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| Product | Description | |
|---|---|---|
| 13-hydroxydocosanoate 13-β-glucosyltransferase | 13-β-D-Glucosyloxydocosanoate can also act as acceptor, leading to the formation by Candida bogoriensis of the extracellular glycolipid, hydroxydocosanoate sophoroside diacetate. Group: Enzymes. Synonyms: 13-glucosyloxydocosanoate 2'-β-glucosyltransferase; UDP-glucose:13-hydroxydocosanoic acid glucosyltransferase; uridine diphosphoglucose-hydroxydocosanoate glucosyltransferase; UDP-glucose-13-hydroxydocosanoate glucosyltransferase. Enzyme Commission Number: EC 2.4.1.158. CAS No. 70457-13-5. 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-2382; 13-hydroxydocosanoate 13-β-glucosyltransferase; EC 2.4.1.158; 70457-13-5; 13-glucosyloxydocosanoate 2'-β-glucosyltransferase; UDP-glucose:13-hydroxydocosanoic acid glucosyltransferase; uridine diphosphoglucose-hydroxydocosanoate glucosyltransferase; UDP-glucose-13-hydroxydocosanoate glucosyltransferase. Cat No: EXWM-2382. |  |
| 2-?Propyl-1,?3-?Dioxolane-?2-?acetic Acid | 2-?Propyl-1,?3-?Dioxolane-?2-?acetic Acid is an intermediate in synthesizing N-(Ketocaproyl)-L-homoserine Lactone (K180750), an autoinducer of P. fischeri luciferase. A specific genetic regulator that is unrelated to at least one of the enzyme systems that it induces, and it acts after excretion and accumulation in the extracellular medium. Group: Biochemicals. Grades: Highly Purified. CAS No. 5735-99-9. Pack Sizes: 500mg, 1g. Molecular Formula: C8H14O4. US Biological Life Sciences. |  Worldwide |
| 2-Propyl-N-[(3S)-tetrahydro-2-oxo-3-furanyl]-1,3-dioxolane-2-acetamide | 2-Propyl-N-[(3S)-tetrahydro-2-oxo-3-furanyl]-1,3-dioxolane-2-acetamide is an intermediate in synthesizing N-(Ketocaproyl)-L-homoserine Lactone (K180750), an autoinducer of P. fischeri luciferase. A specific genetic regulator that is unrelated to at least one of the enzyme systems that it induces, and it acts after excretion and accumulation in the extracellular medium. Group: Biochemicals. Grades: Highly Purified. CAS No. 1083287-09-5. Pack Sizes: 250mg, 500mg. Molecular Formula: C12H19NO5. US Biological Life Sciences. | Worldwide |
| 3-deoxy-D-glycero-D-galacto-nononate 9-phosphatase | The enzyme, characterized from the bacterium Bacteroides thetaiotaomicron, is part of the biosynthesis pathway of the sialic acid 3-deoxy-D-glycero-D-galacto-nononate (KDN). KDN is abundant in extracellular glycoconjugates of lower vertebrates such as fish and amphibians, but is also found in the capsular polysaccharides of bacteria that belong to the Bacteroides genus. Group: Enzymes. Synonyms: 2-keto-3-deoxy-D-glycero-D-galactonononate-9-phosphate phosphatase. Enzyme Commission Number: EC 3.1.3.103. 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-3612; 3-deoxy-D-glycero-D-galacto-nononate 9-phosphatase; EC 3.1.3.103; 2-keto-3-deoxy-D-glycero-D-galactonononate-9-phosphate phosphatase. Cat No: EXWM-3612. | |
| 3-deoxy-D-glycero-D-galacto-nononate 9-phosphate synthase | The enzyme participates in the biosynthesis of the sialic acid 3-deoxy-D-glycero-D-galacto-nononate (KDN). The human sialic acid synthase (EC 2.5.1.57) is also able to catalyse the reaction. KDN is abundant in extracellular glycoconjugates of lower vertebrates such as fish and amphibians, but is also found in the capsular polysaccharides of bacteria that belong to the Bacteroides genus. Group: Enzymes. Synonyms: 2-keto-3-deoxy-D-glycero-D-galacto-9-phosphonononic acid synthase; KDN 9-P synthase. Enzyme Commission Number: EC 2.5.1.132. 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-2748; 3-deoxy-D-glycero-D-galacto-nononate 9-phosphate synthase; EC 2.5.1.132; 2-keto-3-deoxy-D-glycero-D-galacto-9-phosphonononic acid synthase; KDN 9-P synthase. Cat No: EXWM-2748. | |
| 3-deoxy-D-glycero-D-galacto-nononate cytidylyltransferase | The enzyme is part of the biosynthesis pathway of the sialic acid 3-deoxy-D-glycero-D-galacto-nononate (KDN). KDN is abundant in extracellular glycoconjugates of lower vertebrates such as fish and amphibians, but is also found in the capsular polysaccharides of bacteria that belong to the Bacteroides genus. Group: Enzymes. Enzyme Commission Number: EC 2.7.7.92. 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-3306; 3-deoxy-D-glycero-D-galacto-nononate cytidylyltransferase; EC 2.7.7.92. Cat No: EXWM-3306. | |
| 5'-Nucleotidase from Human, Recombinant | 5'-nucleotidase is an extracellular enzyme that converts nucleoside-5'-monophosphates to nucleosides with a substrate preference of AMP. Native 5'-nucleotidase is a GPI-anchored protein whose exporession is upregulated by hypoxia. 5'-nucleotidase has many functions in vivo including the generation of extracellular adenosine. 5'-Nucleotidase has various clinical significances. It is a key molecule in the regulation of cancer cells proliferation, migration and invasion in vitro tumor angiogenesis, and tumor immune escape in vivo. Due to this important role, the enzyme is a potential target for cancer research.1 It is also involved in salvage of extracellular nucleotides and...Enzyme Commission Number: EC 3.1.3.5. CAS No. 9027-73-0. Purity: >90% (SDS-PAGE). AMPase. Mole weight: ~61 kDa by SDS-PAGE (reducing). Activity: >15 U/mg. Storage: Store at -70°C. Form: Supplied as a solution containing Tris, NaCl, CaCl2, and 20% glycerol. Source: CHO cells. Species: Human. uridine 5'-nucleotidase; 5'-adenylic phosphatase; adenosine 5'-phosphatase; AMP phosphatase; adenosine monophosphatase; 5'-mononucleotidase; AMPase; UMPase; snake venom 5'-nucleotidase; thimidine monophosphate nucleotidase; 5'-AMPase; 5'-AMP nucleotidase; AMP phosphohydrolase; IMP 5'-nucleotidase; EC 3.1.3.5; CD73; NT5E; ecto-5'-nucleotidase. Pack: vial of 6-12 μg. Cat No: NATE-0795. | |
| 8-[(6-Amino)hexyl]-amino-adenosine-2',5'-bisphosphate - DY-480XL | DY-480XL, a biomedicine product specialized in biochemical studies, offers an intricate solution to understanding the dynamics of enzymatic interactions and signaling pathways. As a fluorescent analog of 2',5'-ADP, this product boasts the capability to study complex enzyme activities such as adenylate cyclase and cyclic nucleotide phosphodiesterase. Furthermore, it can delve into the intricate signaling pathways activated by extracellular receptors, which induce G protein-coupled pathways. The product's versatility renders it invaluable in the oncology research sphere, with its potential applications ranging from breast, ovarian to colon cancer. Synonyms: 8-[(6-Amino)hexyl]-amino-adenosine-2',5'-bisphosphate, labeled with DY 480XL, Triethylammonium salt. Grades: ≥ 95% by HPLC. Molecular formula: C42H57N9O16P2S (free acid). Mole weight: 1037.97 (free acid). |  |
| Ac-Glu-Asp(EDANS)-Lys-Pro-Ile-Leu-Phe-Phe-Arg-Leu-Gly-Lys(DABCYL)-Glu-NH2 | Ac-Glu-Asp(EDANS)-Lys-Pro-Ile-Leu-Phe-Phe-Arg-Leu-Gly-Lys(DABCYL)-Glu-NH2 is a sensitive fluorescent (FRET) peptide substrate for cathepsin D. This enzyme degrades extracellular matrix components and may promote the spread of tumor cells. High levels of active cathepsin D were found in senile plaques in the brains of Alzheimer's patients. Synonyms: L-α-Glutamine, N-acetyl-L-α-glutamyl-N-[2-[(5-sulfo-1-naphthalenyl)amino]ethyl]-L-asparaginyl-L-lysyl-L-prolyl-L-isoleucyl-L-leucyl-L-phenylalanyl-L-phenylalanyl-L-arginyl-L-leucylglycyl-N6-[4-[[4-(dimethylamino)phenyl]azo]benzoyl]-L-lysyl-; N-Acetyl-L-α -glutamyl-N-{2-[ (5-sulfo-1-naphthyl) amino]ethyl}-L-asparaginyl-L-lysyl-L-prolyl-L-isoleucyl-L-leucyl-L-phenylalanyl-L-phenylalanyl-L-arginyl-L-leucylglycyl-N6- (4-{[4- (dimethylamino) phenyl]diazenyl}benzoyl) -L-lysyl-L-α -glutamine. Grades: ≥95%. CAS No. 400716-78-1. Molecular formula: C104H146N24O23S. Mole weight: 2132.52. | |
| 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. | |
| 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. | |
| apyrase | Apyrases are active against both di- and triphosphate nucleotides (NDPs and NTPs) and hydrolyse NTPs to nucleotide monophosphates (NMPs) in two distinct successive phosphate-releasing steps, with NDPs as intermediates. They differ from ATPases, which specifically hydrolyse ATP, by hydrolysing both ATP and ADP. The eukaryotic enzymes requires Ca2+, but Mg2+ can substitute. Most of the ecto-ATPases that occur on the cell surface and hydrolyse extracellular nucleotides belong to this enzyme family. Group: Enzymes. Synonyms: ATP-diphosphatase; adenosine diphosphatase; ADPase; ATP diphosphohydrolase [ambiguous]. Enzyme Commission Number: EC 3.6.1.5. CAS No. 9000-95-7. Apyrase. 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-4623; apyrase; EC 3.6.1.5; 9000-95-7; ATP-diphosphatase; adenosine diphosphatase; ADPase; ATP diphosphohydrolase [ambiguous]. Cat No: EXWM-4623. | |
