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| Product | Description | |
|---|---|---|
| Acetyl-Coenzyme A acetyltransferase 2 from Human, Recombinant | ACAT2 enzyme participates in lipid metabolism. ACAT2 takes part in lipoprotein assembly, catalyzing cholesterol esterification in mammalian cells. ACAT2 is an integral membrane protein that localizes to the endoplasmic reticulum of human intestinal cells. ACAT2 deficiency contributes to severe mental retardation and hypotonus. Acat2 recombinant human produced in e. coli is a single, non-glycosylated polypeptide chain containing 433 amino acids (1-397 a.a.) and having a molecular mass of 45.4 kda. the acat2 is fused to 36 amino acid his-tag at n-terminus and purified by proprietary chromatographic techniques. Group: Enzymes. Synonyms: Acetyl-CoA acetyltransferase cytosolic; Cytosolic acetoacetyl-CoA thiolase; ACAT2; Acetyl CoA transferase-like protein; ACAT-2. Purity: Greater than 95.0% as determined by SDS-PAGE. ACAT-2. Mole weight: 45.4 kDa. Stability: ACAT2 Human although stable at 4°C for 1 week, should be stored desiccated below -18°C. Please prevent freeze thaw cycles. Appearance: Sterile Filtered clear solution. Source: E. coli. Species: Human. Acetyl-CoA acetyltransferase cytosolic; Cytosolic acetoacetyl-CoA thiolase; ACAT2; Acetyl CoA transferase-like protein; ACAT-2. Cat No: NATE-0798. |  |
| Acyl-Coenzyme A Dehydrogenase 8 from Human, Recombinant | Acyl CoA dehydrogenase is the enzymeused to catalyzethe first step of β-oxidationin Fatty acid metabolism. Acyl-coenzyme A (CoA) dehydrogenases (ACADs) are a family of mitochondrial enzymes that catalyze the first dehydrogenation step in the bets-oxidation of fatty acyl-CoA derivatives. Several human ACADs exist and all ACADs catalyze the same initial dehydrogenation of the substrate at the beta-carbon atom and require electron transfer flavoprotein as an alectron acceptor. The predicted 415-amino acid ACAD8 protein contains many of the residues conserved in most other ACADs, including an active site glutamic acid residue and residues important for tetramer f...mber 8 mitochondrial; ACAD-8; Isobutyryl-CoA dehydrogenase; Activator-recruited cofactor 42 kDa component; ARC42; FLJ22590. Purity: Greater than 95.0% as determined by SDS-PAGE. ACAD-8. Mole weight: 47.7 kDa. Stability: ACAD8 although stable at 4°C for 1 week, should be stored desiccated 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 clear solution. Source: E. coli. Species: Human. Acyl-CoA dehydrogenase family member 8 mitochondrial; ACAD-8; Isobutyryl-CoA dehydrogenase; Activator-recruited cofactor 42 kDa component; ARC42; FLJ22590. Cat No: NATE-0801. | |
| Biotinylated Transglutaminase from Human, Proenzyme (Zymogen) | This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. Applications: The transglutaminase 3 catalyzes acyl transfer reactions from glutamin residues in proteins or peptides to primary amines, e. g. the formation of ε-(γ-glutamyl) lysine bonds between proteins by transferring the acyl group of a peptide-bound glutamine residue to the primary amino group of a peptide-bound lysine residue. biotinylated transglutaminase 3 may also be used for immunoprecipitation. Group: Enzymes. Synonyms: transglutaminase; EC 2.3.2.13; 80146-85-6; transgl...]. Appearance: Liquid. Storage: Store at -20 °C in working aliquots. Repeated freezing and thawing is not recommended. Form: The transglutaminase is formulated in 10 mM Sodium Phosphate pH 8.0, 15 mM NaCl. Sample contains 50% glycerol. Transglutaminase is a Ca2+-dependent enzyme. Source: E. coli. Species: Human. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase; protein-glutamine γ-glutamyltransferase; TG1. Pack: 100 ug. Cat No: NATE-173 | |
| Creatine Kinase MB Isoenzyme Type-1 from Human, Recombinant | The three isoenzymes (MM, MB, and BB) are found in muscle, cardiac and brain tissues. These recombinant proteins are ideal for calibrating diagnostic instruments and researching neuromuscular diseases. Creatine Kinases can be used for indications in many neuromuscular applications. These disorders include cardiac disease, mitochondrial disorders, inflammatory myopathies, myasthenia, polymyositis, McArdle's disease, NMJ disorders, muscular dystrophy, ALS, hypo and hyperthyroid disorders, central core disease, acid maltase deficiency, myoglobinuria, rhabdomyolysis, motor neuron diseases, rheumatic diseases, and other that create elevated or reduced levels of Creat... in elisa. the ckmbiti is purified by proprietary chromatographic techniques. Group: Enzymes. Synonyms: Creatine Kinase MB Isoenzyme Type-I; Creatine Kinase MB Isoenzyme Type-1; CKMBITI; CKMBI; CKMB; CKMBT1. Purity: Greater than 95.0% as determined by (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. CK. Activity: 500 IU/mg. Stability: CKMBITI although stable at 15°C for 7 days, should be stored below -18°C. Please prevent freeze-thaw cycles. Appearance: Sterile Filtered colourless liquid formulation. Source: Pichia Pastoris. Species: Human. Creatine Kinase MB Isoenzyme Type-I; Creatine Kinase MB Isoenzyme Type-1; CKMBITI; CKMBI; CKMB; CKMBT1. Cat No: NATE-0818. | |
| Creatine Kinase MB Isoenzyme Type-2 from Human, Recombinant | CK-MB Type II possesses the naturally occurring carboxy-terminal amino acid lysine. This occurs during a myocardial infarct (MI or heart attack) when CK-MB Type II is released from damaged heart muscle, and the C-terminal lysine is cleaved in the blood stream, thus creating CK-MB Type I. This difference can be exploited in diagnosis of an MI. Ckmbitii human recombinant produced in pichia pastoris is a glycosylated polypeptide chain having an identical amino acid sequence compared to the native enzyme, purified under non-denaturing conditions and reacts with polyclonal antibodies to mb isoenzyme in elisa. the ckmbitii is purified by proprietary chromatographic techniques. Group: Enzymes. Synonyms: Creatine Kinase MB Isoenzyme Type-II; Creatine Kinase MB Isoenzyme Type-2; CKMBT2; CKMBITII; CKMBII; CKMB. Purity: Greater than 95.0% as determined by (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. CK. Activity: 892 IU/mg. Stability: CKMBITII although stable at 15°C for 7 days, should be stored below -18°C. Please prevent freeze-thaw cycles. Appearance: Sterile Filtered colourless liquid formulation. Source: Pichia Pastoris. Species: Human. Creatine Kinase MB Isoenzyme Type-II; Creatine Kinase MB Isoenzyme Type-2; CKMBT2; CKMBITII; CKMBII; CKMB. Cat No: NATE-0819. | |
| Creatine Kinase MM Isoenzyme Type-1 from Human, Recombinant | Creatine Kinase MM is a cytoplasmic enzyme involved in energy homeostasis and is an important serum marker for myocardial infarction. The encoded protein reversibly catalyzes the transfer of phosphate between ATP and various phosphogens such as creatine phosphate. It acts as a homodimer in striated muscle as well as in other tissues, and as a heterodimer with a similar brain isozyme in heart. The encoded protein is a member of the ATP:guanido phosphotransferase protein family. Ckmt1 human recombinant without c-terminal lysine on both chains produced in pichia pastoris is a glycosylated 47kda polypeptide chain having an identical amino acid sequence compared to t...proprietary chromatographic techniques. Group: Enzymes. Synonyms: Creatine kinase M-type; EC 2.7.3.2; Creatine kinase M chain; M-CK; CKM; CKMM; CKMMITI; CKMMT1. Enzyme Commission Number: EC 2.7.3.2. Purity: Greater than 95.0% as determined by (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. CK. Mole weight: 47kDa. Activity: 537 IU/mg. Stability: CKMT1 although stable at 15°C for 7 days, should be stored below -18°C. Please prevent freeze-thaw cycles. Appearance: Sterile Filtered colourless liquid formulation. Source: Pichia Pastoris. Species: Human. Creatine kinase M-type; EC 2.7.3.2; Creatine kinase M chain; M-CK; CKM; CKMM; CKMMITI; CKMMT1. Cat No: NATE-0820. | |
