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HEPES, a nonvolatile zwitterionic chemical buffering agent, is broadly applied in cell culture. HEPES is effective at pH 6.8 to 8.2. HEPES is also a potent inducer of lysosome biogenesis [1] [2] [3]. Uses: Scientific research. Group: Biochemical assay reagents. CAS No. 7365-45-9. Pack Sizes: 500 mg; 1 g. Product ID: HY-D0857.
500g Pack Size. Group: Buffers. Formula: C8H18N2O4S. CAS No. 7365-45-9. Prepack ID 47376574-500g. Molecular Weight 238.31. See USA prepack pricing.
HEPES Buffer, 1M
HEPES Buffer, 1M, is prepared from HEPES Free acid with sterile-filtered, Molecular Biology grade water and is a biological buffer (zwitterionic) designed by Good, et al., and typically referred to as Goods buffer useful in cell culture media formulations. Group: Biochemicals. Alternative Names: N- [2-Hydroxyethyl] piperazine-N- [2-ethanesulfonic acid]. Grades: Molecular Biology Grade. CAS No. 7365-45-9. Pack Sizes: 100ml, 500ml. US Biological Life Sciences.
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HEPES-d18
HEPES-d 18 is the deuterium labeled HEPES[1]. HEPES, a nonvolatile zwitterionic chemical buffering agent, is broadly applied in cell culture. HEPES is effective at pH 6.8 to 8.2. HEPES is also a potent inducer of lysosome biogenesis[2][3][4]. Uses: Scientific research. Group: Isotope-labeled compounds. CAS No. 203805-87-2. Pack Sizes: 1 mg; 5 mg; 10 mg. Product ID: HY-D0857S.
HEPES Free Acid
HEPES is a biological buffer (zwitterionic) designed by Good, et al., and typically referred to as Goods buffer useful in cell culture media formulations. Selection of biological buffer systems should include the following criteria: exclusion by biological membranes, low absorption between 240 and 700nm, chemically stable, and stable to temperature and concentration changes. Group: Biochemicals. Alternative Names: N- [2-Hydroxyethyl] piperazine-N- [2-ethanesulfonic acid]. Grades: Molecular Biology Grade. CAS No. 7365-45-9. Pack Sizes: 100g, 500g, 1Kg, 5Kg, 10Kg. Molecular Formula: C8H18N2O4S, Molecular Weight: 238.31. US Biological Life Sciences.
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HEPES sodium
HEPES sodium, a nonvolatile zwitterionic chemical buffering agent, is broadly applied in cell culture. HEPES sodium is effective at pH 6.8 to 8.2. HEPES sodium is also a potent inducer of lysosome biogenesis [1] [2] [3]. Uses: Scientific research. Group: Biochemical assay reagents. CAS No. 75277-39-3. Pack Sizes: 25 g. Product ID: HY-108535.
HEPES Sodium salt
100g Pack Size. Group: Buffers. Formula: C8H17N2NaO4S. CAS No. 75277-39-3. Prepack ID 80267503-100g. Molecular Weight 260.29. See USA prepack pricing.
HEPES Sodium salt
500g Pack Size. Group: Buffers. Formula: C8H17N2NaO4S. CAS No. 75277-39-3. Prepack ID 80267503-500g. Molecular Weight 260.29. See USA prepack pricing.
HEPES Sodium Salt
HEPES Sodium is a biological buffer. Group: Biochemicals. Alternative Names: N- [2-Hydroxyethyl] piperazine-N- [2-ethanesulfonic acid] sodium salt. Grades: Molecular Biology Grade. CAS No. 75277-39-3. Pack Sizes: 100g, 500g, 1Kg, 5Kg, 10Kg. Molecular Formula: C8H17N2O4SNa, Molecular Weight: 260.3. US Biological Life Sciences.
Reacts specifically and rapidly with thiols to form mixed disulfides. Used to probe the structures of the ACh receptor channel of the GABAA receptor channel and of lactose permease. At pH 7.5 and room temperature, MTSEA hydrolyzes with a half-life of about 15 minutes, MTSET hydrolyzes with a half-life of 10 minutes, and MTSES hydrolyzes with a half-life of 20 minutes. Routinely, one can use 2.5mM MTSEA, 1mM MTSET, or 10mM MTSES, applied for 1 to 5 minutes. (MTSET is 2.5 times as reactive with small sulfhydryl compounds as is MTSEA, and 10 times as reactive as MTSES). (Stauffer and Karlin, 1994; Karlin, personal communication).For application to Xenopus Oocytes, dissolve the compounds in 115mM NaCl, 2.5mM KCl, 1.8mM MgCl2, 10mM Hepes, pH 7.5 with NaOH. MTS reagents decompose in buffer very quickly. DMSO is a good solvent for the MTS reagents which are not water soluble (i.e. the non-charged MTS reagents). Group: Biochemicals. Alternative Names: N,N,N-Trimethyl-2-[(methylsulfonyl)thio]-ethanaminium Bromide; MTSET; (2-Mercaptoethyl) trimethylammonium Bromide Methanesulfonate; Methanethiosulfonate Ethyltrimethylammonium Bromide. Grades: Highly Purified. CAS No. 91774-25-3. Pack Sizes: 250mg. Molecular Formula: C6H16BrNO2S2, Molecular Weight: 278.23. US Biological Life Sciences.