| Ascorbate oxidase, Cucurbit sp. | Ascorbate oxidase, Cucurbit sp., also known as vitamin C oxidase, is a REDOX enzyme involved in the regulation of extracellular matrix. Ascorbate oxidase catalyzes the reaction of ascorbic acid and oxygen to produce dehydroascorbic acid [1] [2]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: ASO, Cucurbit sp. CAS No. 9029-44-1. Pack Sizes: 100 U; 500 U; 1000 U. Product ID: HY-P2742. |  |
| β-1,4-Galactosyltransferase from Neisseria meningitides, Recombinant | β-1,4-Galactosyl Transferase catalyzes the transfer of galactose from UDP-galactose to the terminal N-acetylglucosamine residues on elongating oligosaccharide chains. It is also considered to be a biosynthetic enzyme of the Golgi apparatus. β-1,4-Galactosyl Transferase can also be found on the cell surface functioning as a cell-adhesion molecule during various cellular interactions by binding to N-acetylglucosamine containing oligosaccharide substrates or ligands in the extracellular matrix. Group: Enzymes. Synonyms: lactose synthase; UDP-α-D-galactose-glucose galactosyltransferase; N-acetyllactosamine synthase; uridine diphosphogalactose-glucose galactosyltransferase; lactose synthetase; UDP-galactose:D-glucose 4-β-D-galactotransferase; UDP-galactose:D-glucose 4-&b. Enzyme Commission Number: EC 2.4.1.90. CAS No. 9054-94-8. Purity: min 95% by SDS-PAGE. Galactosyltransferase. Mole weight: 34 kDa. Source: E. coli. Species: Neisseria meningitides. lactose synthase; UDP-α-D-galactose-glucose galactosyltransferase; N-acetyllactosamine synthase; uridine diphosphogalactose-glucose galactosyltransferase; lactose synthetase; UDP-galactose:D-glucose 4-β-D-galactotransferase; UDP-galactose:D-glucose 4-β-D-galactosyltransferase; β-1,4-Galactosyl Transferase. Cat No: NATE-1478. | |
| Chitinase from Aspergillus niger (food grade) | Chitinase is an extracellular enzyme complex that degrades chitin. Chitin is degraded to N-acetyl-D-glucosamine in 2 enzymatic reactions. Group: Enzymes. Synonyms: Chitinase; chitodextrinase; 1,4-β-poly-N-acetylglucosaminidase; poly-β-glucosaminidase; β-1,4-poly-N-acetyl glucosamidinase; poly[1,4-(N-acetyl-β-D-glucosaminide)] glycanohydrolase; (1->4)-2-acetamido-2-deoxy-beta-D-glucan glycanohydrolase; EC 3.2.1.14. Enzyme Commission Number: EC 3.2.1.14. CAS No. 9001-6-3. Chitinase. Activity: 200U/g min. Stability: 1 year when properly stored. Storage: STORED HUMIDITY PROTECTED (RH LESS THAN 60) AT TEMPERATURE BELOW 25°C. Form: Light-brown Powder. Source: Aspergillus niger. Chitinase; chitodextrinase; 1,4-β-poly-N-acetylglucosaminidase; poly-β-glucosaminidase; β-1,4-poly-N-acetyl glucosamidinase; poly[1,4-(N-acetyl-β-D-glucosaminide)] glycanohydrolase; (1->4)-2-acetamido-2-deoxy-beta-D-glucan glycanohydrolase; EC 3.2.1.14. Cat No: DIS-1010. | |
| Chitinase from Clostridium thermocellum, Recombinant | Chitinase is an extracellular enzyme complex that degrades chitin and has a molecular mass of approximately 30 kDa. Chitin is degraded to N-acetyl-D-glucosamine in 2 enzymatic reactions. Firstly, chitobiose units are removed from chitin by chitodextrinase-chitinase. The second reaction involves N-acetyl-glucosaminidase-chitobiase, which cleaves the disaccharide to its monomer subunits (that comprise of N-acetyl-D-glucosamine). Group: Enzymes. Synonyms: Chitinase; chitodextrinase; 1,4-β-poly-N-acetylglucosaminidase; poly-β-glucosaminidase; β-1,4-poly-N-acetyl glucosamidinase; poly[1,4-(N-acetyl-β-D-glucosaminide)] glycanohydrolase; (1->4)-2-acetamido-2-deoxy-beta-D-glucan glycanohydrolase; EC 3.2.1.14. Enzyme Commission Number: EC 3.2.1.14. Purity: > 80 % as judged by SDS-PAGE. Chitinase. Mole weight: 43927.1 Da. Activity: 25 U/mg. Storage: Store at -20°C (shipped at room temperature). Form: Glycerol/buffer solution. Source: Clostridium thermocellum ATCC 27405. Chitinase; chitodextrinase; 1,4-β-poly-N-acetylglucosaminidase; poly-β-glucosaminidase; β-1,4-poly-N-acetyl glucosamidinase; poly[1,4-(N-acetyl-β-D-glucosaminide)] glycanohydrolase; (1->4)-2-acetamido-2-deoxy-beta-D-glucan glycanohydrolase; EC 3.2.1.14. Cat No: NATE-1201. | |
| cyanophycinase | The enzyme is highly specific for the branched polypeptide cyanophycin and does not hydrolyse poly-L-aspartate or poly-L-arginine. A serine-type exopeptidase that belongs in peptidase family S51. Group: Enzymes. Synonyms: cyanophycin degrading enzyme; β-Asp-Arg hydrolysing enzyme; CGPase; CphB; CphE; cyanophycin granule polypeptidase; extracellular CGPase. Enzyme Commission Number: EC 3.4.15.6. CAS No. 131554-16-0. 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-4056; cyanophycinase; EC 3.4.15.6; 131554-16-0; cyanophycin degrading enzyme; β-Asp-Arg hydrolysing enzyme; CGPase; CphB; CphE; cyanophycin granule polypeptidase; extracellular CGPase. Cat No: EXWM-4056. | |
| Deoxyribonuclease B, Recombinant | Deoxyribonuclease B (DNAse B) is one of several extracellular enzymes produced by group A beta-hemolytic streptococci. Since DNAse B is produced extensively by group A serotypes and is not produced in significant amounts by other serological groups (C and G), anti-DNAse B is a reliable streptococcal antibody test for both skin and throat infections. Applications: Used in the formulation of anti-dnase b assays which are used in the diagnosis of group a streptococcal based illnesses. Group: Enzymes. Synonyms: DNASE1; deoxyribonuclease I; deoxyribonuclease-1; DNase I; 9003-98-9; EC 3.1.21.1; pancreatic DNase; DNase; thymonuclease, dornase; dornava; dornavac; pancreatic deoxyribonuclease; pancreatic dornase; deoxyribonuclease (pancreatic); pancreatic DNas. Enzyme Commission Number: EC 3.1.21.1. Purity: > 97%. Mole weight: 21 - 31kD. Form: Frozen liquid. Source: Escherichia coli. DNASE1; deoxyribonuclease I; deoxyribonuclease-1; DNase I; 9003-98-9; EC 3.1.21.1; pancreatic DNase; DNase; thymonuclease, dornase; dornava; dornavac; pancreatic deoxyribonuclease; pancreatic dornase; deoxyribonuclease (pancreatic); pancreatic DNase; DNAase; deoxyribonucleic phosphatase; alkaline deoxyribonuclease; alkaline DNase; endodeoxyribonuclease I; DNA depolymerase; Escherichia coli endonuclease I; deoxyribonuclease A; DNA endonuclease; DNA nuclease. Cat No: NATE-1153. | |
| DNase I, Bovine pancreas | DNase I (EC 3.1.21.1) is an enzyme that degrade DNA, it plays a key role in the cleavage of extracellular DNA is crucial for limiting the inflammatory response and maintaining homeostasis. Exogenous deoxyribonuclease shows beneficial effects in inflammatory diseases and cancer [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: DNase. CAS No. 9003-98-9. Pack Sizes: 50 mg; 100 mg. Product ID: HY-108882. | |
| envelysin | A glycoprotein from various members of the class Echinoidea. Extracellular enzyme requiring Ca2+. In peptidase family M10 (interstitial collagenase family). Group: Enzymes. Synonyms: sea-urchin-hatching proteinase; hatching enzyme; chorionase; chorion-digesting proteinase; chymostrypsin; sea urchin embryo hatching enzyme. Enzyme Commission Number: EC 3.4.24.12. CAS No. 50812-13-0. 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-4293; envelysin; EC 3.4.24.12; 50812-13-0; sea-urchin-hatching proteinase; hatching enzyme; chorionase; chorion-digesting proteinase; chymostrypsin; sea urchin embryo hatching enzyme. Cat No: EXWM-4293. | |
| fragilysin | Thought to be a cause of diarrhoea in animals and humans. Hydrolyses extracellular matrix proteins, and disrupts tight junctions of intestinal epithelial cells. Also degrades intracellular, cytoskeletal proteins actin, myosin and others. In peptidase family M10 (interstitial collagenase family). Group: Enzymes. Synonyms: Bacteroides fragilis (entero)toxin. Enzyme Commission Number: EC 3.4.24.74. CAS No. 188596-63-6. 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-4358; fragilysin; EC 3.4.24.74; 188596-63-6; Bacteroides fragilis (entero)toxin. Cat No: EXWM-4358. | |
| Galactose Oxidase from Dactylium dendroides, Recombinant | Galactose oxidase is an extracellular copper-containing enzyme, secreted by the deuteromycete fungus Dactylium dendroides. It catalyzes the oxidation of a range of primary alcohols, including D-galactose, to the corresponding aldehyde, with reduction of oxygen to hydrogen peroxide. Galactose oxidase (gao) is a recombinantly expressed copper activated enzyme derived from dactylium dendroides that catalyzes the stereospecific oxidation of d-isomer primary alcohols to aldehydes and hydrogen peroxide (1-3). gao has a range of substrates that include d-galactose and polysaccharides, glycolipids, or glycoproteins with d-galactose at their non-reducing end. Applications: Gao has been shown to be useful in a number of biotechnology and medical applications which include monitoring of galactose in blood and urine, paper strengthening additives, test strips for cancer diagnosis, biosensors and lactose detection, dental care and hair coloring and waving. Group: Enzymes. Synonyms: EC 1.1.3.9; D-galactose o. CAS No. 9028-79-9. Purity: >95% by SDS-PAGE. Galactose Oxidase. Mole weight: 68.9 kDa (Calculated). Activity: >1750 U/mg. Stability: 3-6 months. Storage: 2-8°C. Avoid multiple freeze/thaw cycles. Source: Dactylium dendroides. EC 1.1.3.9; D-galactose oxidase; β-galactose oxidase; 9028-79-9; Galactose Oxidase. Cat No: NATE-1288. | |
