheophorbide demethoxycarbonylase (PDC),produces pyropheophorbide a from pheophorbide a without forming an intermediate although the precise reaction is not yet known. Group: Enzymes. Synonyms: phedase; PPD. Enzyme Commission Number: EC 3.1.1.82. 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-3511; pheophorbidase; EC 3.1.1.82; phedase; PPD. Cat No: EXWM-3511. | |
| pheophorbide a oxygenase | This enzyme catalyses a key reaction in chlorophyll degradation, which occurs during leaf senescence and fruit ripening in higher plants. The enzyme from Arabidopsis contains a Rieske-type iron-sulfur cluster and requires reduced ferredoxin, which is generated either by NADPH through the pentose-phosphate pathway or by the action of photosystem I. While still attached to this enzyme, the product is rapidly converted into primary fluorescent chlorophyll catabolite by the action of EC 1.3.7.12, red chlorophyll catabolite reductase. Pheophorbide b acts as an inhibitor. In 18O2 labelling experiments, only the aldehyde oxygen is labelled, suggesting that the other oxygen atom may originate from H2O. Group: Enzymes. Synonyms: pheide a monooxygenase; pheide a oxygenase; PaO; PAO. Enzyme Commission Number: EC 1.14.15.17. 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-0942; pheophorbide a oxygenase; EC 1.14.15.17; pheide a monooxygenase; pheide a oxygenase; PaO; PAO. Cat No: EXWM-0942. | |
| phosphatidylcholine-retinol O-acyltransferase | A key enzyme in retinoid metabolism, catalysing the transfer of an acyl group from the sn-1 position of phosphatidylcholine to retinol, forming retinyl esters which are then stored. Recognizes the substrate both in free form and when bound to cellular-retinol-binding-protein, but has higher affinity for the bound form. Can also esterify 11-cis-retinol. Group: Enzymes. Synonyms: lecithin-retinol acyltransferase; phosphatidylcholine:retinol-(cellular-retinol-binding-protein) O-acyltransferase; lecithin:retinol acyltransferase; lecithin-retinol acyltransferase; retinyl ester synthase; LRAT; lecithin retinol acyl transferase. Enzyme Commission Number: EC 2.3.1.135. CAS No. 117444-03-8. 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-2073; phosphatidylcholine-retinol O-acyltransferase; EC 2.3.1.135; 117444-03-8; lecithin-retinol acyltransferase; phosphatidylcholine:retinol-(cellular-retinol-binding-protein) O-acyltransferase; lecithin:retinol acyltransferase; lecithin-retinol acyltransferase; retinyl ester synthase; LRAT; lecithin retinol acyl transferase. Cat No: EXWM-2073. | |
| phosphoglycerate mutase (2,3-diphosphoglycerate-independent) | The enzymes from higher plants, algae, fungi, nematodes, sponges, coelenterates, myriapods, arachnids, echinoderms, archaea and some bacteria (particularly Gram-positive) have maximum activity in the absence of 2,3-bisphospho-D-glycerate. cf. EC 5.4.2.11 phosphoglycerate mutase (2,3-diphosphoglycerate-dependent). The enzyme contains two Mn2+ (or in some species two Co2+ ions). The reaction involves a phosphotransferase reaction to serine followed by transfer back to the glycerate at the other position. Both metal ions are involved in the reaction. Group: Enzymes. Synonyms: cofactor independent phosphoglycerate mutase; 2,3-diphosphoglycerate-independent phosphoglycerate mutase; phosphoglycerate phosphomutase (ambiguous); pho. Enzyme Commission Number: EC 5.4.2.12. 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-5523; phosphoglycerate mutase (2,3-diphosphoglycerate-independent); EC 5.4.2.12; cofactor independent phosphoglycerate mutase; 2,3-diphosphoglycerate-independent phosphoglycerate mutase; phosphoglycerate phosphomutase (ambiguous); phosphoglyceromutase (ambiguous); monophosphoglycerate mutase (ambiguous); monophosphoglyceromutase (ambiguous); GriP mutase (ambiguous); PGA mutase (ambiguous); iPGM; iPGAM; PGAM-i. Cat No: EXWM-5523. | |