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β-1,3-Glucanase from Clostridium thermocellum, Recombinant
Glucan endo-1,3-beta-D-glucosidase is an enzyme with system name 3-beta-D-glucan glucanohydrolase. This enzyme catalyses the following chemical reaction:Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans. This enzyme is marginally active on mixed-link (1->3,1->4)-beta-D-glucans. Group: Enzymes. Synonyms: endo-1,3-β-glucanase; laminarinase; laminaranase; oligo-1,3-glucosidase; endo-1,3-β-glucanase; callase; β-1,3-glucanase; kitalase; 1,3-β-D-glucan 3-glucanohydrolase; endo-(1,3)-β-D-gl. Enzyme Commission Number: EC 3.2.1.39. CAS No. 9025-37-0. Purity: > 95 % as judged by SDS-PAGE. Glucanase. Mole weight: 82262.8 Da. Activity: 1500 U/mg. Storage: Store at -20°C (shipped at room temperature). Form: Supplied in 35 mM HEPES buffer, pH 7.8, containing 750 mM NaCl, 5 mM imidazole, 2.5 mM CaCl2, 0.02 % (w/v) sodium azide and 25 % (v/v) glycerol. Source: Clostridium thermocellum ATCC 27405. endo-1,3-β-glucanase; laminarinase; laminaranase; oligo-1,3-glucosidase; endo-1,3-β-glucanase; callase; β-1,3-glucanase; kitalase; 1,3-β-D-glucan 3-glucanohydrolase; endo-(1,3)-β-D-glucanase; (1?3)-β-glucan 3-glucanohydrolase; endo-1,3-β-D-glucanase; endo-1,3-β-glucosidase; 1,3-β-D-glucan glucanohydrolase; EC 3.2.1.39; 9044-93-3. Cat No: NATE-1180.
β-Glucosidase from Clostridium thermocellum, Recombinant
Beta-glucosidase is a glucosidase enzyme that acts upon β1->4 bonds linking two glucose or glucose-substituted molecules (i.e., the disaccharide cellobiose). It is one of the cellulases, enzymes involved in the decomposition of cellulose and related polysaccharides; more specifically, an exocellulase with specificity for a variety of beta-D-glycoside substrates. It catalyzes the hydrolysis of terminal non-reducing residues in beta-D-glucosides with release of glucose. Group: Enzymes. Synonyms: EC 3.2.1.21; gentiobiase; cellobiase; emulsin; elaterase; aryl-beta-glucosidase; beta-D-glucosidase; beta-glucoside glucohydrolase; arbutinas. Enzyme Commission Number: EC 3.2.1.21. CAS No. 9001-42-7. Purity: > 95 % as judged by SDS-PAGE. β-Glucosidase. Mole weight: 52700 Da. Activity: 33 U/mg. Storage: Store at -20°C (shipped at room temperature). Form: Supplied in 35 mM HEPES buffer, pH 7.8, containing 750 mM NaCl, 5 mM imidazole, 3.5 mM CaCl2, 0.02 % (w/v) sodium azide and 25 % (v/v) glycerol. Source: Clostridium thermocellum DSM 1237. EC 3.2.1.21; gentiobiase; cellobiase; emulsin; elaterase; aryl-beta-glucosidase; beta-D-glucosidase; beta-glucoside glucohydrolase; arbutinase; amygdalinase; p-nitrophenyl beta-glucosidase; primeverosidase; amygdalase; linamarase; salicilinase; beta-1,6-glucosidase. Cat No: NATE-1182.
β-Mannanase from Clostridium thermocellum, Recombinant
Mannan endo-1,4-beta-mannosidase is an enzyme with system name 4-beta-D-mannan mannanohydrolase. This enzyme catalyses the following chemical reaction: Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans. Group: Enzymes. Synonyms: endo-1,4-β-mannanase; endo-β-1,4-mannase; β-mannanase B; β-1, 4-mannan 4-mannanohydrolase; endo-β-mannanase; β-D-mannanase; mannan endo-1,4-β-mannosidase; 1,4-β-D-mannan mannanohydrolase; EC 3.2.1.78. Enzyme Commission Number: EC 3.2.1.78. CAS No. 37288-54-3. Purity: > 95 % as judged by SDS-PAGE. endo-1,4 β-Mannanase. Mole weight: 42700 Da. Activity: 1500 U/mg. Storage: Store at -20°C (shipped at room temperature). Form: Supplied in 35 mM HEPES buffer, pH 7.5, containing 750 mM NaCl, 200 mM imidazole, 3.5 mM CaCl2, 0.02 % (w/v) sodium azide and 25% (v/v) glycerol. Source: Clostridium thermocellum YS. endo-1,4-β-mannanase; endo-β-1,4-mannase; β-mannanase B; β-1, 4-mannan 4-mannanohydrolase; endo-β-mannanase; β-D-mannanase; mannan endo-1,4-β-mannosidase; 1,4-β-D-mannan mannanohydrolase; EC 3.2.1.78. Cat No: NATE-1184.
Bis-Tris
Bis-Tris is an amine buffer suitable for protein and nucleic acid systems with a pH buffer range of 5.8-7.2. Bis-Tris can also be mixed with HEPES and cacodylic acid buffer to create a pH 8 environment and monitor fluorescence emission intensity at 305 nm. Gels formulated with Bis-Tris also avoid protein degradation in samples prepared at higher pH (pH 8.5) [1] [2] [3]. Uses: Scientific research. Group: Biochemical assay reagents. CAS No. 6976-37-0. Pack Sizes: 25 g; 50 g. Product ID: HY-D0856.