| γ-glutamyltransferase | The mammlian enzyme is part of the cell antioxidant defense mechanism. It initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracelular GSH levels. The protein also has EC 3.4.19.13 (glutathione hydrolase) activity. The enzyme consists of two chains that are created by the proteolytic cleavage of a single precursor polypeptide. The N-terminal L-threonine of the C-terminal subunit functions as the active site for both the cleavage and the hydrolysis reactions. Group: Enzymes. Synonyms: glutamyl transpeptidase; α-glutamyl transpeptidase; γ-glutamyl peptidyltransferase; γ-glutamyl transpeptidase (ambiguous); γ-GPT; γ-GT; γ-GTP; L-γ-glutamyl. Enzyme Commission Number: EC 2.3.2.2. CAS No. 9046-27-9. γ-GT. 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-2293; γ-glutamyltransferase; EC 2.3.2.2; 9046-27-9; glutamyl transpeptidase; α-glutamyl transpeptidase; γ-glutamyl peptidyltransferase; γ-glutamyl transpeptidase (ambiguous); γ-GPT; γ-GT; γ-GTP; L-γ-glutamyl transpeptidase; L-γ-glutamyltransferase; L-glutamyltransferase; GGT (ambiguous); γ-glutamyltranspeptidase (ambiguous). Cat No: EXWM-2293. | |
| glycoprotein-mannosyl O6-kinase | In humans this phosphorylated trisaccharide is attached to an L-threonine residue of α-dystroglycan, an extracellular peripheral glycoprotein that acts as a receptor for extracellular matrix proteins containing laminin-G domains, and is important for its activity. Group: Enzymes. Synonyms: SGK196; protein O-mannose kinase. Enzyme Commission Number: EC 2.7.1.183. 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-3015; glycoprotein-mannosyl O6-kinase; EC 2.7.1.183; SGK196; protein O-mannose kinase. Cat No: EXWM-3015. | |
| Heparanase 1 from Human, Recombinant | Heparanase is an endo β-D-glucuronidase, which degrades heparan sulfate side chains of heparan sulfate proteoglycans (HSPGs) in the extracellular matrix. Heparanase plays an important role in ECM degradation, facilitating the migration and extravasation of tumor cells and inflammatory leukocytes. Upon degradation, heparanase releases growth factors and cytokines that stimulate cell proliferation and chemotaxis. Heparanase is a heterodimer comprised of a 50 kDa subunit harboring the active site and a 8 kDa subunit. It is produced as a latent 65 kDa precursor and proteolytically processed to its active form. Heparanase is highly expressed in myeloid leukocytes (i.e. neutrophils) in platelets and in human placenta. Human heparanase was found to be upregulated in various types of primary tumors, correlating in some cases with increased tumor invasiveness and vascularity and with poor prospective survival. Recombinant heparanase protein hpa1 is produced in cho cells. the protein is purified by several orthogonal chromatography steps. Applications: Positive control for western blot analysis. Group: Enzymes. Synonyms: Heparanase; Hpa1 heparan. HPA1. Storage: Store at -20°C, avoid repeated freeze-thaw cycles. Source: CHO. Species: Human. Heparanase; Hpa1 heparanase; Hpa1; heparanase 1; heparanase-1; C1A heparanase; HPSE; HPA1. Cat No: NATE-0843. | |
| Hyaluronan synthase from Pasteurella multocida, Recombinant | Hyaluronan synthases (HAS) are membrane-bound enzymes which use UDP-α-N-acetyl-D-glucosamine and UDP-α-D-glucuronate as substrates to produce the glycosaminoglycan hyaluronan at the cell surface and extrude it through the membrane into the extracellular space. Group: Enzymes. Synonyms: EC 2.4.1.212; spHAS; seHAS; Hyaluronan synthases; HAS. Enzyme Commission Number: EC 2.4.1.212. CAS No. 39346-43-5. Purity: min 95% by SDS-PAGE. Hyaluronan synthase. Source: E. coli. Species: Pasteurella multocida. EC 2.4.1.212; spHAS; seHAS; Hyaluronan synthases; HAS. Cat No: NATE-1485. | |
| Isatuximab (anti-CD38) | Isatuximab (anti-CD38) is a monoclonal antibody targeting the transmembrane receptor and extracellular enzyme CD38.Isatuximab induces tumor cell killing via fragment crystallizable (Fc)-dependent or Fc-independent mechanisms, including antibody-dependent cellular cytotoxicity (ADCC), antibody-dependent cellular phagocytosis (ADCP), and complement-dependent cytotoxicity (CDC) [1]. Uses: Scientific research. Group: Inhibitory antibodies. CAS No. 1461640-62-9. Pack Sizes: 1 mg; 5 mg; 10 mg. Product ID: HY-P9976A. | |
| Keratinase, Recombinant | Keratinase is a particular class of extracellular proteolytic inducible enzyme with the capability of degrading insoluble keratin substrates. It is important for hydrolyzing hair, feather, and collagen in sewage system during waste water treatment. It is also useful in food industry, animal feed preparation etc. Insoluble feather keratin from poultry industry may be converted by enzymatic hydrolysis to glues, feedstuffs, fertilizers, films or used for the production of rare amino acids serine, cysteine and proline. Applications: Keratinase was used for enzymatic treatment of elementary body (eb), gag molecules, and cells in the study of the role glycosaminoglycans (gags) in the invasion of host cells by chlamydia pneumoniae strains. Group: Enzymes. Synonyms: Keratinase; KerA; Keratinase from Bacillus licheniformis; Keratinolytic protease; EC 3.4.21. Enzyme Commission Number: EC 3.4.21. Keratinase. Mole weight: ~39 kDa. Activity: 300 - 1000 units/mg. Storage: Store at -20°C. Form: Lyophilized powder. Source: E. coli BL21. Keratinase; KerA; Keratinase from Bacillus licheniformis; Keratinolytic protease; EC 3.4.21. Cat No: NATE-0853. | |
| lactocepin | Associated with the cell envelope of Lactococcus lactis and attached via a C-terminal membrane anchor sequence. Responsible for the hydrolysis of casein in milk and the provision of peptides essential to cell growth. Important in cheese making and the production of lactic casein, being required for rapid growth to high cell densities with concomitant production of adequate levels of lactic acid. Specificity differences between lactocepins from different starter strains may be partly responsible for imparting different flavour qualities to cheese. In peptidase family S8 (subtilisin family). Group: Enzymes. Synonyms: CEP; extracellular lactococcal proteinase; lactococcal cell wall-associated proteinase; lactococcal cell envelope-associated proteinase; lactococcal proteinase; PrtP. Enzyme Commission Number: EC 3.4.21.96. CAS No. 205510-58-3. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4188; lactocepin; EC 3.4.21.96; 205510-58-3; CEP; extracellular lactococcal proteinase; lactococcal cell wall-associated proteinase; lactococcal cell envelope-associated proteinase; lactococcal proteinase; PrtP. Cat No: EXWM-4188. | |
| Lys-Lys/Arg-Xaa endopeptidase | The enzyme is a serine peptidase, which has been shown to cleave prothrombin and prekallikrein. It hydrolyses the complement component C5 releasing complement component C5a. Group: Enzymes. Synonyms: ASP (Aeromonas sobria)-type peptidase; Aeromonas extracellular serine protease. Enzyme Commission Number: EC 3.4.21.121. 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-4117; Lys-Lys/Arg-Xaa endopeptidase; EC 3.4.21.121; ASP (Aeromonas sobria)-type peptidase; Aeromonas extracellular serine protease. Cat No: EXWM-4117. | |
| Matrix Metalloproteinase-13 (HisoTag) from Human, Recombinant | Matrix metalloproteinases are members of a unique family of proteolytic enzymes that have a zinc ion at their active sites and can degrade collagens, elastin and other components of the extracellular matrix (ECM). These enzymes are present in normal healthy individuals and have been shown to have an important role in processes such as wound healing, pregnancy, and bone resorption. However, overexpression and activation of MMPs have been linked with a range of pathological processes and disease states involved in the breakdown and remodeling of the ECM. Such diseases include tumor invasion and metastasis, rheumatoid arthritis, periodontal disease and vascular pr..., a ca2+- and zn2+- binding catalytic domain, a hinge region, and a c-terminal hemopexin domain. hydrolyzes collagen type ii 5-6 times faster than collagens type i and iii. exhibits high activity towards gelatin and degrades α1-antichymotrypsin and plasminogen activator inhibitor-2. Group: Enzymes. Synonyms: Collagenase-3; Matrix metallopeptidase 13; MMP13; CLG3; MANDP1; MMP-13. Purity: >90% by SDS-PAGE. Matrix Metalloproteinase. Mole weight: 60 kDa. Activity: >50 mU/mg protein. Storage: < -70°C; Avoid freeze/thaw. Form: Liquid. Source: S. frugiperda. Species: Human. Collagenase-3; Matrix metallopeptidase 13; MMP13; CLG3; MANDP1; MMP-13. Cat No: NATE-0859. | |