| protein O-GlcNAcase | Within higher eukaryotes post-translational modification of protein serines/threonines with N-acetylglucosamine (O-GlcNAc) is dynamic, inducible and abundant, regulating many cellular processes by interfering with protein phosphorylation. EC 2.4.1.255 (protein O-GlcNAc transferase) transfers GlcNAc onto substrate proteins and EC 3.2.1.169 (protein O-GlcNAcase) cleaves GlcNAc from the modified proteins. Group: Enzymes. Synonyms: OGA; glycoside hydrolase O-GlcNAcase; O-GlcNAcase; BtGH84; O-GlcNAc hydrolase. Enzyme Commission Number: EC 3.2.1.169. 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-3851; protein O-GlcNAcase; EC 3.2.1.169; OGA; glycoside hydrolase O-GlcNAcase; O-GlcNAcase; BtGH84; O-GlcNAc hydrolase. Cat No: EXWM-3851. | |
| protein O-GlcNAc transferase | Within higher eukaryotes post-translational modification of protein serines/threonines with N-acetylglucosamine (O-GlcNAc) is dynamic, inducible and abundant, regulating many cellular processes by interfering with protein phosphorylation. EC 2.4.1.255 (protein O-GlcNAc transferase) transfers GlcNAc onto substrate proteins and EC 3.2.1.169 (protein O-GlcNAcase) cleaves GlcNAc from the modified proteins. Group: Enzymes. Synonyms: O-GlcNAc transferase; OGTase; O-linked N-acetylglucosaminyltransferase; uridine diphospho-N-acetylglucosamine:polypeptide β-N-acetylglucosaminyltransferase; protein O-linked β-N-acetylglucosamine transferase. Enzyme Commission Number: EC 2.4.1.255. 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-2485; protein O-GlcNAc transferase; EC 2.4.1.255; O-GlcNAc transferase; OGTase; O-linked N-acetylglucosaminyltransferase; uridine diphospho-N-acetylglucosamine:polypeptide β-N-acetylglucosaminyltransferase; protein O-linked β-N-acetylglucosamine transferase. Cat No: EXWM-2485. | |
| pyrethroid hydrolase | The enzyme is involved in degradation of pyrethroid pesticides. The enzymes from Sphingobium sp., Klebsiella sp. and Aspergillus niger hydrolyse cis-permethrin at approximately equal rate to trans-permethrin. The enzyme from mouse hydrolyses trans-permethrin at a rate about 22-fold higher than cis-permethrin. Group: Enzymes. Synonyms: pyrethroid-hydrolyzing carboxylesterase; pyrethroid-hydrolysing esterase; pyrethroid-hydrolyzing esterase; pyrethroid-selective esterase; pyrethroid-cleaving enzyme; permethrinase; PytH; EstP. Enzyme Commission Number: EC 3.1.1.88. 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-3517; pyrethroid hydrolase; EC 3.1.1.88; pyrethroid-hydrolyzing carboxylesterase; pyrethroid-hydrolysing esterase; pyrethroid-hydrolyzing esterase; pyrethroid-selective esterase; pyrethroid-cleaving enzyme; permethrinase; PytH; EstP. Cat No: EXWM-3517. | |
| red chlorophyll catabolite reductase | The enzyme participates in chlorophyll degradation, which occurs during leaf senescence and fruit ripening in higher plants. The reaction requires reduced ferredoxin, which is generated from NADPH produced either through the pentose-phosphate pathway or by the action of photosystem I. This reaction takes place while red chlorophyll catabolite is still bound to EC 1.14.15.17, pheophorbide a oxygenase. Depending on the plant species used as the source of enzyme, one of two possible C-1 epimers of primary fluorescent chlorophyll catabolite (pFCC), pFCC-1 or pFCC-2, is normally formed, with all genera or species within a family producing the same isomer. After modification and export, pFCCs are eventually imported into the vacuole, where the acidic environment causes their non-enzymic conversion into colourless breakdown products called non-fluorescent chlorophyll catabolites (NCCs). Group: Enzymes. Synonyms: RCCR; RCC reductase; red Chl catabolite reductase. Enzyme Commission Number: EC 1.3.7.12. 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-1393; red chlorophyll catabolite reductase; EC 1.3.7.12; RCCR; RCC reductase; red Chl catabolite reductase. Cat No: EXWM-1393. | |