| Creatine Kinase MM Isoenzyme Type-3 from Human, Recombinant | Creatine Kinase MM is a cytoplasmic enzyme involved in energy homeostasis and is an important serum marker for myocardial infarction. The encoded protein reversibly catalyzes the transfer of phosphate between ATP and various phosphogens such as creatine phosphate. It acts as a homodimer in striated muscle as well as in other tissues, and as a heterodimer with a similar brain isozyme in heart. The encoded protein is a member of the ATP:guanido phosphotransferase protein family. Ckmt3 human recombinant produced in pichia pastoris is a glycosylated polypeptide chain having an identical amino acid sequence compared to the native enzyme, purified under non-denaturing conditions and reacts with polyclonal antibodies to mm isoenzyme in elisa.the ckmt3 is purified by proprietary chromatographic techniques. Group: Enzymes. Synonyms: Creatine kin. Enzyme Commission Number: EC 2.7.3.2. Purity: Greater than 95.0% as determined by (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. CK. Activity: 500 IU/mg. Stability: CKMT3 although stable at 15°C for 7 days, should be stored below -18°C. lease prevent freeze-thaw cycles. Appearance: Sterile Filtered colourless liquid formulation. Source: Pichia Pastoris. Species: Human. Creatine kinase M-type; EC 2.7.3.2; Creatine kinase M chain; M-CK; CKM; CKMM; CKMMITIII; CKMMT3. Cat No: NATE-0821. | |
| 15-Lipoxygenase-2 from human, Recombinant | Two types of 15-lipoxygenase (15-LO) have been discovered and characterized, both of which metabolize arachidonic acid (AA) to produce 15(S)-hydroxyeicosatetraenoic acid (15(S)-HETE). 15-LO-1 oxygenates AA at both C-15 and C-12, whereas 15-LO-2 exclusively oxygenates C-15 of AA. Human 15-LO-2 has a molecular mass of approximately 76 kDa and exhibits approximately 40% identity to the reticulocyte 15-LO-1. Expression of 15-LO-2 appears to be restricted to prostate, lung, skin, and cornea and may play a role in the normal development of these tissues. The protein levels and enzymatic activity of 15-LO-2 are both down-regulated in prostate cancer compared with normal and benign prostate tissues, implicating a possible protective role for 15-LO-2 against tumor formation. Group: Enzymes. Synonyms: Arachidonate 15-lipoxygenase type II; 15-lipoxygenase-2; 15-LO-2; 15-LOX-2; ALOX15B. Enzyme Commission Number: EC 1.13.11.33. Purity: > 95% estimated by SDS-PAGE. Lipoxygenase. Mole weight: 76 kDa. Activity: 234.15 U/ml. Stability: As supplied, 6 months from the QC date provided on the Certificate of Analysis, when stored properly. Storage: at -80°C. Form: PBS, pH 7.4, 1 mM DTT and 20% glycerol. Source: E. coli. Species: Human. Arachidonate 15-lipoxygenase type II; 15-lipoxygenase-2; 15-LO-2; 15-LOX-2; ALOX15B. Cat No: NATE-1248. | |
| 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase | This enzyme is involved in ubiquinone biosynthesis. Ubiquinones from different organisms have a different number of prenyl units (for example, ubiquinone-6 in Saccharomyces, ubiquinone-9 in rat and ubiquinone-10 in human), and thus the natural substrate for the enzymes from different organisms has a different number of prenyl units. However, the enzyme usually shows a low degree of specificity regarding the number of prenyl units. For example, when the COQ5 gene from Saccharomyces cerevisiae is introduced into Escherichia coli, it complements the respiratory deficiency of an ubiE mutant. The bifunctional enzyme from Escherichia coli also catalyses the methylation of demethylmenaquinol-8 (this activity is classified as EC 2.1.1.163). Group: Enzymes. Synonyms: ubiE (gene name, ambiguous). Enzyme Commission Number: EC 2.1.1.201. 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-1802; 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase; EC 2.1.1.201; ubiE (gene name, ambiguous). Cat No: EXWM-1802. | |
| 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase | This enzyme is part of the pathway from urate to (S)-allantoin, which is present in bacteria, plants and animals (but not in humans). Group: Enzymes. Synonyms: OHCU decarboxylase; hpxQ (gene name); PRHOXNB (gene name). Enzyme Commission Number: EC 4.1.1.97. 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-4847; 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase; EC 4.1.1.97; OHCU decarboxylase; hpxQ (gene name); PRHOXNB (gene name). Cat No: EXWM-4847. | |
| 3-demethylubiquinol 3-O-methyltransferase | This enzyme is involved in ubiquinone biosynthesis. Ubiquinones from different organisms have a different number of prenyl units (for example, ubiquinone-6 in Saccharomyces, ubiquinone-9 in rat and ubiquinone-10 in human), and thus the natural substrate for the enzymes from different organisms has a different number of prenyl units. However, the enzyme usually shows a low degree of specificity regarding the number of prenyl units. For example, the human COQ3 enzyme can restore biosynthesis of ubiquinone-6 in coq3 deletion mutants of yeast.The enzymes from yeast, Escherichia coli and rat also catalyse the methylation of 3,4-dihydroxy-5-all-trans-polyprenylbenzoate (a reac...COQ3 (gene name); Coq3 O-methyltransferase; ubiG (gene name, ambiguous). Enzyme Commission Number: EC 2.1.1.64. CAS No. 63774-48-1. 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-1966; 3-demethylubiquinol 3-O-methyltransferase; EC 2.1.1.64; 63774-48-1; 5-demethylubiquinone-9 methyltransferase; OMHMB-methyltransferase; 2-octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone methyltransferase; S-adenosyl-L-methionine:2-octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone-O-methyltransferase; COQ3 (gene name); Coq3 O-methyltransferase; ubiG (gene name, ambiguous). Cat No: EXWM-1966. | |
| 4-Pyridinecarbonitrile | A derivative of Fampridine. Fampridine is a potent convulsant. Uses: 4-cyanopyridine is a reagent for the synthesis of 1-tolyl-5-benzylthiotetrazole and 2-hexylthio-4-pyridinecarbonitrile, an antituberculotics. preparation of the antihypertensive agent pinacidil using the chemoselective and green oxidative rearrangement of an amidine and addition of an amine to a guanidine as the key step. structure-based discovery of human l-xylulose reductase inhibitors from database screening and molecular docking. human l-xylulose reductase (xr) is an enzyme of the glucuronic acid/uronate cycle of glucose metabolism with the possible target for treatment of the long-term complications of diabetes. Synonyms: pyridine-4-carbonitrile. Grades: > 95 %. CAS No. 100-48-1. Molecular formula: C6H4N2. Mole weight: 104.11. |  |
| 5-Hydroxymethylcytidine | 5-Hydroxymethylcytosine is a DNA pyrimidine nitrogen base. It is formed from the DNA base cytosine by adding a methyl group and then a hydroxy group. It is important in epigenetics, because the hydroxymethyl group on the cytosine can possibly switch a gene on and off. It was first seen in bacteriophages in 1952.[1][2] However, in 2009 it was found to be abundant in human and mouse brains,[3] as well as in embryonic stem cells.[4] In mammals, it can be generated by oxidation of 5-methylcytosine, a reaction mediated by the Tet family of enzymes. 5-Hydroxymethylcytidine is a product in DNA hydroxymethylation. The concentrations of 5-Hydroxymethylcytidine in the brain were used to study Alzheimers disease. Group: Biochemicals. Grades: Highly Purified. CAS No. 19235-17-7. Pack Sizes: 25mg. US Biological Life Sciences. |  Worldwide |
| 5-Lipoxygenase from human, Recombinant | Arachidonate 5-lipoxygenase, also known as ALOX5, 5-lipoxygenase, 5-LOX, or 5-LO, is an enzyme that in humans is encoded by the ALOX5 gene. Arachidonate 5-lipoxygenase is a member of the lipoxygenase family of enzymes. It transforms EFAs into leukotrienes and is a current target for pharmaceutical intervention in a number of diseases. Group: Enzymes. Synonyms: Arachidonate 5-lipoxygenase; ALOX5; 5-lipoxygenase; 5-LOX; 5-LO; 5LPG; LOG5. Enzyme Commission Number: EC 1.13.11.34. CAS No. 80619-02-9. Lipoxygenase. Mole weight: 78 kDa. Activity: 1,259.96 U/ml. Stability: As supplied, 6 months from the QC date provided on the Certificate of Analysis, when stored properly. Storage: at -80°C. Form: A solution in 100 mM Tris-HCl, pH 8.0, containing 5 mM EGTA, 1mM CaCl2, and 30% glycerol. Source: S9 insect cells. Species: Human. Arachidonate 5-lipoxygenase; ALOX5; 5-lipoxygenase; 5-LOX; 5-LO; 5LPG; LOG5. Cat No: NATE-1249. | |
| 5-L-Isoleucineangiotensin II | 5-L-Isoleucineangiotensin II is an endogenous potent vasoconstrictor peptide typically generated by the removal of two residues from angiotensin I by angiotensin-converting enzyme (ACE) by binding to both the AT1 and the AT2 receptors. Uses: An endogenous potent vasoconstrictor peptide. Synonyms: 5-Isoleucine-angiotensin II; L-alpha-aspartyl-L-arginyl-L-valyl-L-tyrosyl-L-isoleucyl-L-histidyl-L-prolyl-L-phenylalanine; Angiotensin II human; Human angiotensin II; Hypertensin; H-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-OH; Angiotensin II, 5-L-isoleucine-; Alanine, N-[1-[N-[N-[N-[N-(N2-L-α-aspartyl-L-arginyl)-L-valyl]-L-tyrosyl]-L-isoleucyl]-L-histidyl]-L-prolyl]-3-phenyl-, L-; 5-L-Isoleucine-angiotensin II; L-Phenylalanine, N-[1-[N-[N-[N-[N-(N2-L-α-aspartyl-L-arginyl)-L-valyl]-L-tyrosyl]-L-isoleucyl]-L-histidyl]-L-prolyl]-; [Ile5]-Ang II; [Ile5]-Angiotensin II; Angiotensin 2; Angiotensin II; Angiotensin II (human); Angiotensin II (mouse); Angiotensin II [Ile5]; Asp1-Ile5-angiotensin II; Human angiotensin II; Ileu5-angiotensin II; Isoleucyl5-angiotensin II. Grades: 98%. CAS No. 4474-91-3. Molecular formula: C50H71N13O12. Mole weight: 1046.19. | |