Calmodulin-dependent Protein Kinase II from Rat, Recombinant
Serine-threonine protein kinase:these kinases appear to be involved in neurotransmitter release, control of stimulus-induced gene expression, and in the phosphorylation of microtubule related proteins. Calmodulin-dependent protein kinase ii (camkII) is a serine/threonine kinase. it is a ca2+/calmodulin-dependent, truncated monomer (1-325 amino acid residues) of the α subunit. autophosphorylation of threonine 286 in the presence of ca2+ and calmodulin activates camkii and produces substantial ca2+/calmodulin-independent activity. Group: Enzymes. Synonyms: Calmodulin-dependent Protein Kinase II; 9026-43-1. Purity: > 95% determined by SDS-PAGE. Calmodulin-dependent Protein Kinase II. Mole weight: Apparent: 33 kDa Theoretical: 36 kDa. Activity: 5,000,000 units/mg. Storage: at -70°C. Avoid repeated freeze/thaw cycles. Form: 100 mM NaCl, 50 mM HEPES (pH 7.5 25°C), 0.1 mM EDTA, 1 mM DTT, 0.01% Brij 35 and 50% glycerol. Source: S. frugiperda Sf9. Species: Rat. Calmodulin-dependent Protein Kinase II; 9026-43-1; CaMKII. Cat No: NATE-1273.
Cellulase from Cellvibrio mixtus, Recombinant
Cellulase is any of several enzymes produced chiefly by fungi, bacteria, and protozoans that catalyze cellulolysis, the decomposition of cellulose and of some related polysaccharides; specifically, the hydrolysis of the 1,4-beta-D-glycosidic linkages in cellulose, hemicellulose, lichenin, and cereal beta-D-glucans. Cellulases break down the cellulose molecule into monosaccharides ("simple sugars") such as beta-glucose, or shorter polysaccharides and oligosaccharides. The name is also used for any naturally occurring mixture or complex of various such enzymes, that act serially or synergistically to decompose cellulosic material. Group: Enzymes. Synonyms: Cellulase, the... 3.2.1.4. CAS No. 9012-54-8. Purity: > 95 % as judged by SDS-PAGE. Cellulase. Mole weight: 33835.5 Da. Activity: 950 U/mg. Storage: Store at -20°C (shipped at room temperature). Form: Supplied in 35 mM HEPES buffer, pH 7.5, containing 750 mM NaCl, 200 mM imidazole, 3.5 mM CaCl2 and 25 % (v/v) glycerol. Source: Cellvibrio mixtus ATCC 12120. Cellulase, thermostable; 1,4-(1,3:1,4)-β-D-Glucan 4-glucano-hydrolase; EC 3.2.1.4; Cellulase; endo-1,4-β-D-glucanase; β-1,4-glucanase; β-1,4-endoglucan hydrolase; celluase A; cellulosin AP; endoglucanase D; alkali cellulase; cellulase A 3; celludextrinase; 9.5 cellulase; avicelase; pancellase SS. Cat No: NATE-1200.
Coagulation Factor Calibrator Plasma
The Coagulation Factor Calibrator Plasma is a lyophilized reference plasma intended for use in the calibration of Antigen assays for factor II, factor VII, factor X, factor XI, factor XIII, Protein C, Protein S, Antithrombin III, von Willebrand Factor and fibrinogen by ELISA. It is prepared from a pool of normal citrated human plasma collected from a minimum of 20 donors, buffered with HEPES and stabilizers and lyophilized. Group: Biologicals. Pack Sizes: 1ml. US Biological Life Sciences.
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Fpg Protein from Escherichia coli, Recombinant
Fpg protein, a key enzyme in the DNA base excision repair pathway (BER), catalyses the excision of a broad spectrum of modified purines such as formamidopyrimidine (Fapy) and 8-oxoguanine (8-oxo-G). Fpg possess both DNA glycosylase activity that removes the mutated base and AP-lyase activity that releases ribose, leaving both 5'-and 3'-phosphorylated ends in the DNA. Several analytical methods based on Fpg protein activity in vitro were developed for detection and quantitation of oxidative damage to DNA mainly for FapyA, FapyG and 8-oxo-G. The fpg gene was cloned by Boiteux, et al. Fpg protein possess a zinc finger motif at its C-terminus (one zinc atom per molecule). ... Protein. Mole weight: mol wt 30.2 kDa (269 amino acids, predicted from the nucleotide sequence). Activity: >20 ,000 units/mg protein. Storage: -20°C. Form: buffered aqueous glycerol solution; Solution in 50% glycerol containing 50 mM potassium HEPES, pH 7.5, 1 mM DTT, 1 mM EDTA, and 200 mM NaCl. Source: E. coli. Species: Escherichia coli. Fapy-DNA glycosylase; deoxyribonucleate glycosidase; 2,6-diamino-4-hydroxy-5N-formamidopyrimidine-DNA glycosylase; 2,6-diamino-4-hydroxy-5 (N-methyl)formamidopyrimidine-DNA glycosylase; formamidopyrimidine-DNA glycosylase; DNA-formamidopyrimidine glycosidase; Fpg protein; DNA-formamidopyrimidine glycosylase; EC 3.2.2.23; 78783-53-6;
Granzyme H from Human, Recombinant (carrier-free)
Granzyme H is a member of the granzyme family of serine proteases found specifically in the cytotoxic granules of cytotoxic T lymphocytes (CTL) and natural killer (NK) cells. Granzyme Hs functions are largely unknown. The more abundant expression of Granzyme H than Granzyme B in NK cells suggests that Granzyme H may complement the pro-apoptotic function of Granzyme B in this cell type. Group: Enzymes. Synonyms: Granzyme H; GZMH; Granzyme. Enzyme Commission Number: EC 3.4.21.-. Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain. Alkalophilic proteinase. Mole weight: Multiple bands between 38-40 kDa, reducing conditions by SDS-PAGE. Activity: >5,000 pmol/min/ug. Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.6 months from date of receipt, -70 °C as supplied.3 months, -70 °C under sterile conditions after opening. Form: Supplied as a 0.2 μm filtered solution in HEPES, NaCl and Brij-35. Source: Mouse myeloma cell line. Species: Human. Granzyme H; GZMH; Granzyme. Cat No: NATE-1935.