| Matrix Metalloproteinase-1 from Human, Recombinant | Matrix metalloproteinases are members of a unique family of proteolytic enzymes that have a zinc ion at their active sites and can degrade collagens, elastin and other components of the extracellular matrix (ECM). These enzymes are present in normal healthy individuals and have been shown to have an important role in processes such as wound healing, pregnancy, and bone resorption. However, overexpression and activation of MMPs have been linked with a range of pathological processes and disease states involved in the breakdown and remodeling of the ECM. Such diseases include tumor invasion and metastasis, rheumatoid arthritis, periodontal disease and vascular processe...may also undergo autocatalysis to yield a 27 kda/22 kda active enzyme. expressed by a large number of cell types. cleaves fibrillar type i collagen. must be activated just prior to use. Group: Enzymes. Synonyms: Matrix Metalloproteinase 1; Human Interstitial Collagenase; Collagenase-1; EC 3.4.24.7; vertebrate collagenase. Enzyme Commission Number: EC 3.4.24.7. CAS No. 9001-12-1. Purity: >90% by SDS-PAGE. Matrix Metalloproteinase. Mole weight: 56 kDa/52 kDa. Activity: >15 mU/mg protein. Storage: < -70°C; Avoid freeze/thaw. Form: Liquid. Source: Human Rheumatoid Synovial Fibroblast. Species: Human. Matrix Metalloproteinase 1; Human Interstitial Collagenase; Collagenase | |
| Matrix Metalloproteinase-2 from Human, Recombinant | Matrix metalloproteinases are members of a unique family of proteolytic enzymes that have a zinc ion at their active sites and can degrade collagens, elastin and other components of the extracellular matrix (ECM). These enzymes are present in normal healthy individuals and have been shown to have an important role in processes such as wound healing, pregnancy, and bone resorption. However, overexpression and activation of MMPs have been linked with a range of pathological processes and disease states involved in the breakdown and remodeling of the ECM. Such diseases include tumor invasion and metastasis, rheumatoid arthritis, periodontal disease and vascular processe... does not interfere with activation. may contain up to 10% timp proteins. during storage, a small portion (less than 10%) of the enzyme may also become activated. Group: Enzymes. Synonyms: 72 kDa Gelatinase; Matrix Metalloproteinase 2; Gelatinase A; EC 3.4.24.24; type IV collagenase; 3/4 collagenase; matrix metalloproteinase 5; 72 kDa gelatinase type A; collagenase IV; collagenase type IV; MMP 2; type IV collagen metalloproteinase; type IV collagenase/gelatinase. Enzyme Commission Number: EC 3.4.24.24. CAS No. 146480-35-5. Purity: >90% by SDS-PAGE. Matrix Metalloproteinase. Mole weight: 72 kDa. Storage: < -70°C; Avoid freeze/thaw. Form: Liquid. Source: CHO Cells. Spe | |
| Matrix Metalloproteinase-9 from Human, Recombinant | Matrix metalloproteinases are members of a unique family of proteolytic enzymes that have a zinc ion at their active sites and can degrade collagens, elastin and other components of the extracellular matrix (ECM). These enzymes are present in normal healthy individuals and have been shown to have an important role in processes such as wound healing, pregnancy, and bone resorption. However, overexpression and activation of MMPs have been linked with a range of pathological processes and disease states involved in the breakdown and remodeling of the ECM. Such diseases include tumor invasion and metastasis, rheumatoid arthritis, periodontal disease and vascular processe...(less than 10%) of the enzyme may also become activated. requires activation prior to use. a simple activation protocol is included. Applications: Immunoblotting (1 ug protein/lane) substrate cleavage assay (1 ug protein/lane) zymography (1 ug protein/lane). Group: Enzymes. Synonyms: Gelatinase B; EC 3.4.24.35; 92-kDa gelatinase; matrix metalloproteinase 9; type V collagenase; 92-kDa type IV collagenase; macrophage gelatinase; 95 kDa type IV collagenase/gelatinase; collagenase IV; collagenase type IV; gelatinase MMP 9; MMP 9; type IV collagen metalloproteinase. Enzyme Commission Number: EC 3.4.24.35. CAS No. 146480-36-6. Purity: >90% by SDS-PAGE. Matrix Metalloprotei | |
| mitogen-activated protein kinase | Phosphorylation of specific tyrosineand threonine residues in the activation loop of this enzyme by EC 2.7.12.2, mitogen-activated protein kinase kinase (MAPKK) is necessary for enzyme activation. Once activated, the enzyme phosphorylates target substrates on serine or threonine residues followed by a proline. A distinguishing feature of all MAPKs is the conserved sequence Thr-Xaa-Tyr (TXY). Mitogen-activated protein kinase (MAPK) signal transduction pathways are among the most widespread mechanisms of cellular regulation. Mammalian MAPK pathways can be recruited by a wide variety of stimuli including hormones (e.g. insulin and growth hormone), mitogens (e.g. epidermal growth...pk; PMK-1; PMK-2; PMK-3; pp42; pp44mapk; p44mpk; SAPK; STK26; stress-activated protein kinase. Enzyme Commission Number: EC 2.7.11.24. 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-3144; mitogen-activated protein kinase; EC 2.7.11.24; c-Jun N-terminal kinase; Dp38; ERK; ERK1; ERK2; extracellular signal-regulated kinase; JNK; JNK3α1; LeMPK3; MAP kinase; MAP-2 kinase; MAPK; MBP kinase I; MBP kinase II; microtubule-associated protein 2 kinase; microtubule-associated protein kinase; myelin basic protein kinase; p38Δ; p38-2; p42 mitogen-activated protein kinase; p42mapk; PMK-1; PMK- | |
| Mitogen activated protein kinase from rat, Recombinant | Mitogen-activated protein kinases (MAPK) are protein kinases that are specific to the amino acids serine, threonine, and tyrosine. MAPKs belong to the CMGC (CDK/MAPK/GSK3/CLK) kinase group. MAPKs are involved in directing cellular responses to a diverse array of stimuli, such as mitogens, osmotic stress, heat shock and proinflammatory cytokines. They regulate cell functions including proliferation, gene expression, differentiation, mitosis, cell survival, and apoptosis. > 95% (sds-page), buffered aqueous glycerol solution, recombinant, expressed in e. coli (n-terminal histidine tagged). Group: Enzymes. Synonyms: ERK2; Extracellular-signal regulated kinase; MAP Kinase Activated from rat; MAPK; Mitogen activated protein kinase. Purity: > 95% (SDS-PAGE). MAP kinase. Mole weight: mol wt 42 kDa. Activity: > 500 U/mg. Stability: -70°C. Form: buffered aqueous glycerol solution. Source: E. coli. Species: Rat. ERK2; Extracellular-signal regulated kinase; MAP Kinase Activated from rat; MAPK; Mitogen activated protein kinase. Pack: vial of 100 ng. Cat No: NATE-0443. | |
| NAD(P)H oxidase (H2O2-forming) | Requires FAD, heme and calcium. When calcium is present, this transmembrane glycoprotein generates H2O2 by transfering electrons from intracellular NAD(P)H to extracellular molecular oxygen. The electron bridge within the enzyme contains one molecule of FAD and probably two heme groups. This flavoprotein is expressed at the apical membrane of thyrocytes, and provides H2O2 for the thyroid peroxidase-catalysed biosynthesis of thyroid hormones. Group: Enzymes. Synonyms: THOX2; ThOX; dual oxidase; p138tox; thyroid NADPH oxidase; thyroid oxidase; thyroid oxidase 2; NADPH oxidase; NAD(P)H:oxygen oxidoreductase; NAD(P)H oxidase. Enzyme Commission Number: EC 1.6.3.1. CAS No. 77106-92-4. 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-1583; NAD(P)H oxidase (H2O2-forming); EC 1.6.3.1; 77106-92-4; THOX2; ThOX; dual oxidase; p138tox; thyroid NADPH oxidase; thyroid oxidase; thyroid oxidase 2; NADPH oxidase; NAD(P)H:oxygen oxidoreductase; NAD(P)H oxidase. Cat No: EXWM-1583. | |
| Native Abalone Sulfatase | Sulfatases EC 3.1.6.1 are enzymes of the esterase class that catalyze the hydrolysis of sulfate esters. These may be found on a range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. In the latter case the resultant N-sulfates can also be termed sulfamates. Sulfatases play important roles in the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodelling sulfated glycosaminoglycans in the extracellular space. Together with sulfotransferases, sulfatases form the major catalytic machinery for the synthesis and breakage of sulfa...ne conjugates from hamster embryo fibroblasts. Group: Enzymes. Synonyms: EC 3.1.6.1; 9016-17-5; sulfatase; nitrocatechol sulfatase; phenolsulfatase; phenylsulfatase; p-nitrophenyl sulfatase; arylsulfohydrolase; 4-methylumbelliferyl sulfatase; estrogen sulfatase; arylsulfatase. Enzyme Commission Number: EC 3.1.6.1. CAS No. 9016-17-5. Sulfatases. Activity: 20-40 units/mg solid. Storage: -20°C. Form: lyophilized powder. Source: Abalone entrails. Species: Abalone. EC 3.1.6.1; 9016-17-5; sulfatase; nitrocatechol sulfatase; phenolsulfatase; phenylsulfatase; p-nitrophenyl sulfatase; arylsulfohydrolase; 4-methylumbelliferyl sulfatase; estrogen sulfatase; arylsulfatase. Cat No: NATE-0685. | |