| 6-pyruvoyltetrahydropterin synthase | Catalyses triphosphate elimination and an intramolecular redox reaction in the presence of Mg2+. It has been identified in human liver. This enzyme is involved in the de novo synthesis of tetrahydrobiopterin from GTP, with the other enzymes involved being EC 1.1.1.153 (sepiapterin reductase) and EC 3.5.4.16 (GTP cyclohydrolase I). Group: Enzymes. Synonyms: 2-amino-4-oxo-6-[(1S,2R)-1,2-dihydroxy-3-triphosphooxypropyl]-7,8-dihydroxypteridine triphosphate lyase; 6-[(1S,2R)-1,2-dihydroxy-3-triphosphooxypropyl]-7,8-dihydropterin triphosphate-lyase (6-pyruvoyl-5,6,7,8-tetrahydropterin-forming). Enzyme Commission Number: EC 4.2.3.12. CAS No. 97089-82-2. 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-5132; 6-pyruvoyltetrahydropterin synthase; EC 4.2.3.12; 97089-82-2; 2-amino-4-oxo-6-[(1S,2R)-1,2-dihydroxy-3-triphosphooxypropyl]-7,8-dihydroxypteridine triphosphate lyase; 6-[(1S,2R)-1,2-dihydroxy-3-triphosphooxypropyl]-7,8-dihydropterin triphosphate-lyase (6-pyruvoyl-5,6,7,8-tetrahydropterin-forming). Cat No: EXWM-5132. | |
| Acetolactate Synthase (Crude Enzyme) | The Acetolactate Synthase (ALS) enzyme (also known as acetohydroxy acid synthase, or AHAS) is a protein found in plants and micro-organisms. ALS catalyzes the first step in the synthesis of the branched-chain amino acids (valine, leucine, and isoleucine). It is a human protein of yet unknown function, sharing some sequence similarity with bacterial ALS, and is encoded by the ILVBL gene. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Agriculture; biotechnology; drug development; synthesis; molecular biology. Group: Enzymes. Synonyms: α-acetohydroxy acid synthetase; α-acetohydroxyacid synthase; α-acetolactate synthase; α-acetolactate synthetase; acetohydroxy acid synthetase; acetohydroxyacid synthase; acetolactate pyruvate-lyase (carboxylating); acetolactic synthetase. Enzyme Commission Number: EC 2.2.1.6. CAS No. 9027-45-6. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. α-acetohydroxy acid synthetase; α-acetohydroxyacid synthase; α-acetolactate synthase; α-acetolactate synthetase; acetohydroxy acid synthetase; acetohydroxyacid synthase; acetolactate pyruvate-lyase (carboxylating); acetolactic synthetase. Pack: 100ml. Cat No: NATE-1810. | |
| Active Focal Adhesion Kinase from Human, Recombinant | FAK is a cytoplasmic protein tyrosine kinase which is found concentrated in the focal adhesions that form between cells growing in the presence of extracellular matrix constituents. The encoded protein is a member of the FAK subfamily of protein tyrosine kinases but lacks significant sequence similarity to kinases from other subfamilies. Activation of this gene may be an important early step in cell growth and intracellular signal transduction pathways triggered in response to certain neural peptides or to cell interactions with the extracellular matrix. At least four transcript variants encoding four different isoforms have been found for this gene, but the full-le...Protein-tyrosine kinase 2; FAK; FADK; FAK1; PTK2; FRNK; PPP1R71; p125FAK. Enzyme Commission Number: EC 2.7.10.2. Purity: Greater than 70% as determined by SDS-PAGE. FAK. Mole weight: 146.7 kDa. Activity: 72 nmole of phosphate transferred to poly [Glu,Tyr] 4:1 substrate/minute/mg of total protein at 30°C. Stability: Store at 4°C if entire vial will be used within 1-2 weeks. Store, frozen at -20°C to -80°C for longer periods of time. Avoid multiple freeze-thaw cycles. Source: Baculovirus, SF9 insect cells. Species: Human. Focal adhesion kinase 1; EC 2.7.10.2; FADK 1; pp125FAK; Protein-tyrosine kinase 2; FAK; FADK; FAK1; PTK2; FRNK; PPP1R71; p125FAK. Cat No: NATE-0800. | |
| acylaminoacyl-peptidase | Active at neutral pH. Several variants of this enzyme exist; the human erythrocyte enzyme is relatively specific for removal of N-acetylalanine from peptides. Displays dipeptidyl-peptidase activity on glycyl-peptides, perhaps as a result of mis-recognition of the glycyl residue as an uncharged N-acyl group. Inhibited by diisopropyl fluorophosphate. In peptidase family S9 (prolyl oligopeptidase family). Group: Enzymes. Synonyms: acylamino-acid-releasing enzyme; N-acylpeptide hydrolase; N-formylmethionine (fMet) aminopeptidase; α-N-acylpeptide hydrolase. Enzyme Commission Number: EC 3.4.19.1. CAS No. 73562-30-8. 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-4082; acylaminoacyl-peptidase; EC 3.4.19.1; 73562-30-8; acylamino-acid-releasing enzyme; N-acylpeptide hydrolase; N-formylmethionine (fMet) aminopeptidase; α-N-acylpeptide hydrolase. Cat No: EXWM-4082. | |
| acyloxyacyl hydrolase | The substrate is lipid A on the reducing end of the toxic lipopolysaccharide (LPS) of Salmonella typhimurium and related organisms. It consists of diglucosamine, β-D-GlcN-(1? 6)-D-GlcN, attached by glycosylation on O-6 of its non-reducing residue, phosphorylated on O-4 of this residue and on O-1 of its potentially reducing residue. Both residues carry 3-(acyloxy)acyl groups on N-2 and O-3. The enzyme from human leucocytes detoxifies the lipid by hydrolysing the secondary acyl groups from O-3 of the 3-hydroxyacyl groups on the disaccharide (LPS). It also possesses a wide range of phospholipase and acyltransferase activities [e.g. EC 3.1.1.4 (phospholipase A2), EC 3.1.1.5 (lysophospholipase), EC 3.1.1.32 (phospholipase A1) and EC 3.1.1.52 (phosphatidylinositol deacylase)], hydrolysing diacylglycerol and phosphatidyl compounds, but not triacylglycerols. It has a preference for saturated C12-C16 acyl groups. Group: Enzymes. Enzyme Commission Number: EC 3.1.1.77. CAS No. 110277-64-0. 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-3505; acyloxyacyl hydrolase; EC 3.1.1.77; 110277-64-0. Cat No: EXWM-3505. | |
| Adenosine deaminase Bovine, Recombinant | Adenosine deaminase is an enzyme (EC 3.5.4.4) involved in purine metabolism. It is needed for the breakdown of adenosine from food and for the turnover of nucleic acids in tissues. Present in virtually all mammalian cells, its primary function in Humans is the development and maintenance of the immune system. Protein determined by biuret. Applications: Adenosine deaminase is useful in various molecular biology assays, such as glycerol release assays. adenosine deaminase is a potential target for treatments of combined immunodeficiency disease. Group: Enzymes. Synonyms: ADA; adenosine deaminase; adenosine aminohydrolase; 9026-93-1; EC 3.5.4.4. Enzyme Commission Number: EC 3.5.4.4. CAS No. 9026-93-1. ADA. Mole weight: 32.5-33 kDa. Activity: 60-130 units/mg protein; > 130 units/mg protein; 150-200 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension. Suspension in 3.2 M (NH4)2SO4, 0.01 M potassium phosphate, pH 6.0. Source: E. coli. Species: Bovine. ADA; adenosine deaminase; adenosine aminohydrolase; 9026-93-1; EC 3.5.4.4. Cat No: NATE-0032. | |
| Adenosine deaminase from Human, Recombinant | Adenosine deaminase is an enzyme (EC 3.5.4.4) involved in purine metabolism. It is needed for the breakdown of adenosine from food and for the turnover of nucleic acids in tissues. Present in virtually all mammalian cells, its primary function in Humans is the development and maintenance of the immune system. Applications: Adenosine deaminase (ada) is a key enzyme in purine metabolism and is essential for normal immune function. it is important in the study of immune system diseases such as rheumatoid arthritis. Group: Enzymes. Synonyms: ADA; adenosine deaminase; adenosine aminohydrolase; 9026-93-1; EC 3.5.4.4. Enzyme Commission Number: EC 3.5.4.4. CAS No. 9026-93-1. ADA. Activity: >1 U/mL. Storage: Store at -20°C. Source: E. coli. Species: Human. ADA; adenosine deaminase; adenosine aminohydrolase; 9026-93-1; EC 3.5.4.4. Cat No: NATE-1583. | |
| Adenosine deaminase, Recombinant | Adenosine deaminase is an enzyme (EC 3.5.4.4) involved in purine metabolism. It is needed for the breakdown of adenosine from food and for the turnover of nucleic acids in tissues. Present in virtually all mammalian cells, its primary function in Humans is the development and maintenance of the immune system. Group: Enzymes. Synonyms: ADA; adenosine deaminase; adenosine aminohydrolase; 9026-93-1; EC 3.5.4.4. Enzyme Commission Number: EC 3.5.4.4. CAS No. 9026-93-1. Purity: > 90 %. ADA. Mole weight: About 53kDa (SDS-PAGE). Activity: 200U/mg protein. Appearance: White powder, lyophilized. Storage: Redissolved in 20% glycerol, 4°C, store at -20°C for long-term preservation, Avoid multiple freeze-thaw cycles. Source: E. coli. ADA; adenosine deaminase; adenosine aminohydrolase; 9026-93-1; EC 3.5.4.4. Cat No: NATE-1009. | |
