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Filtered Search Results
Ubpbio GST-HRV 3C Protease, 1 MG
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Protein Purification Reagents - GST-HRV 3C Protease -Human rhinovirus 3C protease (HRV 3C Protease) is a cysteine protease that recognizes the Leu-Glu-Val-Leu-Phe-Gln-Gly-Pro sequence (also called the PreScission site), and cleaves between Gln and Gly. The recombinant GST-HRV 3C can be used to cleave the GST tag in fusion proteins expressed using the pGEX-6p vector or other vectors, then removed by glutathione resin. It exhibits high specificity and activity at 4 0C in an overnight incubation reaction containing 1 mass unit of HRR 3C and 100 mass units of targeting protein.
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Bioassay Systems QuantiChrom™ Pectinase Assay Kit. For quantitative determination of pectinase activity determination in biological samples.
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For quantitative determination of pectinase activity determination in biological samples. Key Features: Linear detection range from 9.2-100 U/L pectinase activity in a 96-well plate assay. Simple and convenient 40 minute "Add-Mix-Measure" type assay. High-throughput format and compatible with laboratory liquid handling systems. No heating required. The kit does not use toxic materials. Refer to the previously established DNS method. Method: OD600nm. Samples: Enzyme extracts, agriculture and biological samples. Species: Plant, fungal tissues, juice, bacteria, etc. Procedure: Assay takes 40 min. Kit size: 100 tests. Detection limit: 9.2 U/L.
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Research Products International Corp Proteinase K, 100 Milligrams
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From Tritirachium album. Serine protease for proteolytic inactivation of nucleases during isolation of DNA and RNA.
Description
Proteinase K is a highly reactive serine protease that displays an ability to digest native proteins, thereby inactivating enzymes such as DNase and RNase without recourse to a denaturation process. It is the most powerful proteinase among all proteinases characterized so far. It cleaves at the peptide bond adjacent to the carboxylic acid group of aliphatic, aromatic or hydrophobic amino acids.
Recombinant Proteinase K is used in the isolation or preparation of high molecular weight nucleic acids. It is highly pure and has a higher specific activity and is more stable at room temperature when compared to native Proteinase K.
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Enzo Life Sciences Cyclooxygenase (sheep), (purified) (1mg)
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Alternative name: COX. Purity: ≥95%. Formulation: Liquid. In 0.1M Tris-HCl, pH 7.4 containing 1mM Tryptophan and 1% Tween-80. Source: Isolated from ram seminal vesicles. Long Term Storage: -80°C.
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New England Biolabs, Inc. PNGase F – 15000 units
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PNGase F is the most effective enzymatic method for removing almost all N-linked oligosaccharides from glycoproteins. PNGase F is an amidase, which cleaves between the innermost GlcNAc and asparagine residues of high mannose, hybrid, and complex oligosaccharides.
- Leaves N-glycan core oligosaccharides intact and suitable for further analysis
- Non-recombinant with no detectable endoglycosidase F1, F2 or F3 contamination
- >= 95% purity, as determined by SDS-PAGE and intact ESI-MS
- Stored in 50% glycerol
- Optimal activity and stability for up to 24 months
- Can be used under native or denaturing conditions
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New England Biolabs, Inc. α2-3,6,8 Neuraminidase - 10000 units
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2-3,6,8 Neuraminidase catalyzes the hydrolysis of 2-3, 2-6, and 2-8 linked sialic acid residues from glycoproteins and oligosaccharides.
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New England Biolabs, Inc. Lambda Protein Phosphatase – 20000 units
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Lambda Protein Phosphatase is a Mn2+-dependent protein phosphatase with activity towards phosphorylated serine, threonine and tyrosine residues.