| Native Aerobacter aerogenes Sulfatase | Sulfatases EC 3.1.6.1 are enzymes of the esterase class that catalyze the hydrolysis of sulfate esters. These may be found on a range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. In the latter case the resultant N-sulfates can also be termed sulfamates. Sulfatases play important roles in the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodelling sulfated glycosaminoglycans in the extracellular space. Together with sulfotransferases, sulfatases form the major catalytic machinery for the synthesis and breakage o...17-5; sulfatase; nitrocatechol sulfatase; phenolsulfatase; phenylsulfatase; p-nitrophenyl sulfatase; arylsulfohydrolase; 4-methylumbelliferyl sulfatase; estrogen sulfatase; arylsulfatase. Enzyme Commission Number: EC 3.1.6.1. CAS No. 9016-17-5. Sulfatases. Activity: 2-5 units/mg protein (biuret), 10-20 units/mL. Storage: -20°C. Form: buffered aqueous glycerol solution; Solution in 50% glycerol containing 0.01 M Tris, pH 7.5. Source: Aerobacter aerogenes. EC 3.1.6.1; 9016-17-5; sulfatase; nitrocatechol sulfatase; phenolsulfatase; phenylsulfatase; p-nitrophenyl sulfatase; arylsulfohydrolase; 4-methylumbelliferyl sulfatase; estrogen sulfatase; arylsulfatase. Cat No: NATE-0686. | |
| Native Bacillus licheniformis Keratinase (feed grade) | Keratinase is a particular class of extracellular proteolytic inducible enzyme with the capability of degrading insoluble keratin substrates. It is important for hydrolyzing hair, feather, and collagen in sewage system during waste water treatment. It is also useful in food industry, animal feed preparation etc. Insoluble feather keratin from poultry industry may be converted by enzymatic hydrolysis to glues, feedstuffs, fertilizers, films or used for the production of rare amino acids serine, cysteine and proline. Group: Enzymes. Synonyms: KerA; Keratinolytic protease; EC 3.4.21. Enzyme Commission Number: EC 3.4.21. Keratinase. Form: Powder. Source: Bacillus licheniformis. Keratinase; KerA; Keratinase from Bacillus licheniformis; Keratinolytic protease; EC 3.4.21. Cat No: FEED-0001. | |
| Native Bovine β-1,4-Galactosyl Transferase | β-1,4-Galactosyl Transferase catalyzes the transfer of galactose from UDP-galactose to the terminal N-acetylglucosamine residues on elongating oligosaccharide chains. It is also considered to be a biosynthetic enzyme of the Golgi apparatus. β-1,4-Galactosyl Transferase can also be found on the cell surface functioning as a cell-adhesion molecule during various cellular interactions by binding to N-acetylglucosamine containing oligosaccharide substrates or ligands in the extracellular matrix. Group: Enzymes. Synonyms: lactose synthase; UDP-α-D-galactose-glucose galactosyltransferase; N-acetyllactosamine synthase; uridine diphosphogalactose-glucose galactosyltransferase; lactose synthetase; UDP-galactose:D-glucose 4-β-D-galactotransferase; UDP-galactose:D-glucose 4-β-D-galactosyltransferase; EC . Enzyme Commission Number: EC 2.4.1.22. CAS No. 9030-11-9. Galactosyltransferase. Mole weight: Mr ~44000. Activity: > 0.6 units/mg. Storage: -20°C. Source: Bovine milk. Species: Bovine. lactose synthase; UDP-α-D-galactose-glucose galactosyltransferase; N-acetyllactosamine synthase; uridine diphosphogalactose-glucose galactosyltransferase; lactose synthetase; UDP-galactose:D-glucose 4-β-D-galactotransferase; UDP-galactose:D-glucose 4-β-D-galactosyltransferase; EC 2.4.1.22; 9030-11-9. Cat No: NATE-0760. | |
| Native Caldariomyces fumago Chloroperoxidase | Chloroperoxidase (CPO) is a 42 kDa Da extracellular heme glycoenzyme containing ferriprotoporphyrin IX as the prosthetic group. CPO is secreted from fungus and exhibits a broad spectrum of chemical reactivities. It is a peroxide-dependent chlorinating enzyme. It also catalyzes peroxidase-, catalase-and cytochrome P450-type reactions of dehydrogenation, H2O2 decomposition and oxygen insertion, respectively. The enzyme has magnetic and spectroscopic properties similar to that of cyctochrome P-450. CPO from the fungus Caldariomyces fumago has the capacity to chlorinate aromatic hydrocarbons, including polycyclic aromatic hydrocarbons (PAHs). Applications: A useful alternative to lactoperoxidase for 131i ion labeling studies, for bromination of proteins, and for cl labeling of macromolecules in long-term isolation procedures. Group: Enzymes. Synonyms: Chloroperoxidase; CPO; Vanadium halopero. Enzyme Commission Number: EC 1.11.1.10. CAS No. 9055-20-3. CPO. Activity: 1,000-2,000 units/mg protein (E1%/280); > 3,000 units/mL; >10,000 U/mL. Storage: 2-8°C. Form: buffered aqueous suspension. Purified suspension in 0.1 M sodium phosphate solution, pH approx. 4.5. Source: Caldariomyces fumago. Chloroperoxidase; CPO; Vanadium haloperoxidase; EC 1.11.1.10; 9055-20-3; Chloride Peroxidase; Chloride:hydrogen-peroxide oxidoreductase. Cat No: NATE-0156. | |
| Native Clostridium histolyticum Collagenase | Collagenases are endopeptidases that digest native collagen in the triple helix region. Collagens are the major fibrous component of animal extracellular connective tissue. Bacterial collagenases differ from vertebrate collagenases in that they exhibit broader substrate specificity (Peterkofsky 1982, Birkedal-Hansen 1987). Unlike animal collagenases that split collagen in its native triple-helical conformation (Woolley et al. 1975, Gross et al. 1974), bacterial collagenase is unique because it can degrade both water-insoluble native collagens and water-soluble denatured ones. It can attack almost all collagen types, and is able to make multiple cleavages within triple h...ations needing to avoid introduction of animal derived pathogens into bioprocessing procedures. Group: Enzymes. Synonyms: EC 3.4.24.3; Collagenase; Clostridiopeptidase A; Clostridium histolyticum collagenase; collagenase A; collagenase I; Achromobacter iophagus collagenase; aspergillopeptidase C; nucleolysin; Collagenase, Type 1; Collagenase, Type 2; Collagenase, Type 3; Collagenase, Type 4; Collagenase, Type 5. Enzyme Commission Number: EC 3.4.24.3. CAS No. 9001-12-1. Collagenase. Mole weight: 68 to 130 kDa. Activity: Type 1 > 125 units per mg; Type 2 > 125 units per mg; Type 3 > 100 units per mg; Type 4 > 160 units per mg; Type 5 > 450 units per mg. Stability: This pro | |
| Native Dactylium dendroides Galactose Oxidase | Galactose oxidase is an extracellular copper-containing enzyme, secreted by the deuteromycete fungus Dactylium dendroides. It catalyzes the oxidation of a range of primary alcohols, including D-galactose, to the corresponding aldehyde, with reduction of oxygen to hydrogen peroxide. Galactose oxidase is an extracellular copper-containing enzyme, secreted by the deuteromycete fungus dactylium dendroides. it catalyzes the oxidation of a range of primary alcohols, including d-galactose, to the corresponding aldehyde, with reduction of oxygen to hydrogen peroxide. Applications: Galactose oxidase may be used as an analytical tool for the specific determination of d-galactose in blood plasma, plant extracts, and phospholipids. it could be used for the characterization of terminal d-galactoside units in several polymers. it may also be useful in the determination of lactose. Group: Enzymes. Synonyms: EC 1.1.3.9; D-galactose oxidase; β-galacto. Enzyme Commission Number: EC 1.1.3.9. CAS No. 9028-79-9. Galactose Oxidase. Activity: Type I, 500-1,500 units/mg protein; Type II, > 3000 units/g solid. Storage: -20°C. Form: Type I, Lyophilized, contains buffer salts and stabilizer; Type II, lyophilized powder. Source: Dactylium dendroides. EC 1.1.3.9; D-galactose oxidase; β-galactose oxidase; 9028-79-9; Galactose Oxidase. Cat No: NATE-0273. | |
| Native Flavobacterium heparinum Heparinase I and III Blend | 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. Heparinase is an inducible, non-extracellular heparin-degrading enzyme. three types of heparinises are produced by flavobacterium heparinum and contains specific sequences of heparin. Applications: Heparinase i and iii may be used for the study of heparin production during fermentation and specific activity of heparinise. Group: Enzymes. Synonyms: Heparinase; Heparin lyase; Heparin eliminase; Heparin-sulfate lyase; Heparin-sulfate eliminase; Heparitin-sulfate lyase; Heparinase I; Heparinase III. Heparinase. Storage: -20°C. Source: Flavobacterium heparinum. Heparinase; Heparin lyase; Heparin eliminase; Heparin-sulfate lyase; Heparin-sulfate eliminase; Heparitin-sulfate lyase; Heparinase I; Heparinase III. Cat No: NATE-0337. | |