Lambda Protein Phosphatase, Recombinant
λ Protein Phosphatase (λ-PPase) is a Mn+2-dependent protein phosphatase with activity towards phosphorylated serine, threonine, tyrosine and histidine residues. It is the 221 amino-acid product of ORF221 open reading frame on bacteriophage lambda (1, 2). λ-PPase was expressed as a recombinant protein in E.coli and highly purified (2). This product is an intact enzyme of high quality without tag. Applications: Λ-ppase can be used to release phosphate groups from phosphorylated serine, threonine, tyrosine and histidine residues in proteins (2). it should be noted that different proteins are dephosphorylated at different rates. optimal reaction temperature is 30°c. inclusion of protease inhibitor cocktail and shortest incubation time is desired when assays are done with crude samples. Group: Enzymes. Synonyms: Protein phosphatase 1F; PPM1F; CAMKP; CaMKPase; FEM-2; POPX2; hFEM-2; Lambda Protein. Purity: >98% by SDS-PAGE. λ-PPase. Activity: 400,000 U/mg (400 U/ul). Storage: Store at -80°C. Avoid repeating freeze-thaw cycles. Form: 400 U/ul λ-PPase in 50mM HEPES (pH 7.5), 100mM NaCl, 2mM dithiothreitol, 0.1 mM MnCl2, 0.1mM EDTA, 50% glycerol, 0.01% Brij 35. Source: E. coli. Protein phosphatase 1F; PPM1F; CAMKP; CaMKPase; FEM-2; POPX2; hFEM-2; Lambda Protein Phosphatase; λ-PPase. Cat No: NATE-0990.
Luciferase from Photinus pyralis (firefly), Recombinant
Firefly luciferase is an enzyme that catalyzes production of light from luciferin in the presence of Mg2+-ATP and oxygen. The reaction of this enzyme with luciferin, ATP, and O2 results in the emission of light. Luciferase activity can be inhibited by general anesthetics including isoflurane and ketamine/medetomidine thereby affecting the sensitivity of bioluminescence imaging. Applications: The reaction of this enzyme with luciferin, atp, and o2 results in the emission of light. luciferase can be used to detect trace amounts of atp. firefly luciferase is also one of the most commonly utilized reporter genes for the study of gene expression. the bioluminescent rea...pe I , > 5 ,000 ,000 units/mg protein; Type II, 15-30×106 light units/mg protein. Storage: -70°C. Form: Type I, Supplied as a solution in 50 mM Tris HCl pH 8.0, 1 mM dithiothreitol, 1 mM EDTA, and 10% (v/v) glycerol; Type II, Lyophilized powder approximately 20% protein; balance is primarily NaCl, HEPES buffer salts, and carbohydrate. Source: E. coli. Species: Photinus pyralis (firefly). Photinus-luciferin 4-monooxygenase (ATP-hydrolysing); firefly luciferase; luciferase (firefly luciferin); Photinus luciferin 4-monooxygenase (adenosine triphosphate-hydrolyzing); firefly luciferin luciferase; Photinus pyralis luciferase; EC 1.13.12.7; 61970-00-1. Cat No: NATE-0424.
Matrix Metalloproteinase-3 from Human, Recombinant
Matrix metalloproteinase-3 (MMP-3) also known as stromelysin-1 and transin (EC 3.4.24.17) cleaves a number of substrates including cartilage proteoglycan, collagen types II, III, IV, V and IX, fibronectin, laminin, and can activate MMP 1. MMP-3 is secreted as 57 and 59 kDa proenzymes and can be activated in vitro by organomercurials (e.g., 4 aminophenylmercuric acetate, APMA) and in vivo by proteases via intermediate forms to a 45 kDa active MMP 3 enzyme. Further autolysis to a 28 kDa form can also occur. MMP-3 is thought to play an important role in pathophysiological degradation processes associated with conditions such as rheumatoid arthritis and cancer cell invas...C 3.4.24.17; matrix metalloproteinase 3; proteoglycanase; collagenase activating protein; procollagenase activator; transin; MMP-3; neutral proteoglycanase; stromelysin; collagen-activating protein. Enzyme Commission Number: EC 3.4.24.17. CAS No. 79955-99-0. Purity: >95% by SDS-PAGE. Matrix Metalloproteinase. Mole weight: 57 kDa. Storage: < -70°C; Avoid freeze/thaw. Form: Lyophilized from 100 mM NaCl, 50 mM HEPES, pH 7.3. Species: Human. Stromelysin 1; EC 3.4.24.17; matrix metalloproteinase 3; proteoglycanase; collagenase activating protein; procollagenase activator; transin; MMP-3; neutral proteoglycanase; stromelysin; collagen-activating protein. Cat No: NATE-0861.