| Adenosine Kinase from Human, Recombinant | E.coli. Applications: Human adenosine kinase is an active and purified, 345-aa short form adk protein (39kda) cloned by rt-pcr amplification of mrna extracted from human hepatoma cells and expressed in e.coli. the sequence of the cloned adk (genbank accession number u50196) was confirmed by dna sequencing (100% identity). Group: Enzymes. Synonyms: ADK. Enzyme Commission Number: EC 2.7.1.20. CAS No. 9027-72-9. Mole weight: 39kDa. Activity: ≥ 0.200 unit/mg protein. Source: Human. Species: ADK. ADK; EC 2.7.1.20. Pack: stable lyophilized form. Cat No: NATE-1740. | |
| adenylyl-sulfate kinase | The human phosphoadenosine-phosphosulfate synthase (PAPSS) system is a bifunctional enzyme (fusion product of two catalytic activities). In a first step, sulfate adenylyltransferase catalyses the formation of adenosine 5'-phosphosulfate (APS) from ATP and inorganic sulfate. The second step is catalysed by the adenylylsulfate kinase portion of 3'-phosphoadenosine 5'-phosphosulfate (PAPS) synthase, which involves the formation of PAPS from enzyme-bound APS and ATP. In contrast, in bacteria, yeast, fungi and plants, the formation of PAPS is carried out by two individual polypeptides, sulfate adenylyltransferase (EC 2.7.7.4) and adenylyl-sulfate kinase (EC 2.7.1.25). Group: Enzymes. Synonyms: adenylylsulfate kinase (phosphorylating); 5'-phosphoadenosine sulfate kinase; adenosine 5'-phosphosulfate kinase; adenosine phosphosulfate kinase; adenosine phosphosulfokinase; . Enzyme Commission Number: EC 2.7.1.25. CAS No. 9012-38-8. 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-3055; adenylyl-sulfate kinase; EC 2.7.1.25; 9012-38-8; adenylylsulfate kinase (phosphorylating); 5'-phosphoadenosine sulfate kinase; adenosine 5'-phosphosulfate kinase; adenosine phosphosulfate kinase; adenosine phosphosulfokinase; adenosine-5'-phosphosulfate-3'-phosphokinase; APS kinase. Cat No: EXWM-3055. | |
| 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. | |
| Alanine-Valine transaminase (Crude Enzyme) | Branched chain aminotransferase is an aminotransferase enzyme which acts upon branched-chain amino acids. It uses largely α-ketoglutarate in forming branched chain α-keto acids and glutamate. The biological function of branched chain aminotransferases (BCAT) is to catalyse the synthesis or degradation of the branched chain amino acids leucine, isoleucine, and valine. In humans, branched chain amino acids are essential and are degraded by BCATs. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Nutrition. Group: Enzymes. Synonyms: Transaminase B; branched-chain amino acid aminotransferase; branched-chain amino acid-glutamate Transaminase; branched-chain aminotransferase; L-branched chain amino acid aminotransferase; glutamate-branched-chain amino acid Transaminase. Enzyme Commission Number: EC 2.6.1.42. CAS No. 9054-65-3. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. Transaminase B; branched-chain amino acid aminotransferase; branched-chain amino acid-glutamate Transaminase; branched-chain aminotransferase; L-branched chain amino acid aminotransferase; glutamate-branched-chain amino acid Transaminase. Pack: 100ml. Cat No: NATE-1821. | |
| Albumin | Albumin. CAS No. 9048-49-1. Product ID: PE-0600. Category: Stabilizer; Therapeutic Agents. Product Keywords: Other Materials; Stabilizers; PE-0600; Albumin; Stabilizer; Therapeutic Agents; ; 9048-49-1. Chemical Name: Serum albumin. Grade: Pharmceutical Excipients. Administration route: Intravenous. Dosage Form: Intravenous injection. Stability and Storage Conditions: Albumin is a protein and is therefore prone to chemical degradation and denaturation under extreme pH conditions, high salt concentrations, heat, enzymes, organic solvents and other chemical agents present. Albumin solution should be stored away from light at 2 ~ 25 ° C, or according to label instructions. Source and Preparation: Human blood albumin is a sterile, pyrogen free serum albumin product obtained from a healthy donor's isolate (source blood, plasma, serum or placenta); The source material must not be tested to contain hepatitis B surface antigen. The production process should ensure that the product is safe and can be used for intravenous injection. Applications: Albumin is mainly used as an excipient in the prescription of injectable drugs, as a stabilizer for proteins and enzymes in the prescription. Albumin is also used in the preparation of microspheres and microcapsules in experimental drug delivery systems. As a stabilizer, albumin is used in protein prescriptions at a low concentration of 0.003%. However, concentrations of 1.to 5% are usually |  |
| 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. | |
| Alkaline Phosphatase Mutein from Bovine, Recombinant | Part of marker enzyme portfolio. In addition to the AP Mutein, recombinant the lyophilizate contains a mixture of proteins from the Pichia system supporting the interference elimination. AP Mutein is lyophilized from a solution containing in NaCl, 0.2 mol/l; ZnCl2, 0.1 mmol/l; Tea, 30 mmol/l; MgCl2, 1 mmol/l; raffinose, 50% (w/v); pH approximately 7.6. Production is done according to the procedures of the active enzyme. Rely on the special design for reducing alkaline phosphatase-related assay interference interactions. Applications: Use alkaline phosphatase mutein (ap mutein) to eliminate human serum derived ap directed assay interferences. Group: Enzymes. Synonyms: ALKP; ALPase; Alk Phos; Alkaline phosphomonoesterase; Glycerophosphatase; Phosphomonoesterase. CAS No. 9001-78-9. ALP. Activity: <10 U/mg protein. Stability: At +2 to +8°C within specification range for 24 months. Appearance: White to yellowish lyophilizate. Source: Pichia pastoris. Species: Calf intestine. Alkaline phosphatase; ALP; ALKP; ALPase; Alk Phos; EC 3.1.3.1; Alkaline phosphomonoesterase; Glycerophosphatase; Phosphomonoesterase. Cat No: NATE-0992. | |
| Alkaline phosphatase (placental) from Human , Recombinant | Alkaline phosphatase (ALP, ALKP, ALPase, Alk Phos) (EC 3.1.3.1) is a hydrolase enzyme responsible for removing phosphate groups from many types of molecules, including nucleotides, proteins, and alkaloids. The process of removing the phosphate group is called dephosphorylation. As the name suggests, alkaline phosphatases are most effective in an alkaline environment. It is sometimes used synonymously as basic phosphatase. Group: Enzymes. Synonyms: ALPP; Alkaline phosphatase Regan isozyme; Placental alkaline phosphatase 1; PLAP-1. Enzyme Commission Number: EC 3.1.3.1. Purity: > 95% by SDS-PAGE. ALP. Mole weight: This protein is fused with 6x His tag at C terminus (23-506 aa) and the protein has a calculated MW of 53.9 kDa (118aa). The protein migrates at 50-70KDa in SDS-PAGE under reducing conditions. Activity: > 2,500 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: Baculovirus. Species: Human. ALPP; Alkaline phosphatase Regan isozyme; Placental alkaline phosphatase 1; PLAP-1; Alkaline phosphatase; ALP; ALKP; ALPase; Alk Phos; EC 3.1.3.1; Alkaline phosphomonoesterase; Glycerophosphatase; Phosphomonoesterase. Cat No: NATE-1664. | |
| α-N-Acetylgalactosaminidase from Chryseobacterium meningosepticum, Recombinant | α-N-acetylgalactosaminidase (EC 3.2.1.49) is a glycoside hydrolase from bacteria and animals, also known as nagalase. The human gene that codes for this enzyme is NAGA. Mutations in this gene and the deficiency in alpha-N-acetylgalactosaminidase activity have been identified as the cause of Schindler disease. Group: Enzymes. Synonyms: EC 3.2.1.49; α-N-acetylgalactosaminidase; Alpha-N-acetylgalactosaminidase; α-acetylgalactosaminidase; N-acetyl-α-D-galactosaminidase; N-acetyl-α-galactosaminidase; α-NAGAL; α-NAGA; α-GalNAcase. α-NAGA. Mole weight: 47 kDa. Storage: at -20°C. Source: E. coli. Species: Chryseobacterium meningosepticum. EC 3.2.1.49; α-N-acetylgalactosaminidase; Alpha-N-acetylgalactosaminidase; α-acetylgalactosaminidase; N-acetyl-α-D-galactosaminidase; N-acetyl-α-galactosaminidase; α-NAGAL; α-NAGA; α-GalNAcase. Cat No: NATE-1259. | |