| Native Helix pomatia Sulfatase | Sulfatases EC 3.1.6.1 are enzymes of the esterase class that catalyze the hydrolysis of sulfate esters. These may be found on a range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. In the latter case the resultant N-sulfates can also be termed sulfamates. Sulfatases play important roles in the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodelling sulfated glycosaminoglycans in the extracellular space. Together with sulfotransferases, sulfatases form the major catalytic machinery for the synthesis and breakage of su...n. Group: Enzymes. Synonyms: EC 3.1.6.1; 9016-17-5; sulfatase; nitrocatechol sulfatase; phenolsulfatase; phenylsulfatase; p-nitrophenyl sulfatase; arylsulfohydrolase; 4-methylumbelliferyl sulfatase; estrogen sulfatase; arylsulfatase. Enzyme Commission Number: EC 3.1.6.1. CAS No. 9016-17-5. Sulfatases. Activity: Type I, > 10 ,000 units/g solid; Type II, > 2 ,000 units/mL. Storage: -20°C. Form: Type I, powder; Type II, aqueous solution. Source: Helix pomatia. EC 3.1.6.1; 9016-17-5; sulfatase; nitrocatechol sulfatase; phenolsulfatase; phenylsulfatase; p-nitrophenyl sulfatase; arylsulfohydrolase; 4-methylumbelliferyl sulfatase; estrogen sulfatase; arylsulfatase. Cat No: NATE-0687. | |
| Native Human Cathepsin G | Cathepsin G is an enzymatic protein belonging to the peptidase or protease families. In humans, it is coded by the CTSG gene. The protein encoded by this gene, a member of the peptidase S1 protein family, is found in azurophil granules of neutrophilic polymorphonuclear leukocytes. The encoded protease has a specificity similar to that of chymotrypsin C, but it is most closely related to other immune serine proteases, such as neutrophil elastase and the granzymes. Cathepsin G may participate in the killing and digestion of engulfed pathogens, and in connective tissue remodeling at sites of inflammation. It also localizes to Neutrophil extracellular traps (NETs), via its high affinity for DNA, an unusual property for serine proteases. Transcript variants utilizing alternative polyadenylation signals exist for this gene. Group: Enzymes. Synonyms: CTSG; cathepsin G; CG; CATG; EC 3.4.21.20; chymotrypsin-like proteinase; neutral proteinase. Enzyme Commission Number: EC 3.4.21.20. CAS No. 56645-49-9. Purity: > 96% (SDS-PAGE). CTSG. Activity: > 5 U/mL. Appearance: Clear, colorless solution. Storage: 2-8°C. Form: Liquid. Source: Human Neutrophils. Species: Human. CTSG; cathepsin G; CG; CATG; EC 3.4.21.20; chymotrypsin-like proteinase; neutral proteinase. Cat No: NATE-0173. | |
| Native Human Elastase | Neutrophil elastase is a serine proteinase in the same family as chymotrypsin and has broad substrate specificity. Secreted by neutrophils and macrophages during inflammation, it destroys bacteria and host tissue. It also localizes to Neutrophil extracellular traps (NETs), via its high affinity for DNA, an unusual property for serine proteases. Leuk ocyte elastase is a 29 kda serine endoprotease of the proteinase s1 family. it exists as a single 238 amino acid-peptide chain with four disulfide bonds. it contains two or thee n-linked glycans of variable composition which account for its three major isoforms. Applications: Elastase from creative enzymes has been used to digest fibro...mal models. Group: Enzymes. Synonyms: ELANE; elastase; EC 3.4.21.37; leukocyte elastase; ELA2; elastase 2; neutrophil elaszym; serine elastase; lysosomal elastase; neutrophil elastase; polymorphonuclear leukocyte elastase; elaszym; granulocyte elastase. Enzyme Commission Number: EC 3.4.21.37. CAS No. 9004-6-2. ELA2. Mole weight: 29 kDa. Activity: > 50 units/mg protein (Bradford). Storage: -20°C. Form: Lyophilized from 0.05 M sodium acetate (pH 5.5) and 0.6 M NaCl. Source: Human leuk ocytes. Species: Human. ELANE; elastase; EC 3.4.21.37; leukocyte elastase; ELA2; elastase 2; neutrophil elaszym; serine elastase; lysosomal elastase; neutrophil elastase; polymorphonuclear leukocyte ela | |
| Native Human Myeloperoxidase | Myeloperoxidase (MPO) is a peroxidase enzyme that in humans is encoded by the MPO gene on chromosome 17. MPO is most abundantly expressed in neutrophil granulocytes (a subtype of white blood cells), and produces hypohalous acids to carry out their antimicrobial activity. It is a lysosomal protein stored in azurophilic granules of the neutrophil and released into the extracellular space during degranulation. MPO has a heme pigment, which causes its green color in secretions rich in neutrophils, such as pus and some forms of mucus. Group: Enzymes. Synonyms: MPO; myeloperoxidase; Peroxidase; myelo; EC 1.11.1.7; 9003-99-0. Enzyme Commission Number: EC 1.11.1.7. CAS No. 9003-99-0. Peroxidase. Activity: > 50 units/mg protein. Storage: -20°C. Form: Lyophilized from 50 mM sodium acetate buffer, pH 6.0, 0.1 M sodium chloride. Source: Human leuk ocytes. Species: Human. MPO; myeloperoxidase; Peroxidase; myelo; EC 1.11.1.7; 9003-99-0. Cat No: NATE-0457. | |
| Native Human Myeloperoxidase A+B | Myeloperoxidase (MPO) is a peroxidase enzyme that in humans is encoded by the MPO gene on chromosome 17. MPO is most abundantly expressed in neutrophil granulocytes (a subtype of white blood cells), and produces hypohalous acids to carry out their antimicrobial activity. It is a lysosomal protein stored in azurophilic granules of the neutrophil and released into the extracellular space during degranulation. MPO has a heme pigment, which causes its green color in secretions rich in neutrophils, such as pus and some forms of mucus. Group: Enzymes. Synonyms: MPOAB; MPOA+B; Myeloperoxidase A+B. Purity: > 98% (SDS-PAGE). Peroxidase. Activity: Typically > 1,000 U/mL. Storage: 2-8°C. Form: Liquid. Source: Human Neutrophils. Species: Human. MPOAB; MPOA+B; Myeloperoxidase A+B. Cat No: NATE-0459. | |
| Native Human Myeloperoxidase Isoform A | Myeloperoxidase (MPO) is a peroxidase enzyme that in humans is encoded by the MPO gene on chromosome 17. MPO is most abundantly expressed in neutrophil granulocytes (a subtype of white blood cells), and produces hypohalous acids to carry out their antimicrobial activity. It is a lysosomal protein stored in azurophilic granules of the neutrophil and released into the extracellular space during degranulation. MPO has a heme pigment, which causes its green color in secretions rich in neutrophils, such as pus and some forms of mucus. Group: Enzymes. Synonyms: MPOA; Myeloperoxidase Isoform A; EC 1.11.1.7; 9003-99-0; MPO A. Enzyme Commission Number: EC 1.11.1.7. CAS No. 9003-99-0. Purity: > 98% (SDS-PAGE). Peroxidase. Mole weight: 151 kDa. Activity: Typically > 1 ,000 U/mL. Storage: 2-8°C. Form: Liquid. Source: Human Neutrophils. Species: Human. MPOA; Myeloperoxidase Isoform A; EC 1.11.1.7; 9003-99-0; MPO A. Cat No: NATE-0458. | |
| Native Human Myeloperoxidase Isoform B | Myeloperoxidase (MPO) is a peroxidase enzyme that in humans is encoded by the MPO gene on chromosome 17. MPO is most abundantly expressed in neutrophil granulocytes (a subtype of white blood cells), and produces hypohalous acids to carry out their antimicrobial activity. It is a lysosomal protein stored in azurophilic granules of the neutrophil and released into the extracellular space during degranulation. MPO has a heme pigment, which causes its green color in secretions rich in neutrophils, such as pus and some forms of mucus. Group: Enzymes. Synonyms: MPOB; MPO B; Myeloperoxidase Isoform B; EC 1.11.1.7; 9003-99-0. Enzyme Commission Number: EC 1.11.1.7. CAS No. 9003-99-0. Purity: > 96% (SDS-PAGE). Peroxidase. Mole weight: 149 kDa. Activity: > 500 U/mL. Storage: 2-8°C. Form: Liquid. Source: Human Neutrophils. Species: Human. MPOB; MPO B; Myeloperoxidase Isoform B; EC 1.11.1.7; 9003-99-0. Cat No: NATE-0460. | |
| Native Human Myeloperoxidase Isoform C | Myeloperoxidase (MPO) is a peroxidase enzyme that in humans is encoded by the MPO gene on chromosome 17. MPO is most abundantly expressed in neutrophil granulocytes (a subtype of white blood cells), and produces hypohalous acids to carry out their antimicrobial activity. It is a lysosomal protein stored in azurophilic granules of the neutrophil and released into the extracellular space during degranulation. MPO has a heme pigment, which causes its green color in secretions rich in neutrophils, such as pus and some forms of mucus. Applications: Protein cystalline research. Group: Enzymes. Synonyms: MPOC; MPO C; Myeloperoxidase Isoform C; EC 1.11.1.7; 9003-99-0. Enzyme Commission Number: EC 1.11.1.7. CAS No. 9003-99-0. Purity: > 96% (SDS-PAGE). Peroxidase. Mole weight: 146 kDa. Activity: Typically > 1 ,000 U/mg protein. Storage: 2-8°C. Form: Liquid. Source: Human Neutrophils. Species: Human. MPOC; MPO C; Myeloperoxidase Isoform C; EC 1.11.1.7; 9003-99-0. Cat No: NATE-0461. | |
| Native Human Renin | Renin, also known as an angiotensinogenase, is an enzyme that participates in the body's renin-angiotensin aldosterone system (RAAS)--also known as the renin-angiotensin-aldosterone axis--that mediates extracellular volume (i.e., that of the blood plasma, lymph and interstitial fluid), and arterial vasoconstriction. Thus, it regulates the body's mean arterial blood pressure. Renin is often improperly referred to as a hormone even though it has no peripheral receptors and rather has an enzymatic activity with which it hydrolyses angiotensinogen to angiotensin I. Applications: Research elisa assay life science clinical chemistry. Group: Enzymes. Synonyms: REN; HNFJ2; Renin; angiotensinogenase. CAS No. 9015-94-5. Renin. Activity: >90% (>0.5 U/mg). Storage: 4°C. Source: Human Kidney. Species: Human. REN; HNFJ2; Renin; angiotensinogenase. Cat No: NATE-0650. | |