Matrix Metalloproteinase-7 from human, Recombinant
MMP-7 degrades general matrix components and may have a role in processes such as host defense, cell proliferation, and protein turnover as well as tissue remodeling. Group: Enzymes. Synonyms: MMP7; matrix metallopeptidase 7; MMP-7; matrin; uterine metalloendopeptidase; matrix metalloproteinase 7; putative (or punctuated) metalloproteinase-1; matrix metalloproteinase pump 1; MMP 7; PUMP-1 proteinase; PUMP; metalloproteinase pump-1; putative metalloproteinase; MMP. CAS No. 141256-52-2. Matrix Metalloproteinase. Storage: -70°C. Form: buffered aqueous solution, Supplied in a buffer containing the active enzyme in 10 mM HEPES, pH 7.4, 0.15 M sodium chloride, 5 mM calcium chloride. Source: E. coli. Species: Human. MMP7; matrix metallopeptidase 7; MMP-7; matrin; uterine metalloendopeptidase; matrix metalloproteinase 7; putative (or punctuated) metalloproteinase-1; matrix metalloproteinase pump 1; MMP 7; PUMP-1 proteinase; PUMP; metalloproteinase pump-1; putative metalloproteinase; MMP. Cat No: NATE-0451.
Native Crotalus atrox venom 5'-Nucleotidase
5'-nucleotidase is an enzyme with system name 5'-ribonucleotide phosphohydrolase. This enzyme catalyses the following chemical reaction:a 5'-ribonucleotide + H2O<-> a ribonucleoside + phosphate. This enzyme has a wide specificity for 5'-nucleotides. Group: Enzymes. Synonyms: 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. Enzyme Commission Number: EC 3.1.3.5. CAS No. 9027-73-0. AMPase. Activity: > 200 units/mg protein. Storage: -20°C. Form: Lyophilized powder balance primarily trehalose, HEPES and CaCl2. Source: Crotalus atrox. 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. Cat No: NATE-0072.
Native Human erythrocytes Acetylcholinesterase
Acetylcholinesterase, also known as AChE or acetylhydrolase, is a hydrolase that hydrolyzes the neurotransmitter acetylcholine. AChE is found at mainly neuromuscular junctions and cholinergic brain synapses, where its activity serves to terminate synaptic transmission. It belongs to carboxylesterase family of enzymes. It is the primary target of inhibition by organophosphorus compounds such as nerve agents and pesticides. The activity obtained using acetylcholine as substrate is 30-100 times that obtained with butyrylcholine, using acetylcholinesterase from electric eel. Applications: Acetylcholinesterase (ache) from creative enzymes has been used in the structure-activity study of phosphoramido acid esters as inhibitors of ache. Group: Enzymes. Synonyms: true cholinesterase; choline esterase I; cholines. Enzyme Commission Number: EC 3.1.1.7. CAS No. 9000-81-1. Acetylcholinesterase. Mole weight: ~80 kDa. Activity: > 500 units/mg protein (BCA). Storage: 2-8°C. Form: buffered aqueous solution. Solution in 20 mM HEPES, pH 8.0, containing 0.1% TRITON X-100. Source: Human erythrocytes. Species: Human. true cholinesterase; choline esterase I; cholinesterase; acetylthiocholinesterase; acetylcholine hydrolase; acetyl; β-methylcholinesterase; AcCholE; EC 3.1.1.7; 9000-81-1; Acetylcholinesterase; AChE; acetylhydrolase. Cat No: NATE-0019.
Native Porcine Carboxypeptidase B
Carboxypeptidase B (or peptidyl-L-lysine (-L-arginine) hydrolase) catalyzes the hydrolysis of the basic amino acids, lysine, arginine, and ornithine from the C-terminal position of polypeptides. It has been shown to be a single polypeptide of 34 kDa Da. Trypsin is capable of converting native enzyme to the active enzyme, carboxypeptidase B II in vitro. The optimum pH is found to be 9.0. The enzyme may be used for sequence analysis by successive cleavage of C-terminal basic amino acids. It can also be used as a serum marker for the diagnosis of acute pancreatitis. Protein determined by biuret. Applications: Carboxypeptidase b has been used in a study to develop a non-invasive...ith carboxypeptidase b, which is a c-terminal lysine-specific endopeptidase, is measured using flow cytometry analysis. Group: Enzymes. Synonyms: carboxypeptidase B; protaminase; CPB1; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase; EC 3.4.17.2; 9025-24-5. Enzyme Commission Number: EC 3.4.17.2. CAS No. 9025-24-5. CPB1. Storage: -20°C. Form: lyophilized powder. Contains HEPES buffer salts and carbohydrate. Source: Porcine pancreas. Species: Porcine. carboxypeptidase B; protaminase; CPB1; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase; EC 3.4.17.2; 9025-24-5. Cat No: NATE-0152.