| [ribulose-bisphosphate carboxylase]-lysine N-methyltransferase | The enzyme catalyses three successive methylations of Lys-14 in the large subunits of hexadecameric higher plant ribulose-bisphosphate-carboxylase (EC 4.1.1.39). Only the three methylated form is observed. The enzyme from pea (Pisum sativum) also three-methylates a specific lysine in the chloroplastic isoforms of fructose-bisphosphate aldolase (EC 4.1.2.13). Group: Enzymes. Synonyms: rubisco methyltransferase; ribulose-bisphosphate-carboxylase/oxygenase N-methyltransferase; ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit εN-methyltransferase; S-adenosyl-L-methionine:[3-phospho-D-glycerate-carboxy-lyase (dimerizing)]-lysine 6-N-methyltransferase; RuBisCO methyltransf. Enzyme Commission Number: EC 2.1.1.127. CAS No. 139171-98-5. 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-1724; [ribulose-bisphosphate carboxylase]-lysine N-methyltransferase; EC 2.1.1.127; 139171-98-5; rubisco methyltransferase; ribulose-bisphosphate-carboxylase/oxygenase N-methyltransferase; ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit εN-methyltransferase; S-adenosyl-L-methionine:[3-phospho-D-glycerate-carboxy-lyase (dimerizing)]-lysine 6-N-methyltransferase; RuBisCO methyltransferase; RuBisCO LSMT. Cat No: EXWM-1724. | |
| sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming) | This enzyme catalyses the final step in the de novo synthesis of tetrahydrobiopterin from GTP. The enzyme, which is found in higher animals and some fungi and bacteria, produces the erythro form of tetrahydrobiopterin. cf. EC 1.1.1.325, sepiapterin reductase (L-threo-7,8-dihydrobiopterin forming). Group: Enzymes. Synonyms: SR. Enzyme Commission Number: EC 1.1.1.153. CAS No. 9059-48-7. 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-0058; sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming); EC 1.1.1.153; 9059-48-7; SR. Cat No: EXWM-0058. | |
| sphingolipid 8-(E)-desaturase | The enzyme, characterized from the yeasts Kluyveromyces lactis and Candida albicans and from the diatom Thalassiosira pseudonana, introduces a trans double bond at the 8-position of sphingoid bases in sphingolipids. The enzyme determines the position of the double bond by its distance from the alcohol end of the sphingoid base, and contains a cytochrome b5 domain that acts as the direct electron donor to the active site of the desaturase. The homologous enzymes from higher plants, EC 1.14.19.29, sphingolipid 8-(E/Z)-desaturase, act on phytosphinganine (4-hydroxysphinganine) and produces a mixture of trans and cis isomers. Group: Enzymes. Synonyms: 8-sphingolipid desaturase (ambiguous); 8 fatty acid desaturase (ambiguous); DELTA8-sphingolipid desaturase (ambiguous). Enzyme Commission Number: EC 1.14.19.18. 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-0980; sphingolipid 8-(E)-desaturase; EC 1.14.19.18; 8-sphingolipid desaturase (ambiguous); 8 fatty acid desaturase (ambiguous); DELTA8-sphingolipid desaturase (ambiguous). Cat No: EXWM-0980. | |
| sphingolipid 8-(E/Z)-desaturase | The enzymes from higher plants convert sphinganine, 4E-sphing-4-enine and phytosphinganine into E/Z-mixtures of Δ8-desaturated products displaying different proportions of geometrical isomers depending on plant species. The nature of the actual desaturase substrate has not yet been studied experimentally. The enzymes contain an N-terminal cytochrome b5 domain that acts as the direct electron donor to the active site of the desaturase. The homologous enzymes from some yeasts and diatoms, EC 1.14.19.18, sphingolipid 8-(E)-desaturase, act on sphing-4-enine ceramides and produce only the trans isomer. Group: Enzymes. Synonyms: 8-sphingolipid desaturase (ambiguous); 8 fatty acid desaturase (ambiguous); DELTA8-sphingolipid desaturase (ambiguous). Enzyme Commission Number: EC 1.14.19.29. 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-0992; sphingolipid 8-(E/Z)-desaturase; EC 1.14.19.29; 8-sphingolipid desaturase (ambiguous); 8 fatty acid desaturase (ambiguous); DELTA8-sphingolipid desaturase (ambiguous). Cat No: EXWM-0992. | |
| sulfofructose kinase | The enzyme, characterized from the bacterium Escherichia coli, is involved in the degradation pathway of sulfoquinovose, the polar headgroup of sulfolipids found in the photosynthetic membranes of all higher plants, mosses, ferns, algae, and most photosynthetic bacteria, as well as the surface layer of some archaea. Group: Enzymes. Synonyms: yihV (gene name). Enzyme Commission Number: EC 2.7.1.184. 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-3016; sulfofructose kinase; EC 2.7.1.184; yihV (gene name). Cat No: EXWM-3016. | |