| Native Human Urokinase | Urokinase is a serine protease (EC 3.4.21.73). Urokinase was originally isolated from human urine, but is present in several physiological locations, such as blood stream and the extracellular matrix. The primary physiological substrate is plasminogen, which is an inactive form (zymogen) of the serine protease plasmin. Activation of plasmin triggers a proteolysis cascade that, depending on the physiological environment, participates in thrombolysis or extracellular matrix degradation. This links urokinase to vascular diseases and cancer. Urokinase from human urine. Group: Enzymes. Synonyms: Urokinase; EC 3.4.21.73; urokinase-type plasminogen activator; uPA; U-plasminogen activator; Cellular plasminogen activator; Urinary plasminogen activator. Enzyme Commission Number: EC 3.4.21.73. CAS No. 9039-53-6. Purity: Purity by SDS Electrophoresis ? 95 %. uPA. Activity: > 500 units/mg protein. Form: Lyophilized from 1 mL of 50 mM Tris-HCl, pH 7.4 with 100 mM NaCl, 0.1% PEG 6000, and 200 mM mannitol. Source: Human urine. Species: Human. Urokinase; EC 3.4.21.73; urokinase-type plasminogen activator; uPA; U-plasminogen activator; Cellular plasminogen activator; Urinary plasminogen activator. Cat No: PHAM-262. | |
| Native Klebsiella pneumoniae Pullulanase | Pullulanase is a lipoprotein generated as a precursor containing a 19-amino acid signal peptide followed by a palmitate-modified cysteine residue. The signal peptide gets cleaved prior to secretion into the extracellular matrix. Pullulanase is a lipoprotein generated as a precursor containing a 19-amino acid signal peptide followed by a palmitate-modified cysteine residue. the signal peptide gets cleaved prior to secretion into the extracellular matrix. Applications: Pullulanase has been used in a study to assess its l ocation in escherichia coli k12 carrying the cloned structural gene from klebsiella pneumoniae. it has also been used in a study to investigate the role of...lpha;-1,6-glucanohydrolase; 9075-68-7. Enzyme Commission Number: EC 3.2.1.41. CAS No. 9075-68-7. Pullulanase. Activity: Type I, 10-30 units/mg protein; Type II, > 5 units/mg protein (biuret). Storage: -20°C. Form: Type I, Lyophilized powder containing potassium phosphate buffer salts and stabilizer; Type II, ammonium sulfate suspension, Suspension in 3.2 M (NH4)2SO4 solution, pH 6.2. Source: Klebsiella pneumoniae. Pullulanase; EC 3.2.1.41; limit dextrinase (erroneous); amylopectin 6-glucanohydrolase; bacterial debranching enzyme; debranching enzyme; α-dextrin endo-1,6-α-glucosidase; R-enzyme; pullulan α-1,6-glucanohydrolase; 9075-68-7. Cat No: NATE-0643. | |
| Native Patella vulgata (keyhole limpet) Sulfatase | Sulfatases EC 3.1.6.1 are enzymes of the esterase class that catalyze the hydrolysis of sulfate esters. These may be found on a range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. In the latter case the resultant N-sulfates can also be termed sulfamates. Sulfatases play important roles in the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodelling sulfated glycosaminoglycans in the extracellular space. Together with sulfotransferases, sulfatases form the major catalytic machinery for the synthesis and breakage of sulfate esters. Group: Enzymes. Synonyms: EC 3.1.6.1; 9016-17-5; sulfatase; nitrocatechol sulfatase; phenolsulfatase; phenylsulfatase; p-nitrophenyl sulfatase; arylsulfohydrolase; 4-methylumbellifery. Enzyme Commission Number: EC 3.1.6.1. CAS No. 9016-17-5. Sulfatases. Activity: Type I, > 10 units/mg solid; Type II, > 5 units/mg solid. Storage: -20°C. Form: essentially salt-free, lyophilized powder. Source: Patella vulgata (keyhole limpet). EC 3.1.6.1; 9016-17-5; sulfatase; nitrocatechol sulfatase; phenolsulfatase; phenylsulfatase; p-nitrophenyl sulfatase; arylsulfohydrolase; 4-methylumbelliferyl sulfatase; estrogen sulfatase; arylsulfatase. Cat No: NATE-0688. | |
| Native Penicillium sp. Dextranase | An endodextranase that hydrolyzes-(1,6)-glucosidic linkages in dextran. Dextrans are undesirable compounds synthesized from sucrose by microbial contaminants during sugar production that increase viscosity of the flow and decrease industrial recovery. Dextranase has been used for hydrolyzing dextran at sugar mills in order to improve efficiency of sugar production. Applications: Dextranase from penicillium has been used in a study to assess the purification properties of an extracellular dextranase from penicillium janthinellum. dextranase from penicillium has also been used in a study to investigate the carbohydrate component of penicillium funiculosum dextranase. it has been used for the hydrolysis of carbohydate polymers, during the study of polysaccharide synthesis by phanerochaete chrysosporium. it has also been used in the synthesis of new enzymatically degradable thermo-responsive nanogels. Group: Enzymes. Synonyms: EC 3.2.1.11, dextran hydrolase; endodextranase; dextran. Enzyme Commission Number: EC 3.2.1.11. CAS No. 9025-70-1. Dextranase. Activity: 3,000 units/mg. Storage: 2-8°C. Form: lyophilized powder. Source: Penicillium sp. EC 3.2.1.11, dextran hydrolase; endodextranase; dextranase DL 2; DL 2; endo-dextranase; α-D-1,6-glucan-6-glucanohydrolase; 1,6-α-D-glucan 6-glucanohydrolase; 9025-70-1; Dextranase. Cat No: NATE-0194. | |
| Native Rat Protein Kinase C Catalytic Subunit | Protein Kinase C (PKC) is a serine/threonine kinase that is activated intracellularly by signal transduction pathways that produce DAG from phosphatidylinositol diphosphate (PIP2) and phosphatidylcholine (PC) through the action of various activated phospholipases. Phorbol esters also stimulate PKC. At least 11 PKC isozymes have been identified that differ in primary structure, tissue distribution, subcellular localization, response to extracellular signals, and substrate specificity. The isozymes can be grouped into three subfamilies. Members of the first family require Ca2+ and phospholipid and include PKCα, βI, βII, and &gamma. Members of the second family are phospholipid-dependent but Ca2+-independent, and include PKCδ, ε, η, and &theta. Members of the third family are not activated by either DAG or phorbol esters and include PKCξ, μ, and &Iota. Does not require ca2+ or phosphatidylserine for its activity. Group: Enzymes. Synonyms: PKC-M, PKM; PKCM; Protein Kinase C Catalytic Subunit. Purity: > 90% (SDS-PAGE). PKC. Activity: > 800 units/mg protein. Stability: -70°C. Source: rat brain. Species: Rat. PKC-M, PKM; PKCM; Protein Kinase C Catalytic Subunit. Pack: vial of 200 ng. Cat No: NATE-0578. | |
| Native Staphylococcus aureus α-Hemolysin | α-Hemolysin is a 33 kDa extracellular protein secreted by most strains of pathogenic Staphylococcus aureus. It is selectively hemolytic and has a marked preference for rabbit red blood cells. It induces dermonecrosis, spastic muscle paralysis, and it is lethal for laboratory animals. The toxin must be in the monomeric form to initially bind to a membrane and specific receptors are not required for binding. Upon binding to biological membranes and/or artificial membranes, self-oligomerization occurs, resulting in ring structures (hexameric aggregates) believed to represent transmembrane pores, which are permeable to ions and small metabolites. Group: Enzymes. Synonyms: α-Hemolysin; 94716-94-6; α-Toxin. α-Hemolysin. Activity: > 10,000 units/mg protein. Storage: 2-8°C. Source: Staphylococcus aureus. α-Hemolysin; 94716-94-6; α-Toxin. Cat No: NATE-0753. | |
| Native Streptomyces griseus Chitinase | Chitinase is an extracellular enzyme complex that degrades chitin and has a molecular mass of approximately 30 kDa. Chitin is degraded to N-acetyl-D-glucosamine in 2 enzymatic reactions. Firstly, chitobiose units are removed from chitin by chitodextrinase-chitinase. The second reaction involves N-acetyl-glucosaminidase-chitobiase, which cleaves the disaccharide to its monomer subunits (that comprise of N-acetyl-D-glucosamine). Applications: Chitinase from streptomyces griseus has been used to study the effect of the allosamidin on the regulatory system for chitinase production. it has also been used to study the enrichment of chitinolytic microorganisms. this enrichment wa...;-glucosaminidase; β-1,4-poly-N-acetyl glucosamidinase; poly[1,4-(N-acetyl-β-D-glucosaminide)] glycanohydrolase; (1->4)-2-acetamido-2-deoxy-beta-D-glucan glycanohydrolase; EC 3.2.1.14. Enzyme Commission Number: EC 3.2.1.14. CAS No. 9001-6-3. Chitinase. Activity: > 200 units/g solid. Storage: -20°C. Form: lyophilized powder (essentially salt free). Source: Streptomyces griseus. Chitinase; chitodextrinase; 1,4-β-poly-N-acetylglucosaminidase; poly-β-glucosaminidase; β-1,4-poly-N-acetyl glucosamidinase; poly[1,4-(N-acetyl-β-D-glucosaminide)] glycanohydrolase; (1->4)-2-acetamido-2-deoxy-beta-D-glucan glycanohydrolase; EC 3.2.1.14. Cat No: NATE-0123. | |