Nitric Oxide Synthase, Inducible from mouse, Recombinant
Nitric oxide synthases (NOSs) are a family of enzymes catalyzing the production of nitric oxide (NO) from L-arginine. NO is an important cellular signaling molecule. It helps modulate vascular tone, insulin secretion, airway tone, and peristalsis, and is involved in angiogenesis and neural development. It may function as a retrograde neurotransmitter. Nitric oxide is mediated in mammals by the calcium-calmodulin controlled isoenzymes eNOS (endothelial NOS) and nNOS (neuronal NOS). The inducible isoform, iNOS, is involved in immune response, binds calmodulin at physiologically relevant concentrations, and produces NO as an immune defense mechanism, as NO is a free ...DPH); Inducible Nitric Oxide Synthase; NOS II; iNOS; macNOS; EC 1.14.13.39; NOSs. Enzyme Commission Number: EC 1.14.13.39. CAS No. 125978-95-2. NOSs. Mole weight: mol wt 130 kDa (homodimer); mol wt 130 kDa (subunit, homodimer). Storage: -70°C. Form: buffered aqueous solution; Solution in 50 mM HEPES, pH 7.4, with 10% glycerol, 8 μM tetrahydrobiopterin. Source: E. coli. Species: Mouse. nitric oxide synthetase; endothelium-derived relaxation factor-forming enzyme; endothelium-derived relaxing factor synthase; NO synthase; NADPH-diaphorase; nitric-oxide synthase (NADPH); Inducible Nitric Oxide Synthase; NOS II; iNOS; macNOS; EC 1.14.13.39; NOSs. Cat No: NATE-0489.
Polynucleotide Phosphorylase from Escherichia coli, Recombinant
Polynucleotide phosphorylase (PNPase) is a bifunctional enzyme with a phosphorolytic 3' to 5' exoribonuclease activity and a 3'-terminal oligonucleotide polymerase activity. It is also involved in mRNA processing and degradation in bacteria, plants, and humans. Applications: Polynucleotide phosphorylase (pnp) has been used in a study to show that spontaneous mutations resulting from replication errors are reduced in a pnp-deficient strain. it has also been used in a study to show that the absence of pnpase makes e. coli cells sensitive to uv, which suggests pnp has a role in survival of uv damage. Group: Enzymes. Synonyms: PNPase; nucleoside diphosphate:polynucleotidyl transferase; polyribonucleotide nucleotidyltransferase; polynucleotide phosphorylase; polyribonucleotide phosphorylase; EC 2.7.7.8; 9014-12-4. Enzyme Commission Number: EC 2.7.7.8. CAS No. 9014-12-4. Polynucleotide phosphorylase. Storage: -70°C. Form: Supplied as a solution in 20 mM Hepes buffer pH 7.9, 0.1 mM EDTA, 2 mM DTT, 12.5 mM MgCl2, 200 mM KCl, 21.4% (w/v) Glycerol. Source: E. coli. Species: Escherichia coli. PNPase; nucleoside diphosphate:polynucleotidyl transferase; polyribonucleotide nucleotidyltransferase; polynucleotide phosphorylase; polyribonucleotide phosphorylase; EC 2.7.7.8; 9014-12-4. Cat No: NATE-0608.
Polynucleotide phosphorylase from Human, Recombinant
Polynucleotide phosphorylase (PNPase) is a bifunctional enzyme with a phosphorolytic 3' to 5' exoribonuclease activity and a 3'-terminal oligonucleotide polymerase activity. It is also involved in mRNA processing and degradation in bacteria, plants, and humans. Group: Enzymes. Synonyms: PNPase; nucleoside diphosphate:polynucleotidyl transferase; polyribonucleotide nucleotidyltransferase; polynucleotide phosphorylase; polyribonucleotide phosphorylase; EC 2.7.7.8; 9014-12-4. Enzyme Commission Number: EC 2.7.7.8. CAS No. 9014-12-4. Polynucleotide phosphorylase. Storage: -70°C. Form: supplied as a solution in 20 mM HEPES buffer, pH 7.9, with 0.1 mM EDTA, 2 mM DTT, 12.5 mM MgCl2, ~130 mM KCl, and 20% (w/v) glycerol. Source: E. coli. Species: Human. PNPase; nucleoside diphosphate:polynucleotidyl transferase; polyribonucleotide nucleotidyltransferase; polynucleotide phosphorylase; polyribonucleotide phosphorylase; EC 2.7.7.8; 9014-12-4. Cat No: NATE-0609.
Protein Kinase CβII isozyme from human, Recombinant
Protein Kinase C (PKC) is a serine/threonine kinase that is activated intracellularly by signal transduction pathways that produce DAG from phosphatidylinositol diphosphate (PIP2) and phosphatidylcholine (PC) through the action of various activated phospholipases. Phorbol esters also stimulate PKC. At least 11 PKC isozymes have been identified that differ in primary structure, tissue distribution, subcellular localization, response to extracellular signals, and substrate specificity. The isozymes can be grouped into three subfamilies. Members of the first family require Ca2+ and phospholipid and include PKCα, βI, βII, and &gamma. Members of the sec... esters and include PKCξ, μ, and &Iota. Group: Enzymes. Synonyms: PRKCB; PKCB; PRKCB1; PRKCB2; protein kinase C, beta 1; protein kinase C beta type; PKC-beta; EC 2.7.1.37. Enzyme Commission Number: EC 2.7.1.37. Purity: >95% (SDS-PAGE). PKC. Mole weight: calculated mol wt 76.9 kDa; mol wt 80 kDa by SDS-PAGE. Storage: -70°C. Form: buffered aqueous glycerol solution; Solution in 20 mM HEPES, pH 7.4; 2 mM EDTA, 2 mM EGTA, 5 mM DTT, 100 mM NaCl, 0.05% Triton X-100, and 50% glycerol. Source: Baculovirus infected insect cells. Species: Human. PRKCB; PKCB; PRKCB1; PRKCB2; protein kinase C, beta 1; protein kinase C beta type; PKC-beta; EC 2.7.1.37. Cat No: NATE-0622.