| (+)-α-Tocopherol | (+)-α-Tocopherol. Synonyms: 2,5,7,8-Tetramethyl-2-(4',8',12'-trimethyltridecyl)-6-chromanol, 5,7,8-Trimethyltocol, D-α-Tocopherol, Vitamin E. CAS No. 59-02-9. Pack Sizes: 10, 100 g in ampule. Product ID: CDC10-0027. Molecular formula: C29H50O2. Category: Antioxidant Cosmetic Chemicals. Product Keywords: Cosmetic Ingredients; Antioxidant Cosmetic Chemicals; (+)-α-Tocopherol; CDC10-0027; 59-02-9; C29H50O2; 2,5,7,8-Tetramethyl-2-(4',8',12'-trimethyltridecyl)-6-chromanol, 5,7,8-Trimethyltocol, D-α-Tocopherol, Vitamin E; 200-412-2; MFCD00072045; 59-02-9. Purity: >97.0%(GC). Color: Clear yellow to red. EC Number: 200-412-2. Physical State: Viscous Liquid. Solubility: Practically insoluble in water, freely soluble in acetone, in anhydrous ethanol, in methylene chloride and in fatty oils. Quality Level: 200. Storage: -20°C. Boiling Point: 200-220 °C/0.1 mmHg (lit.). Melting Point: 4 °C. Density: 0.95 g/mL at 25 °C (lit.). Product Description: α-Tocopherol is synthesized from γ-tocopherol by the action of enzyme γ-tocopherol methyltransferase. It is the major form of Vitamin E in human plasma. It is present in sunflower seed oil. | |
| Altenusin | Altenusin is a a biphenyl derivative with an IC50 value of 4.3±0.3 μM in the TR assay, which is isolated from the endophytic fungus Alternaria. It inhibits Src kinase with an IC50 value of 20 nM. Altenusin inhibits fibrillization of recombinant tau fragments in vitro and phosphorylation of tau in SH-SY5Y cells expressing human P301L mutant tau when used at a concentration of 10 μM. Altenusin is known to have antioxidant properties and to inhibit several enzymes, including myosin light chain kinase, sphingomyelinase, acetylcholinesterase, cFMS kinase, pp60c-SRc kinase and HIV-1 integrase. Synonyms: Alutenusin; MS 341; MS-341; MS341. Grades: ≥98%. CAS No. 31186-12-6. Molecular formula: C15H14O6. Mole weight: 290.27. | |
| amidophosphoribosyltransferase | Amidophosphoribosyltransferase (ATase), also known as glutamine phosphoribosylpyrophosphate amidotransferase (GPAT), is an enzyme responsible for catalyzing the conversion of 5-phosphoribosyl-1-pyrophosphate (PRPP) into 5-phosphoribosyl-1-amine (PRA), using the ammonia group from a glutamine side-chain. This is the committing step in de novo purine synthesis. In humans it is encoded by the PPAT (phosphoribosyl pyrophosphate amidotransferase) gene. ATase is a member of the purine/pyrimidine phosphoribosyltransferase family. Group: Enzymes. Synonyms: phosphoribosyldiphosphate 5-amidotransfer. Enzyme Commission Number: EC 2.4.2.14. CAS No. 9031-82-7. 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-2641; amidophosphoribosyltransferase; EC 2.4.2.14; 9031-82-7; phosphoribosyldiphosphate 5-amidotransferase; glutamine phosphoribosyldiphosphate amidotransferase; α-5-phosphoribosyl-1-pyrophosphate amidotransferase; 5'-phosphoribosylpyrophosphate amidotransferase; 5-phosphoribosyl-1-pyrophosphate amidotransferase; 5-phosphororibosyl-1-pyrophosphate amidotransferase; glutamine 5-phosphoribosylpyrophosphate amidotransferase; glutamine ribosylpyrophosphate 5-phosphate amidotransferase; phosphoribose pyrophosphate amidotransferase; phosphoribosyl pyrophosphate amidotransfe | |
| 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. | |
| Angiotensin II (1-4), human | Angiotensin II (1-4), human is an endogenous peptide produced from ATI by angiotensin-converting-enzyme (ACE). Synonyms: H-DRVY-OH; L-alpha-aspartyl-L-arginyl-L-valyl-L-tyrosine; (S)-3-amino-4-((S)-1-((S)-1-((S)-1-carboxy-2-(4-hydroxyphenyl)ethylamino)-3-methyl-1-oxobutan-2-ylamino)-5-guanidino-1-oxopentan-2-ylamino)-4-oxobutanoic acid; L-α-Aspartyl-N5-(diaminomethylene)-L-ornithyl-L-valyl-L-tyrosine. Grades: ≥95%. CAS No. 52580-29-7. Molecular formula: C24H37N7O8. Mole weight: 551.59. | |
| Anti-oxidant enzyme blend for skin | An anti-oxidant enzyme blend used with conditioning agents to protect skin from super oxide free radicals, UV radiation, environmental pollutants, and cumulative effects of normal skin-cell metabolism. Applications: Cosmetic. Group: Enzymes. Synonyms: Anti-oxidant; Anti-oxidant enzyme blend; for skin; Cosmetic; protect skin; Anti-oxidant enzyme blend for skin. Cosmetic enzymes. Appearance: powder or liquid. Lipase; Cosmetic; lipase-based enzyme blend; breaks down human sebum; breaks down residual oil; human sebum; breaks down human sebum and residual oil; residual oil; human sebum; Lipase-based enzyme blend for cosmetic. Pack: 25kg/paper barrel (powder form), 30kg/polyster barrel (liquid form). Cat No: BODY-2812. | |
| APC 366 trifluoroacetate salt | APC 366 is a mast cell tryptase inhibitor with Ki of 7.1 μM for human recombinant enzyme. It is a selective inhibitor of mast cell tryptase, which has been shown to inhibit antigen-induced early asthmatic response (EAR), late asthmatic response (LAR), and bronchial hyperresponsiveness (BHR) in a sheep model of allergic asthma. APC 366 can reduce maximum contractile response to histamine in isolated bronchial tissue from ovalbumin-sensitized guinea pigs. It can also reduce airway resistance and increases dynamic lung compliance in A. suum antigen-challenged pigs. Grades: ≥95%. Molecular formula: C22H28N6O4·xCF3COOH. Mole weight: 440.50. | |
| aryl-sulfate sulfotransferase | The enzyme, characterized from bacteria that colonize the human and mouse intestine, catalyses the transfer of a sulfate group from a phenol sulfate ester to other phenolic compounds. Activity is enhanced by Mg2+ and Mn2+. Unlike EC 2.8.2.9, tyrosine-ester sulfotransferase and EC 2.8.2.1, aryl sulfotransferase, the enzyme does not act on 3'-phosphoadenylyl sulfate or adenosine 3',5'-bisphosphate.The level of sulfation of polyphenols depends on the positions of the hydroxyl groups. Hydroxy groups of tyrosine residues in peptides such as angiotensin can also act as acceptors. The reaction proceeds according to a ping pong bi bi mechanism. Group: Enzymes. Synonyms: arylsulfate-phenol sulfotransferase; arylsulfotransferase; ASST; arylsulfate sulfotransferase; arylsulfate:phenol sulfotransferase; astA (gene name). Enzyme Commission Number: EC 2.8.2.22. CAS No. 158254-86-5. 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-3381; aryl-sulfate sulfotransferase; EC 2.8.2.22; 158254-86-5; arylsulfate-phenol sulfotransferase; arylsulfotransferase; ASST; arylsulfate sulfotransferase; arylsulfate:phenol sulfotransferase; astA (gene name). Cat No: EXWM-3381. | |
| assemblin | Involved in the breakdown of the scaffold protein during the late stages of assembly of the herpes-virus virion. Inhibited by diisopropyl fluorophosphate. Type example of peptidase family S21. Catalytic residues are His, Ser, His, a combination not known for any other peptidase, and the protein fold also is unique. Known from herpes viruses of several types, cytomegalovirus, Epstein-Barr virus and human herpesvirus 3. Group: Enzymes. Enzyme Commission Number: EC 3.4.21.97. CAS No. 139691-88-6. 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-4189; assemblin; EC 3.4.21.97; 139691-88-6. Cat No: EXWM-4189. | |
| Atazanavir | Atazanavir is a novel and potent azapeptide protease inhibitor that specifically inhibits the human immunodeficiency virus type 1 (HIV-1) protease enzyme with inhibition constant Ki of 66 nmol/L and also inhibits the viral replication of HIV-1 with 50% effective concentration EC50 ranging from 2.6 to 5.3 nmol/L. Atazanavir binds to HIV-1 protease preventing the cleavage of gag and gag-pol polyproteins, which results in the formation of immature virions in HIV-1-infected cells. Atazanavir has a different C-2 symmetric chemical structure and a generally greater antiretroviral potency in various HIV strains compared to other protease inhibitors, including indinavir, nelfinavir, ritonavir, saquinavir and amprenavir. Synonyms: Atazanavir ; Reyataz ; Atazanavir sulfate ; CGP75136 ; CGP75176 ; CGP75355 ; BMS232632 ; CGP 73547 ; CGP 75136 ; CGP 75176 ; CGP 75355 ; CGP-73547 ; CGP-75136 ; CGP-75176 ; CGP-75355 ; BMS 232632 ; BMS-232632 ; BMS-232632-05 ; C413408. Grades: 0.98. CAS No. 198904-31-3. Molecular formula: C38H52N6O7. Mole weight: 704.869. | |