| 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 | |
| Native Trichoderma viride Chitinase | Chitinase is an extracellular enzyme complex that degrades chitin and has a molecular mass of approximately 30 kDa. Chitin is degraded to N-acetyl-D-glucosamine in 2 enzymatic reactions. Firstly, chitobiose units are removed from chitin by chitodextrinase-chitinase. The second reaction involves N-acetyl-glucosaminidase-chitobiase, which cleaves the disaccharide to its monomer subunits (that comprise of N-acetyl-D-glucosamine). Applications: Chitinase from trichoderma viride has been used in a study to investigate the differential release of high mannose structural isoforms by fungal and bacterial endo-β-n-acetylglucosaminidases. chitinase from trichoderma viride has al...glucosaminidase; poly-β-glucosaminidase; β-1,4-poly-N-acetyl glucosamidinase; poly[1,4-(N-acetyl-β-D-glucosaminide)] glycanohydrolase; (1->4)-2-acetamido-2-deoxy-beta-D-glucan glycanohydrolase; EC 3.2.1.14. Enzyme Commission Number: EC 3.2.1.14. CAS No. 9001-6-3. Chitinase. Activity: > 600 units/g solid. Storage: -20°C. Form: lyophilized powder. Source: Trichoderma viride. Chitinase; chitodextrinase; 1,4-β-poly-N-acetylglucosaminidase; poly-β-glucosaminidase; β-1,4-poly-N-acetyl glucosamidinase; poly[1,4-(N-acetyl-β-D-glucosaminide)] glycanohydrolase; (1->4)-2-acetamido-2-deoxy-beta-D-glucan glycanohydrolase; EC 3.2.1.14. Cat No: NATE-0124. | |
| N-(Ketocaproyl)-L-homoserine Lactone (N-(3-Oxohexanoyl)-homoserine Lactone) | An autoinducer of P. fischeri luciferase. A specfic genetic regulator that is unrelated to at least one of the enzyme systems that it induces, and it acts after excretion and accumulation in the extracellular medium. Group: Biochemicals. Alternative Names: N-(3-Oxohexanoyl)-homoserine Lactone. Grades: Highly Purified. CAS No. 143537-62-6. Pack Sizes: 100mg. US Biological Life Sciences. | Worldwide |
| Oleclumab | Oleclumab (MEDI9447) is a human IgG1λ monoclonal antibody targeting CD73 and inhibits the exonuclease activity of the extracellular enzyme CD73. Oleclumab can adjust the composition of bone marrow and lymphoid infiltrating leukocyte populations in the tumor microenvironment and has anti-tumor activity [1] [2]. Uses: Scientific research. Group: Inhibitory antibodies. Alternative Names: MEDI9447. CAS No. 1803176-05-7. Pack Sizes: 1 mg; 5 mg. Product ID: HY-P99039. | |
| oryzin | A peptidase of family S8 (subtilisin family), not containing cysteine, that is the predominant extracellular alkaline endopeptidase of the mold Aspergillus oryzae.Identical or closely related enzymes are produced by A. flavus and A. sojae. Group: Enzymes. Synonyms: Aspergillus alkaline proteinase; aspergillopeptidase B; API 21; aspergillopepsin B; aspergillopepsin F; Aspergillus candidus alkaline proteinase; Aspergillus flavus alkaline proteinase; Aspergillus melleus semi-alkaline proteinase;. Enzyme Commission Number: EC 3.4.21.63. CAS No. 9074-7-1. 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-4154; oryzin; EC 3.4.21.63; 9074-07-1; Aspergillus alkaline proteinase; aspergillopeptidase B; API 21; aspergillopepsin B; aspergillopepsin F; Aspergillus candidus alkaline proteinase; Aspergillus flavus alkaline proteinase; Aspergillus melleus semi-alkaline proteinase; Aspergillus oryzae alkaline proteinase; Aspergillus parasiticus alkaline proteinase; Aspergillus serine proteinase; Aspergillus sydowi alkaline proteinase; Aspergillus soya alkaline proteinase; Aspergillus melleus alkaline proteinase; Aspergillus sulphureus alkaline proteinase; prozyme; P 5380; kyorinase; seaprose S; semi-alkaline protease; sumizyme MP; prozyme 10; onoprose; onoprose SA; protease P; promelase. Cat No: EXWM-4154. | |
| P1,P5-Di(adenosine-5')pentaphosphate trilithium salt | A diadenosine polyphosphate stored in secretory granules of thrombocytes, chromaffin and neuronal cells. After release into the extracellular space, it affects a variety of biological activities in a wide range of target tissues. In the nervous system it acts through various purinergic receptors. It also activates 5?-nucleotidase and inhibits adenosine kinase activity in vitro. Ap5A is metabolized by soluble enzymes in the blood plasma and by membrane-bound ectoenzymes of a number of cell types including endothelial and smooth muscle cells. In cardiac muscle, pM to nM concentrations significantly increase the open-probability of ryanodine-receptor (RyR2) gates, with prolonged action due to slow dissociation from the receptor. Group: Biochemicals. Alternative Names: P1,P5-Di(adenosine-5) pentaphosphate pentalithium salt, 94108-02-8, A(5)P5(5)A, AC1O4WDE, D6392_SIGMA, CTK8G2238, EINECS 302-339-2, AP5A lithium salt P1,P5-Di(adenosine-5) pentaphosphate pentalithium salt, AG-H-86941, Diadenosine pentaphosphate trilithium salt, Diadenosine pentaphosphate pentalithium salt, K00187, A(5 inverted exclamation marka)P5(5 inverted exclamation marka)A trilithium sal. Grades: Highly Purified. CAS No. 75522-97-3. Pack Sizes: 25mg, 50mg, 100mg, 250mg. Molecular Formula: C20H26N10O22P5Li3, Molecular Weight: 934.17. US Biological Life Sciences. | Worldwide |
| poly(3-hydroxybutyrate) depolymerase | Reaction also occurs with esters of other short-chain-length (C1-C5) hydroxyalkanoic acids (HA). There are two types of polymers: native (intracellular) granules are amorphous and have an intact surface layer; denatured (extracellular) granules either have no surface layer or a damaged surface layer and are partially crystalline. Group: Enzymes. Synonyms: PHB depolymerase; poly(3HB) depolymerase; poly[(R)-hydroxyalkanoic acid] depolymerase; poly(HA) depolymerase; poly(HASCL) depolymerase; poly[(R)-3-hydroxybutyrate] hydrolase. Enzyme Commission Number: EC 3.1.1.75. CAS No. 9014-11-3. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3503; poly(3-hydroxybutyrate) depolymerase; EC 3.1.1.75; 9014-11-3; PHB depolymerase; poly(3HB) depolymerase; poly[(R)-hydroxyalkanoic acid] depolymerase; poly(HA) depolymerase; poly(HASCL) depolymerase; poly[(R)-3-hydroxybutyrate] hydrolase. Cat No: EXWM-3503. | |
| Protein kinase Cα isozyme human, Recombinant | Protein Kinase C (PKC) is a serine/threonine kinase that is activated intracellularly by signal transduction pathways that produce DAG from phosphatidylinositol diphosphate (PIP2) and phosphatidylcholine (PC) through the action of various activated phospholipases. Phorbol esters also stimulate PKC. At least 11 PKC isozymes have been identified that differ in primary structure, tissue distribution, subcellular localization, response to extracellular signals, and substrate specificity. The isozymes can be grouped into three subfamilies. Members of the first family require Ca2+ and phospholipid and include PKCα, βI, βII, and &gamma. Members of the second...third family are not activated by either DAG or phorbol esters and include PKCξ, μ, and &Iota. > 70% (sds-page), recombinant, expressed in baculovirus infected insect cells, buffered aqueous glycerol solution. Group: Enzymes. Synonyms: PRKCA; protein kinase C, alpha; PKCA; protein kinase C alpha type; PKC-A; PKCα; AAG6; PKC-alpha; PRKACA. Purity: > 70% (SDS-PAGE). PKC. Mole weight: mol wt 80-81 kDa by SDS-PAGE. Stability: -70°C. Form: buffered aqueous glycerol solution. Source: baculovirus infected insect cells. Species: Human. PRKCA; protein kinase C, alpha; PKCA; protein kinase C alpha type; PKC-A; PKCα; AAG6; PKC-alpha; PRKACA. Cat No: NATE-0574. | |
| Protein Kinase CβII isozyme from human, Recombinant | Protein Kinase C (PKC) is a serine/threonine kinase that is activated intracellularly by signal transduction pathways that produce DAG from phosphatidylinositol diphosphate (PIP2) and phosphatidylcholine (PC) through the action of various activated phospholipases. Phorbol esters also stimulate PKC. At least 11 PKC isozymes have been identified that differ in primary structure, tissue distribution, subcellular localization, response to extracellular signals, and substrate specificity. The isozymes can be grouped into three subfamilies. Members of the first family require Ca2+ and phospholipid and include PKCα, βI, βII, and &gamma. Members of the sec... esters and include PKCξ, μ, and &Iota. Group: Enzymes. Synonyms: PRKCB; PKCB; PRKCB1; PRKCB2; protein kinase C, beta 1; protein kinase C beta type; PKC-beta; EC 2.7.1.37. Enzyme Commission Number: EC 2.7.1.37. Purity: >95% (SDS-PAGE). PKC. Mole weight: calculated mol wt 76.9 kDa; mol wt 80 kDa by SDS-PAGE. Storage: -70°C. Form: buffered aqueous glycerol solution; Solution in 20 mM HEPES, pH 7.4; 2 mM EDTA, 2 mM EGTA, 5 mM DTT, 100 mM NaCl, 0.05% Triton X-100, and 50% glycerol. Source: Baculovirus infected insect cells. Species: Human. PRKCB; PKCB; PRKCB1; PRKCB2; protein kinase C, beta 1; protein kinase C beta type; PKC-beta; EC 2.7.1.37. Cat No: NATE-0622. | |
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