Protein Kinase CβI isozyme from human, Recombinant
Protein Kinase C (PKC) is a serine/threonine kinase that is activated intracellularly by signal transduction pathways that produce DAG from phosphatidylinositol diphosphate (PIP2) and phosphatidylcholine (PC) through the action of various activated phospholipases. Phorbol esters also stimulate PKC. At least 11 PKC isozymes have been identified that differ in primary structure, tissue distribution, subcellular localization, response to extracellular signals, and substrate specificity. The isozymes can be grouped into three subfamilies. Members of the first family require Ca2+ and phospholipid and include PKCα, βI, βII, and &gamma. Members of the sec...ted by either DAG or phorbol esters and include PKCξ, μ, and &Iota. Group: Enzymes. Synonyms: PRKCB; PKCB; PRKCB1; PRKCB2; protein kinase C, beta 1; protein kinase C beta type; PKC-beta; EC 2.7.1.37. Enzyme Commission Number: EC 2.7.1.37. Purity: > 95% (SDS-PAGE). PKC. Mole weight: apparent mol wt 79-80 kDa. Storage: -70°C. Form: buffered aqueous glycerol solution; Solution in 20 mM HEPES, pH 7.4; 2 mM EDTA, 2 mM EGTA, 5 mM DTT, 100 mM NaCl, 0.05% Triton X-100, and 50% glycerol. Source: Baculovirus infected insect cells. Species: Human. PRKCB; PKCB; PRKCB1; PRKCB2; protein kinase C, beta 1; protein kinase C beta type; PKC-beta; EC 2.7.1.37. Cat No: NATE-0621.
Protein Kinase Cδ isozyme from human, Recombinant
Protein Kinase C (PKC) is a serine/threonine kinase that is activated intracellularly by signal transduction pathways that produce DAG from phosphatidylinositol diphosphate (PIP2) and phosphatidylcholine (PC) through the action of various activated phospholipases. Phorbol esters also stimulate PKC. At least 11 PKC isozymes have been identified that differ in primary structure, tissue distribution, subcellular localization, response to extracellular signals, and substrate specificity. The isozymes can be grouped into three subfamilies. Members of the first family require Ca2+ and phospholipid and include PKCα, βI, βII, and &gamma. Members of the sec...DAG or phorbol esters and include PKCξ, μ, and &Iota. Group: Enzymes. Synonyms: PRKCD; protein kinase C, delta; protein kinase C delta type; ALPS3; CVID9; MAY1; PKCD; nPKC-delta; EC 2.7.1.37. Enzyme Commission Number: EC 2.7.1.37. Purity: >95% (SDS-PAGE). PKC. Mole weight: mol wt 74-79 kDa by SDS-PAGE. Storage: -70°C. Form: buffered aqueous glycerol solution; Solution in 20 mM HEPES, pH 7.4; 2 mM EDTA, 2 mM EGTA, 5 mM DTT, 100 mM NaCl, 0.05% Triton X-100, and 50% glycerol. Source: Baculovirus infected insect cells. Species: Human. PRKCD; protein kinase C, delta; protein kinase C delta type; ALPS3; CVID9; MAY1; PKCD; nPKC-delta; EC 2.7.1.37. Cat No: NATE-0623.
Protein kinase Cγ isozyme from human, Recombinant
Protein Kinase C (PKC) is a serine/threonine kinase that is activated intracellularly by signal transduction pathways that produce DAG from phosphatidylinositol diphosphate (PIP2) and phosphatidylcholine (PC) through the action of various activated phospholipases. Phorbol esters also stimulate PKC. At least 11 PKC isozymes have been identified that differ in primary structure, tissue distribution, subcellular localization, response to extracellular signals, and substrate specificity. The isozymes can be grouped into three subfamilies. Members of the first family require Ca2+ and phospholipid and include PKCα, βI, βII, and &gamma. Members of the sec...vated by either DAG or phorbol esters and include PKCξ, μ, and &Iota. Group: Enzymes. Synonyms: PRKCG; protein kinase C, gamma; protein kinase C gamma type; PKC-gamma; PKCC; PKCG; SCA14; EC 2.7.1.37. Enzyme Commission Number: EC 2.7.1.37. Purity: >95% (SDS-PAGE). PKC. Mole weight: mol wt 77-84 kDa by SDS-PAGE. Storage: -70°C. Form: buffered aqueous glycerol solution; Solution in 20 mM HEPES, pH 7.4; 2 mM EDTA, 2 mM EGTA, 5 mM DTT, 250 mM NaCl, 0.05% Triton X-100, and 50% glycerol. Source: Baculovirus infected insect cells. Species: Human. PRKCG; protein kinase C, gamma; protein kinase C gamma type; PKC-gamma; PKCC; PKCG; SCA14; EC 2.7.1.37. Cat No: NATE-0624.
Protein Kinase Cζ isozyme from human, Recombinant
Protein Kinase C (PKC) is a serine/threonine kinase that is activated intracellularly by signal transduction pathways that produce DAG from phosphatidylinositol diphosphate (PIP2) and phosphatidylcholine (PC) through the action of various activated phospholipases. Phorbol esters also stimulate PKC. At least 11 PKC isozymes have been identified that differ in primary structure, tissue distribution, subcellular localization, response to extracellular signals, and substrate specificity. The isozymes can be grouped into three subfamilies. Members of the first family require Ca2+ and phospholipid and include PKCα, βI, βII, and &gamma. Members of the seco...Members of the third family are not activated by either DAG or phorbol esters and include PKCξ, μ, and &Iota. Group: Enzymes. Synonyms: PRKCZ; protein kinase C, zeta; protein kinase C zeta type; PKC2; PKC-ZETA; EC 2.7.1.37. Enzyme Commission Number: EC 2.7.1.37. Purity: > 75% (SDS-PAGE). PKC. Mole weight: mol wt 76-80 kDa by SDS-PAGE. Storage: -70°C. Form: buffered aqueous solution; Solution in 20 mM HEPES, pH 7.5; 2 mM EDTA, 2 mM EGTA, 5 mM DTT, 250 mM NaCl, 0.05% Triton X-100, and 50% glycerol. Source: Baculovirus infected insect cells. Species: Human. PRKCZ; protein kinase C, zeta; protein kinase C zeta type; PKC2; PKC-ZETA; EC 2.7.1.37. Cat No: NATE-0625.