| ATP Citrate Lyase Active from Human, Recombinant | ATP Citrate lyase is an enzyme involved in fatty acid synthesis that generates cytosolic acetyl-CoA and oxaloacetate from Citrate and CoA. ATP Citrate lyase is often upregulated in cancer. Applications: Active human atp citrate lyase is useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling. active human atp citrate lyase has been used in a study to ascertain the nature of the catalytic phosphorylation that initiates the acl reaction, and to identity the active site residues involved. active human atp citrate lyase has also been used in a study to analyze tumor metabolism to reveal mitochondrial glucose oxidation in genetically diverse human glioblastomas. Group: Enzymes. S. Purity: > 90% (SDS-PAGE). ACLY. Mole weight: 147 kDa. Storage: Store at -70°C. Avoid multiple freeze-thaw cycles. Form: Aqueous solution, Formulated in 25 mM Tris-HCl, pH 8.0, 100 mM NaCl, 0.05% Tween-20 and 10% glycerol. Source: Baculovirus. Species: Human. ACLY; ATP-Citrate synthase; ATPCL; CLATP; ATP-citric lyase; ATP:Citrate oxaloacetate-lyase [(pro-S)-CH2COO-->acetyl-CoA] (ATP-dephosphorylating); acetyl-CoA:oxaloacetate acetyltransferase (isomerizing; ADP-phosphorylating); adenosine triphosphate Citrate lyase; Citrate cleavage enzyme; Citrate-ATP lyase; citric cleavage enzyme; ATP Citrate (pro-S)-lyase. Cat No: NATE-0944. | |
| Bakuchiol | Bakuchiol is a phytoestrogen that can be obtained from psoralen seeds. Bakuchiol has been proven to be a non-competitive inhibitor of multiple enzymes, including UDP-glucuronosyltransferase 2B7 ( UGT2B7 ) [2] and human carboxylesterase 2 ( hCE2 ) [3] , with IC 50 s values of 40.9 μM and 7.28 μM, respectively. Bakuchiol exhibits significant research and application potential in areas such as anti-inflammatory [5] , antibacterial [4] , antitumor [1] therapies, as well as drug metabolism regulation. Uses: Scientific research. Group: Natural products. Alternative Names: (S)-(+)-Bakuchiol. CAS No. 10309-37-2. Pack Sizes: 10 mM * 1 mL; 5 mg; 10 mg; 25 mg; 50 mg; 100 mg. Product ID: HY-N0235. |  |
| Benzyl 2-O-[2-(Acetylamino)-2-deoxy-β-D-glucopyranosyl]-α-D-mannopyranoside | A product formed from Benzyl α-D-mannopyranoside by α-3-D-mannoside by the enzyme UDP-GlcNAc:α-3-D-mannoside β1,2-N-acetylglucosaminyltransferase I.2 in humans. Synonyms: GlcNAc(β1-2)Man(α1-)O-benzyl; Phenylmethyl 2-O-[2-(Acetylamino)-2-deoxy-D-glucopyranosyl]-α-D-mannopyranoside. CAS No. 436853-00-8. Molecular formula: C21H31NO11. Mole weight: 473.37. | |
| β (1,4)-Galactosyltransferase from human, Recombinant | β (1,4)-Galactosyltransferase (B4GalT1, EC 2.4.1.38) transfers galactose from a donor substrate, UDP-galactose, to GlcNAcβ1-2Man units on glycoproteins and complex molecules. Group: Enzymes. Synonyms: β (1,4)-Galactosyltransferase; β-GalT; EC 2.4.1.38. Enzyme Commission Number: EC 2.4.1.38. CAS No. 37237-43-7. Galactosyltransferase. Mole weight: 39.5 kDa (by cDNA). Activity: > 12 U/mg. Stability: Enzyme is stable when stored at-20°C to the reported expiration date. Avoid repeated freeze-thaw cycles as this decreases the efficacy of the enzyme. Dispense working aliquots (15 :g) after initial thaw if not utilizing entire quantity. Storage: stored at-20°C Shipped on ice pack for next day delivery. Form: 50 mM Tris HCl 100 mM NaCl (pH 8.4). Source: HEK 293F. Species: Human. β (1,4)-Galactosyltransferase; β-GalT; EC 2.4.1.38. Cat No: NATE-0763. | |
| β-Enolase from Human, Recombinant | Beta-enolase, also known as ENO3, is one of the three enolase isoenzymes found in mammals. This isoenzyme, a homodimer, is found in skeletal muscle cells in the adult. ENO3 play a role in converting phosphoglyceric acid to phosphenolpyruvic acid in the glycolytic pathway. Mutations in its gene can be associated with metabolic myopathies that may result from decreased stability of the enzyme. Recombinant human ENO3 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. Group: Enzymes. Synonyms: 2-phospho-D-glycerate hydro-lyase; Beta-enolase; ENO3; Enolase 3; Muscle-specific enolase. Purity: > 95% (SDS-PAGE). Enolase. Mole weight: 49 kDa. Storage: Store at -70°C. Form: Liquid; 0.5 mg/mL solution in 20 mM Tris-HCl (pH 8.0) containing 1 mM DTT, 20% glycerol and 0.1 mM NaCl. Source: E. coli. Species: Human. 2-phospho-D-glycerate hydro-lyase; Beta-enolase; ENO3; Enolase 3; Muscle-specific enolase. Cat No: NATE-0941. | |
| β-Galactosidase Mutein from E. coli, Recombinant | β-galactosidase, also called beta-gal or β-gal, is a hydrolase enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides. Substrates of different β-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins. Eliminate the interference activity of β-galactosidase directed antibodies: β-galactose mutein reacts with β-galactosidase directed antibodies in the same way as the active β-galactosidase. Applications: Use β-galactosidase mutein to eliminate β-galactosidase directed interferences in immunoassays derived from human sera. Group: Enzymes. Synonyms: β-galactosidase; beta-gal; β-gal; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; trilactase; β-D-galactanase; β-D-galactoside galactohydrolase. CAS No. 9031-11-2. β-gal. Activity: < 0.2 U/mg protein. Stability: At -15 to -25°C within specification range for 24 months. Appearance: White lyophilizate. Source: E. coli. 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-0985. | |
| Bifunctional Chimeras of Glutamylcysteine Synthetase and Glutathione Synthetase (Crude Enzyme) | GSH, and by extension GCL, is critical to cell survival. Nearly every eukaryotic cell, from plants to yeast to humans, expresses a form of the GCL protein for the purpose of synthesizing GSH. To further highlight the critical nature of this enzyme, genetic knockdown of GCL results in embryonic lethality. Furthermore, dysregulation of GCL enzymatic function and activity is known to be involved in the vast majority of human diseases, such as diabetes, Parkinson's disease, Alzheimers disease, COPD, HIV/AIDS, and cancer. This typically involves impaired function leading to decreased GSH biosynthesis, reduced cellular antioxidant capacity, and the in...se forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Agriculture; medicine; synthesis; biotechnology; pharmacology. Group: Enzymes. Enzyme Commission Number: EC 6.3.2.2/ 6.3.2.3. CAS No. 9023-64-7/9023-62-5. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. Bifunctional Chimeras of Glutamylcysteine Synthetase and Glutathione Synthetase; Glutamylcysteine Synthetase; Glutathione Synthetase. Pack: 100ml. Cat No: NATE-1859. | |
| Carbovir Monophosphate | Carbovir Monophosphate (Abacavir - In House Impurity) is a phosphorylated metabolite of the human immunodeficiency virus inhibitor Carbovir. It is converted from Abacavir 5'-phosphate by the enzyme N6-Methyl-AMP aminohydrolase. Uses: A phosphorilated metabolite of the human immunodeficiency virus inhibitor carbovir (c177740). it is converted from abacavir 5'-phosphate by the enzyme n6-methyl-amp aminohydrolase. Synonyms: rel-2-Amino-1,9-dihydro-9-[(1R,4S)-4-[(phosphonooxy)methyl]-2-cyclopenten-1-yl]-6H-purin-6-one; cis-(±)-2-Amino-1,9-dihydro-9-[4-[(phosphonooxy)methyl]-2-cyclopenten-1-yl]-6H-purin-6-one; Carbovir 5'-Phosphate; Abacavir - In House Impurity; Abacavir Impurities. Grades: 98%. CAS No. 144490-73-3. Molecular formula: C11H14N5O5P. Mole weight: 327.23. | |
| Carboxylesterase 1 isoform b from Human, Recombinant | Carboxylesterase 1 is a member of a large multigene carboxylesterase family. These enzymes are responsible for the hydrolysis of ester- and amide-bond-containing drugs such as cocaine and heroin. They also hydrolyze long-chain fatty acid esters and thioesters. This enzyme is known to hydrolyze aromatic and aliphatic esters and is necessary for cellular cholesterol esterification. It may also play a role in detoxification in the lung and/or protection of the central nervous system from ester or amide compounds. Applications: Delivers high catalytic activity, ideal for robust high-throughput screening assays including drug-drug interaction studies, and pharmacokinetic...er: EC 3.1.1.1. CAS No. 9016-18-6. Esterase. Activity: ≥500 units/mg protein. Storage: at -70°C. Form: Liquid. Source: Baculovirus infected BTI insect cells. Species: Human. EC 3.1.1.1; Esterase Isoenzyme 1; 9016-18-6; carboxylesterase; ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyrate esterase; triacetin esterase; carboxyl ester hydrolase; butyrate esterase; methylbutyrase; α-carboxylesterase; propionyl esterase; nonspecific carboxylesterase; esterase D; esterase B; esterase A; serine esterase; carboxyl | |