| sulfofructosephosphate aldolase | The enzyme, characterized from the bacterium Escherichia coli, is involved in the degradation pathway of sulfoquinovose, the polar headgroup of sulfolipids found in the photosynthetic membranes of all higher plants, mosses, ferns, algae, and most photosynthetic bacteria, as well as the surface layer of some archaea. Group: Enzymes. Synonyms: yihT (gene name). Enzyme Commission Number: EC 4.1.2.57. 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-4894; sulfofructosephosphate aldolase; EC 4.1.2.57; yihT (gene name). Cat No: EXWM-4894. | |
| sulfolactaldehyde 3-reductase | The enzyme, characterized from the bacterium Escherichia coli, is involved in the degradation pathway of sulfoquinovose, the polar headgroup of sulfolipids found in the photosynthetic membranes of all higher plants, mosses, ferns, algae, and most photosynthetic bacteria, as well as the surface layer of some archaea. Group: Enzymes. Synonyms: yihU (gene name). Enzyme Commission Number: EC 1.1.1.373. 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-0291; sulfolactaldehyde 3-reductase; EC 1.1.1.373; yihU (gene name). Cat No: EXWM-0291. | |
| sulfoquinovose isomerase | The enzyme, characterized from the bacterium Escherichia coli, is involved in the degradation pathway of sulfoquinovose, the polar headgroup of sulfolipids found in the photosynthetic membranes of all higher plants, mosses, ferns, algae, and most photosynthetic bacteria, as well as the surface layer of some archaea. Group: Enzymes. Synonyms: yihS (gene name). Enzyme Commission Number: EC 5.3.1.31. 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-5471; sulfoquinovose isomerase; EC 5.3.1.31; yihS (gene name). Cat No: EXWM-5471. | |
| Tissue Transglutaminase from Human, Recombinant | Celiac disease is an enteropathy that is characterized by intestinal lesions of variable severity. Tissue-type transglutaminase (tTG) is believed to be the predominant autoantigen for celiac disease and the corresponding autoantibodies show higher sensitivity and specificity than anti-gliadin antibodies. Highly pure recombinant human tTG is now available to replace the traditionally used tTG fraction from guinea pig. Tissue-type transglutaminase antigens have been specifically modified for improved handling: exchange of an active site amino acid eliminates the protein cross-linking activity of the enzyme, while maintaining the native three-dimensional structure and th...tern-blot. Group: Enzymes. Synonyms: Protein-glutamine gamma-glutamyltransferase 2; EC 2.3.2.13; Tissue transglutaminase; TGase C; TGC; TG(C); Transglutaminase-2; TGase-H; TG2; TGM2. Enzyme Commission Number: EC 2.3.2.13. Purity: Greater than 95% as determined by SDS-PAGE. Transglutaminase. Mole weight: 78,018 Da. Stability: Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°Cfor longer periods of time. Avoid multiple freeze-thaw cycles. Source: Sf9 insect cells. Species: Human. Protein-glutamine gamma-glutamyltransferase 2; EC 2.3.2.13; Tissue transglutaminase; TGase C; TGC; TG(C); Transglutaminase-2; TGase-H; TG2; TGM2. Cat No: NATE-0921. | |
| 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase | Involved in the biosynthesis of lysine in bacteria (including cyanobacteria) and higher plants. The 1992 edition of the Enzyme List erroneously gave the name 2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase to this enzyme. Group: Enzymes. Synonyms: tetrahydropicolinate succinylase; tetrahydrodipicolinate N-succinyltransferase; tetrahydrodipicolinate succinyltransferase; succinyl-CoA:tetrahydrodipicolinate N-succinyltransferase; succinyl-CoA:2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase. Enzyme Commission Number: EC 2.3.1.117. CAS No. 88086-34-4. 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-2056; 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase; EC 2.3.1.117; 88086-34-4; tetrahydropicolinate succinylase; tetrahydrodipicolinate N-succinyltransferase; tetrahydrodipicolinate succinyltransferase; succinyl-CoA:tetrahydrodipicolinate N-succinyltransferase; succinyl-CoA:2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase. Cat No: EXWM-2056. | |
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