11(R)-Hepe
Heterocyclic Organic Compound. Alternative Names: 11R-HYDROXY-5Z,8Z,12E,14Z,17Z-EICOSAPENTAENOIC ACID;11(R)-HEPE;11R-Hydroxy-5Z,8Z,12E,14Z,17Z-eicosadienoic acid. CAS No. 109430-11-7. Molecular formula: C20H30O3. Mole weight: 318.45. Catalog: ACM109430117.
(+/-)12-HEPE
(+/-)12-HEPE is a compound which inhibits platelet aggregation. Group: Biochemicals. Grades: Highly Purified. CAS No. 81187-21-5. Pack Sizes: 25ug, 50ug. Molecular Formula: C20H30O3, Molecular Weight: 318.45. US Biological Life Sciences.
Worldwide
12(R)-Hepe
Heterocyclic Organic Compound. Alternative Names: 12(R)-HEPE;12R-HYDROXY-5Z,8Z,10E,14Z,17Z-EICOSAPENTAENOIC ACID. CAS No. 109430-12-8. Molecular formula: C20H30O3. Mole weight: 318.45. Catalog: ACM109430128.
12(S)-Hepe
Heterocyclic Organic Compound. Alternative Names: 12(S)-HEPE;12S-HYDROXY-5Z,8Z,10E,14Z,17Z-EICOSAPENTAENOIC ACID. CAS No. 116180-17-7. Molecular formula: C20H30O3. Mole weight: 318.45. Appearance: A solution in ethanol. Purity: 0.98. Catalog: ACM116180177.
12(S)-HEPE
12(S)-HEPE is a monohydroxy fatty acid with potential antiinflammatory properties. Group: Biochemicals. Grades: Highly Purified. CAS No. 116180-17-7. Pack Sizes: 25ug, 50ug. Molecular Formula: C20H30O3, Molecular Weight: 318.45. US Biological Life Sciences.
Worldwide
15(S)-HEPE
15(S)-HEPE is a monohydroxy fatty acid. 15(S)-HEPE is biosynthesized from eicosapentaenoic acid by 15-lipoxygenase (15-LO). Serum levels of 15(S)-HEPE are elevated in patients with asthma. Uses: Scientific research. Group: Signaling pathways. Alternative Names: 15(S)-hydroxy-Eicosapentaenoic acid; 15(S)-hydroxy EPA. CAS No. 86282-92-0. Pack Sizes: 25 μg (314.02 μM * 250 μL in Ethanol); 50 μg (314.02 μM * 500 μL in Ethanol). Product ID: HY-130675A.
15(S)-HEPE
15(S)-HEPE is a polyunsaturated fatty acid that is a monohydroxy fatty acid synthesized from EPA by the action of 15-LO. Synonyms: 15S-hydroxy-5Z,8Z,11Z,13E,17Z-eicosapentaenoic acid. Grades: ≥95%. CAS No. 86282-92-0. Molecular formula: C20H30O3. Mole weight: 318.45.
18-HEPE
18-HEPE (18-Hydroxy-5(Z), 8(Z), 11(Z), 14(Z), 16(E)-eicosapentaenoic acid) is an ester product. Uses: Scientific research. Group: Signaling pathways. Alternative Names: 18-Hydroxy-5(Z), 8(Z), 11(Z), 14(Z), 16(E)-eicosapentaenoic acid. CAS No. 141110-17-0. Pack Sizes: 25 μg (314.02 μM * 250 μL in Ethanol). Product ID: HY-101495.
20-HEPE
20-HEPE is a metabolite of eicosapentaenoic acid that is formed via ω-oxidation of EPA by cytochrome P450 (CYP) ω-oxidases, including human CYP4F3B. Grades: ≥95%. CAS No. 116477-57-7. Molecular formula: C20H30O3. Mole weight: 318.5.
Heterocyclic Organic Compound. Alternative Names: (8)S-HEPE;8S-HYDROXY-5Z,9E,11Z,14Z,17Z-EICOSAPENTAENOIC ACID. CAS No. 118492-81-2. Molecular formula: C20H30O3. Mole weight: 318.5. Canonical SMILES: CC / C=C\\\\C / C=C\\\\C / C=C\\\\C=C\\\\[C@H] (C / C=C\\\\CCCC (=O) O) O. Catalog: ACM118492812.
8(S)-HEPE
8(S)-HEPE is a monohydroxy fatty acid produced by lipoxygenase oxidation of EPA. It acts to promote hatching of barnacle eggs at 10 nM, although it is not clearly identified as the natural egg hatching factor. Uses: Scientific research. Group: Signaling pathways. CAS No. 118492-81-2. Pack Sizes: 25 μg (314.02 μM * 250 μL in Ethanol); 50 μg (314.02 μM * 500 μL in Ethanol). Product ID: HY-126108A.
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