| Carboxylesterase 1 isoform c from Human, Recombinant | Carboxylesterase 1 is a member of a large multigene carboxylesterase family. These enzymes are responsible for the hydrolysis of ester- and amide-bond-containing drugs such as cocaine and heroin. They also hydrolyze long-chain fatty acid esters and thioesters. This enzyme is known to hydrolyze aromatic and aliphatic esters and is necessary for cellular cholesterol esterification. It may also play a role in detoxification in the lung and/or protection of the central nervous system from ester or amide compounds. Applications: Delivers high catalytic activity, ideal for robust high-throughput screening assays including drug-drug interaction studies, and pharmacokinetic...er: EC 3.1.1.1. CAS No. 9016-18-6. Esterase. Activity: ≥1000 units/mg protein. Storage: at -70°C. Form: Liquid. Source: Baculovirus infected BTI insect cells. Species: Human. EC 3.1.1.1; Esterase Isoenzyme 1; 9016-18-6; carboxylesterase; ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyrate esterase; triacetin esterase; carboxyl ester hydrolase; butyrate esterase; methylbutyrase; α-carboxylesterase; propionyl esterase; nonspecific carboxylesterase; esterase D; esterase B; esterase A; serine esterase; carboxy | |
| caspase-1 | From mammalian monocytes. This enzyme is part of the family of inflammatory caspases, which also includes caspase-4 (EC 3.4.22.57) and caspase-5 (EC 3.4.22.58) in humans and caspase-11 (EC 3.4.22.64), caspase-12, caspase-13 and caspase-14 in mice. Contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation. Cleaves pro-interleukin-1β (pro-IL-1β) to form mature IL-1β, a potent mediator of inflammation. Also activates the proinflammatory cytokine, IL-18, which is also known as interferon-γ-inducing factor. Inhibited by Ac-Tyr-Val-Ala-Asp-CHO. Caspase-11 plays a critical role in the activation of caspase-1 in mi...proteinase; ICE. Enzyme Commission Number: EC 3.4.22.36. CAS No. 122191-40-6. 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-4211; caspase-1; EC 3.4.22.36; 122191-40-6; interleukin 1β-converting enzyme; protease VII; protease A; interleukin 1β precursor proteinase; interleukin 1 converting enzyme; interleukin 1β-converting endopeptidase; interleukin-1β convertase; interleukin-1β converting enzyme; interleukin-1β precursor proteinase; prointerleukin 1β protease; precursor interleukin-1β converting enzyme; pro-interleukin 1β proteinase; ICE. Cat No: EXWM-4211. | |
| caspase-4 | This enzyme is part of the family of inflammatory caspases, which also includes caspase-1 (EC 3.4.22.36) and caspase-5 (EC 3.4.22.58) in humans and caspase-11 (EC 3.4.22.64), caspase-12, caspase-13 and caspase-14 in mice. Contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation. The enzyme is able to cleave itself and the p30 caspase-1 precursor, but, unlike caspase-1, it is very inefficient at generating mature interleukin-1β (IL-1β) from pro-IL-1&beta. Both this enzyme and caspase-5 can cleave pro-caspase-3 to release the small subunit (p12) but not the large subunit (p17). The caspase-1 inhibitor Ac-Tyr-Val-Ala-Asp-CHO can also inhibit this enzyme, but more slowly. Belongs in peptidase family C14. Group: Enzymes. Synonyms: ICErelII; ICErel-II; Ich-2; transcript X; TX; TX protease; caspase 4; CASP-4. Enzyme Commission Number: EC 3.4.22.57. CAS No. 182762-08-9. 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-4232; caspase-4; EC 3.4.22.57; 182762-08-9; ICErelII; ICErel-II; Ich-2; transcript X; TX; TX protease; caspase 4; CASP-4. Cat No: EXWM-4232. | |
| caspase-5 | This enzyme is part of the family of inflammatory caspases, which also includes caspase-1 (EC 3.4.22.36) and caspase-4 (EC 3.4.22.57) in humans and caspase-11 (EC 3.4.22.64), caspase-12, caspase-13 and caspase-14 in mice. Contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation. The enzyme is able to cleave itself and the p30 caspase-1 precursor, but is very inefficient at generating mature interleukin-1β (IL-1β) from pro-IL-1&beta. Both this enzyme and caspase-4 can cleave pro-caspase-3 to release the small subunit (p12) but not the large subunit (p17). Unlike caspase-4, this enzyme can be induced by lipopolysaccharide. Belongs in peptidase family C14. Group: Enzymes. Synonyms: ICErel-III; Ich-3; ICH-3 protease; transcript Y; TY; CASP-5. Enzyme Commission Number: EC 3.4.22.58. CAS No. 192465-11-5. 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-4233; caspase-5; EC 3.4.22.58; 192465-11-5; ICErel-III; Ich-3; ICH-3 protease; transcript Y; TY; CASP-5. Cat No: EXWM-4233. | |
| Caspase-9 (Active) from Human, Recombinant | The expressed caspase-9 spontaneously undergoes autoprocessing to yield the subunits characteristic of the native enzyme. Active enzyme purified from E. coliThis product is useful in screening caspase inhibitors for pharmaceutical Applications. Group: Enzymes. Synonyms: CASP9; APAF-3; APAF3; ICE-LAP6; MCH6; PPP1R56; Caspase-9 (Active); Caspase-9. Purity: 90% (SDS-PAGE). Caspase 9. Activity: ~400 units/mg. Appearance: Lyophilized Powder. Storage: -80°C. Source: E. coli. Species: Human. CASP9; APAF-3; APAF3; ICE-LAP6; MCH6; PPP1R56; Caspase-9 (Active); Caspase-9. Cat No: NATE-0816. | |
| CATALASE | CATALASE. Synonyms: equilase;Catalase-Agarose;H2O2 oxidoreductase;Catalase from A. niger, lyophil.;Catalase from bovine liver, lyophil.;Catalase-peroxidase;CATALASE FROM BOVINE LIVERCA.65000 U/MG PROTEIN SUSPENSION;CATALASE FROM ASPERGILLUSNIGER CA.2000 U/MG LYOPH.SALT-FREE. CAS No. 9001-5-2. Pack Sizes: 1 kg. Product ID: CDF4-0037. Molecular formula: C9H10O3. Category: Enzyme Preparations. Product Keywords: Food Ingredients; Enzyme Preparations; CATALASE; CDF4-0037; 9001-05-2; C9H10O3; 232-577-1; 9001-05-2. Purity: 0.99. Color: Deep Brown. EC Number: 232-577-1. Physical State: Suspension. Storage: -20°C. Product Description: CAT (catalase) is an endogenous antioxidant enzyme, thus conferring protection to cells against damage by ROS (reactive oxygen species). In humans, this gene is localized to chromosome 11p13, which is composed of 12 introns and 13 exons. | |
| Cathepsin D from Human, recombinant | Cathepsin D is a lysosomal aspartyl protease composed of a protein dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. It is an estrogen-regulated protein associated with tissue breakdown. Levels of cathepsin D have been positively correlated with recurring breast cancers of both node negative and node positive types. Additionally cathepsin D has been associated with amyloid formation in Alzheimer's plaques. Cathepsin D is produced initially as a pre-pro-enzyme which gets transported to lysosomes via endosomes in most cell types. In endosomes, it gets proteolyzed by unidentified proteases by removal of the pro-peptide to generate...e cathepsins B and L generates mature, active double-chain Cathepsin D. Group: Enzymes. Synonyms: CTSD; 9025-26-7; EC 3.4.23.5; CLN10; CPSD; HEL-S-130P; Procathepsin D. Enzyme Commission Number: EC 3.4.23.5. CAS No. 9025-26-7. Purity: > 80% by SDS-PAGE. CTSD. Mole weight: 45.1 kDa. Activity: >100 pmol/min/mg. Storage: Store at -20°C. Stable for at least 6 months as supplied. Reconstitute to 1 mg/ml in sterile water, store at -80°C in aliquots and use within 6 months after reconstitution. Avoid repeated freeze-thaw cycles. Form: Freeze-Dried. Source: E. coli. Species: Human. CTSD; cathepsin D; 9025-26-7; EC 3.4.23.5; CLN10; CPSD; HEL-S-130P; Procathepsin D. Cat No: NATE-1707. | |
| Cathepsin S from Human, recombinant | Cathepsin S (CTSS) is a lysosomal cysteine protease of the papain family and may participate in the degradation of antigenic proteins to peptides for presentation on MHC class II molecules. CTSS is synthesized as inactive precursor of 331 amino acids consisting of a 15-aa signal peptide, a propeptide of 99 aa, and a mature polypeptide of 217 aa. It is activated in the lysosomes by a proteolytic cleavage of the propeptide. The deduced amino acid sequence contains only one potential N-glycosylation site located in the propeptide. Compared with the abundant cathepsins B, L and H, cathepsin S shows a restricted tissue distribution, with highest levels in spleen, heart, and lung...l compartment, and is implicated in the pathogenesis of Alzheimers disease and Down Syndrome. Group: Enzymes. Synonyms: CTSS; cathepsin S; EC 3.4.22.27; FLJ50259; MGC3886. Enzyme Commission Number: EC 3.4.22.27. CAS No. 71965-46-3. Purity: > 90% by SDS-PAGE. CTSS. Mole weight: 23.9 kDa (115-331 aa). Activity: >2000 mU/mg. Storage: Stable for at least 1 year as supplied. Briefly spin down the vial and reconstitute in 50 mM sodium acetate, 100 mM NaCl (pH 5.5) to 0.1-1 mg/ml and store at -80°C. Avoid repeated freeze and thaw cycles. Form: Lyophilized from proprietary buffer. Source: E. coli. Species: Human. CTSS; cathepsin S; EC 3.4.22.27; FLJ50259; MGC3886. Cat No: NATE-1702. | |