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New England Biolabs, Inc. Antarctic Phosphatase – 1000 units
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Antarctic Phosphatase (AnP) is a heat labile alkaline phosphatase purified from a recombinant source. AnP nonspecifically catalyzes the dephosphorylation of 5' and 3' ends of DNA and RNA phosphomonoesters. Also, AnP Hydrolyses ribo-, as well as deoxyribonucleoside triphosphates (NTPs and dNTPs). AnP is useful in many molecular biology applications such as the removal of phosphorylated ends of DNA and RNA for subsequent use in cloning or end-labeling of probes. In cloning, dephosphorylation prevents religation of linearized plasmid DNA. The enzyme acts on 5' protruding, 5' recessed, and blunt ends. AnP may also be used to degrade unincorporated dNTPs in PCR reactions to prepare templates for DNA sequencing or SNP analysis. AnP is completely and irreversibly inactivated by heating at 80C for 2 minutes, thereby making removal of AnP prior to ligation or end-labeling unnecessary.
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New England Biolabs, Inc. Factor Xa Protease – 250 µg
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Factor Xa cleaves after the arginine residue in its preferred cleavage site Ile-Glu/Asp-Gly-Arg. It will sometimes cleave at other basic residues, depending on the conformation of the protein substrate. The most common secondary site, among those that have been sequenced, is Gly-Arg.
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Aldevron SpCas9 Nuclease, 0.25mg
0.25mg dispense of SpCas9 Nuclease. Aldevron provides Research-grade Cas9 nucleases via Fisher Scientific for use in development work as well as standard cGMP products for clinical studies when ordered direct.
Functional Performance
•Ready to use for electroporation or transfection
•Extensive QC panels
•10 mg/mL formulation
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Qiagen Beverly Inc RNASE H
Ribonuclease; RNAse H; Conc. 5,000 U/ul; 5,000 U; incl. 10X buffer
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Enzo Life Sciences p300 (catalytic domain) (human), (recombinant) (100 µg)
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Synonyms: E1A binding protein p300, Histone acetyltransferase p300. MW: 45.1 kDa. UniProt ID: Q09472. Source: Produced in E. coli. Catalytic domain (aa 1284-1673) of human p300. Purification: Partially purified by single-step affinity chromatography and gel filtration. Formulation: Liquid. In 50mM TRIS/HCl, pH 8.0, containing 0.1mM EDTA, 10% glycerol.
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AG Scientific Inc Lactate Oxidase, 1 KU
Lactate oxidase is a flavin mononucleotide-dependent alpha hydroxyl acid oxidizing enzyme. Lactate oxidase is useful for enzymatic determination of lactic acid. It uses molecular oxygen to catalyze the oxidation of L-lactate.Lactate oxidase enzymes belong to the family of oxidoreductase which act on single donors with O2 as oxidants. The enzymes often come from Aerococcus viridian and appear in viruses and cellular organisms.CAS Number: 9028-72-2Molecular Weight: 80 kDa (gel filtration)Storage Temperature: -20CResearch or further manufacturing use only, not for food or drug use.
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AG Scientific Inc Proteinase K, 500 MG
Proteinase K is a highly reactive serine protease that displays an ability to digest native proteins, thereby inactivating enzymes such as DNase and RNase without recourse to a denaturation process. It is the most powerful proteinase among all proteinases characterized so far. It cleaves at the peptide bond adjacent to the carboxylic acid group of aliphatic, aromatic or hydrophobic amino acids. Recombinant Proteinase K is used in the isolation or preparation of high molecular weight nucleic acids. It is highly pure and has a higher specific activity and is more stable at room temperature when compared to native Proteinase K.CAS Number: 39450-01-06Molecular Weight: 29.3 kDaSolubility: 50mM Tris-HCl (pH 7.5), 3mM CaCl2, 50% GlycerolStorage Temperature: +4CResearch or further manufacturing use only, not for food or drug use.
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AG Scientific Inc RNase A, 100 MG
RNase stands for ribonuclease, an RNA digesting enzyme. RNase consists of 124 amino acids in one polypeptide chain with 4 disulphide linkages. Ribonucleases can be divided into endoribonucleases and exoribonucleases. RNases have important roles in RNA degradation and turnover in all organisms. Ribonuclease enzyme can unwind the RNA helix by complexing with single-stranded RNA. RNase A is an endoribonuclease with functions in RNA metabolism and regulation of gene expression. It was found to play roles in diseases such as autoimmune diseases, renal insufficiencies and pancreas disorder.CAS Number: 9001-99-4Chemical Formula: C9H14N4O3Storage Temperature: -20CResearch or further manufacturing use only, not for food or drug use.
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