| CAY10502 | Phospholipases A2 (PLA2s) are enzymes that cleave fatty acid in position two of phospholipids, hydrolyzing the bond between the second fatty acid "tail" and the glycerol molecule. It catalyzes the hydrolysis of phospholipids at the sn-2 position leading to the production of lysophospholipids and free fatty acids. CAY10502 is a potent Calcium-dependent cytosolic PLA2 (cPLA2α) inhibitor with IC50 value of 4.3 nM for the purified enzyme from human platelets. It inhibits arachidonic acid mobilization from A23187-stimulated or TPA-stimulated human platelets with IC50 values of 570 and 0.9 nM, respectively. Synonyms: CAY10502; CAY-10502. Grades: ≥98% (mixture of isomers). CAS No. 888320-29-4. Molecular formula: C30H37NO7. Mole weight: 523.6. | |
| CAY10566 | Stearoyl-CoA desaturase (SCD) is an endoplasmic reticulum enzyme that catalyzes the rate-limiting step in the formation of monounsaturated fatty acids (MUFAs), specifically oleate and palmitoleate from stearoyl-CoA and palmitoyl-CoA. CAY10566 is a potent and selective inhibitor with IC50s of 4.5 and 26 nM in mouse and human enzymatic assays, respectively. It also shows excellent cellular activity in blocking the conversion of saturated long-chain fatty acid-CoAs (LCFA-CoAs) to monounsaturated LCFA-CoAs in HepG2 cells. Synonyms: CAY 10566; CAY-10566. Grades: ≥98%. CAS No. 944808-88-2. Molecular formula: C18H17ClFN5O2. Mole weight: 389.8. | |
| CAY10606 | Arachidonate 5-lipoxygenase, also known as ALOX5, 5-lipoxygenase, 5-LOX, or 5-LO, is a non-heme iron-containing enzyme that in humans is encoded by the ALOX5 gene. 5-LO initiates the synthesis of leukotrienes (LTs) from arachidonic acid, primarily in certain leukocyte populations. CAY10606 is a potent, reversible inhibitor of 5-LO, both in cell-free assays (IC50 = 86 nM) and in intact neutrophils (IC50 = 230 nM). It prevents the production of LTs in whole blood, whether 5-LO is activated with the calcium ionophore A23187 with IC50 of 1.6 μM. Synonyms: CAY 10606; CAY-10606. Grades: ≥98%. CAS No. 1159576-98-3. Molecular formula: C22H18ClNO3. Mole weight: 379.8. | |
| CAY10649 | Arachidonate 5-lipoxygenase, also known as ALOX5, 5-lipoxygenase, 5-LOX, or 5-LO, is a non-heme iron-containing enzyme that in humans is encoded by the ALOX5 gene. 5-LO initiates the synthesis of (LTs) from arachidonic acid, primarily in certain leukocyte populations. CAY10649 is a thiazolinone compound that demonstrates direct inhibition of 5-lipoxygenase (5-LO) product formation in intact polymorphonuclear leukocytes (PMNL) with IC50 of 0.28 μM. Synonyms: CAY 10649; CAY-10649. Grades: ≥98%. CAS No. 1272519-89-7. Molecular formula: C17H12ClNO2S. Mole weight: 329.8. | |
| Cepharanthine | Cepharanthine is a natural product that can be isolated from the plant Stephania?cephalantha?Hayata. Cepharanthine has anti-severe acute respiratory syndrome coronavirus 2 (anti-SARS-CoV-2) activities. Cepharanthine has good effective in suppressing viral proliferation (half maximal (50%) inhibitory concentration ( IC 50 ) and 90% inhibitory concentration ( IC 90 ) values of 1.90 and 4.46?μM [1]. Cepharanthine can also effectively reverses P-gp-mediated multidrug resistance in K562 cells and increase enhances the sensitivity of anticancer agents in xenograft mice model [2] [3]. Cepharanthine shows inhibitory effects of human liver cytochrome P450 enzymes CYP3A4, CYP2E1 and CYP2C9. Cepharanthine has antitumor, anti-inflammatory and antinociceptive effects [4] [5] [6] [7] [8]. Uses: Scientific research. Group: Natural products. CAS No. 481-49-2. Pack Sizes: 10 mM * 1 mL; 50 mg. Product ID: HY-N6972. | |
| 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). | |
| coagulation factor VIIa | Formed from the precursor factor VII. The cattle enzyme is more readily inhibited by diisopropyl fluorophosphate than the human. In peptidase family S1 (trypsin family). Group: Enzymes. Synonyms: blood-coagulation factor VIIa; activated blood coagulation factor VII. Enzyme Commission Number: EC 3.4.21.21. CAS No. 65312-43-8. 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-4121; coagulation factor VIIa; EC 3.4.21.21; 65312-43-8; blood-coagulation factor VIIa; activated blood coagulation factor VII. Cat No: EXWM-4121. | |
| Coenzyme Q10 | Coenzyme Q10 is an electron transport chain component of the mitochondria, which assists proton and electron transfer across the inner mitochondrial membrane. Studies indicate that Coenzyme Q10 can protect human endothelial cells from oxidative damage by modulating the nitric oxide pathway. In addition, Coenzyme Q10 inhibits LDL oxidation, a major process in the development of atherosclerosis. Coenzyme Q10 is known to suppress the down regulation of NOS3 (endothelial nitric oxide synthase, eNOS) and up-regulation of NOS2 (inducible nitric oxide synthase, iNOS). As a result of its ability to bind Ca2+, Coenzyme Q10 can transport this cation across artificial biomimetic membranes. Applications: A mitochondrial transporter chain component. Group: Coenzymes. Synonyms: CoQ10; Ubidecarenone; Ubiquinone-10; Q-10. CAS No. 303-98-0. Purity: ≥98%. Mole weight: 863.34. Appearance: Powder. Form: Solid. CoQ10; Ubidecarenone; Ubiquinone-10; Q-10; Coenzyme Q10; 303-98-0. Cat No: COEC-013. | |
| Collagenase AF-1 GMP Grade | Collagenase AF-1 GMP Grade, often in combination with Neutral Protease AF GMP Grade, is suitable for the dissociation of sensitive cells from several tissues, such as pancreas, liver and dental pulp. It has been shown to be highly effective for the isolation of islets of Langerhans from human pancreas intended for transplantation. Applications: Collagenase af-1 gmp grade is suitable for cell isolation from several tissue types intended for clinical applications. it is often used in combination with neutral protease af gmp grade. Group: Enzymes. Synonyms: Collagenase AF-1; Collagenase; Collagenase AF-1 GMP; Collagenase GMP. Enzyme Commission Number: EC 3.4.24.3. CAS No. 9001-12-1. Collagenase. Activity: ≥ 3.00 U/mg. Storage: 2 to 8 °C. Form: Lyophilized powder. Source: Clostridium histolyticum. Collagenase AF-1; Collagenase; Collagenase AF-1 GMP; Collagenase GMP. Cat No: NATE-1919. | |
| Collagenase NB 6 from Clostridium histolyticum (GMP Grade) | Collagenases from Clostridium histolyticum are proteolytic enzymes that cleave peptide bonds in the triple helical collagen molecule of human or animal tissue in situ. For this reason collagenases are widely used for isolation of various cell types by tissue dissociation. Applications: Collagenase nb 6 gmp grade is suitable for cell isolation from various tissue types intended for clinical applications. if a research or sterile product is required, collagenase nb 4 standard grade or collagenase nb 5 sterile grade, respectively, are recommended. both products have comparable enzymatic activities to collagenase nb 6 gmp grade. Group: Enzymes. Synonyms: Collagenase NB 6; Collagenase NB; Collagenase. Enzyme Commission Number: EC 3.4.24.3. CAS No. 9001-12-1. Collagenase. Mole weight: 70 000 - 120 000 (collagenases). Activity: ≥ 0.100 U/mg. Storage: 2 to 8 °C. Form: Lyophilized powder. Source: Clostridium histolyticum. Collagenase NB 6; Collagenase NB; Collagenase. Cat No: NATE-1918. | |
| Collagenase/Neutral Protease Blend (GMP Grade) | NATE-1917 is an avian and mammalian tissue-free Collagenase and neutral protease enzyme blend produced under GMP quality conditions. Applications: Nate-1917 is specifically designed for stem cell isolation from human and other adipose tissue with following advantages:o a single, sterile, ready-to-use vial containing both collagenase and neutral protease can digest up to 280g of adipose tissue with best-in-class gmp quality and shelf life of up to 72 months.o currently included in ide applications approved by the u.s. fda for alopecia, chronic heart failure, hamstring injuries, osteoarthritis of the knee, and hand manifestations of scleroderma.o research protocols are a...sociation of nucleated cells from adipose tissue.o produced using avian and mammalian tissue-free raw materials, aseptic processes and sterile filtration under gmp guidelines to assure the lowest levels of impurities and stringent quality standards. Group: Enzymes. Synonyms: Collagenase/Neutral Protease Blend; GMP, Collagenase/Neutral Protease Blend; Collagenase; Neutral Protease; GMP. Collagenase. Stability: 48 months at -15 to -25° C. Appearance: White lyophilizate. Source: Clostridium histolyticum/Bacillus polymyxa. Collagenase/Neutral Protease Blend; GMP, Collagenase/Neutral Protease Blend; Collagenase; Neutral Protease; GMP. Pack: 1 vial, 35 mg. Cat No: NATE-1917. | |
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