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Filtered Search Results
Sigma Aldrich Fine Chemicals Biosciences Proteinase K from Tritirachium album | 39450-01-6 | MFCD00132129 | 5mg
Proteinase K from Tritirachium album | Mol Wt: 28.93 kDa | 39450-01-6 | MFCD00132129 | 5mg
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Sigma Aldrich Fine Chemicals Biosciences Papain from papaya latex lyophilized powder, ≥10 units/mg protein | 9001-73-4 | MFCD00131791 | 50mg
Papain from papaya latex lyophilized powder, ≥10 units/mg proteinMW: | 9001-73-4 | MFCD00131791 | 50mg
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Cayman Chemical Coenzyme Q1 5mg
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An electron acceptor and a derivative of the mitochondrial electron transport chain cofactor CoQ10; induces the permeability transition pore opening and induces apoptosis in clone 9 cells at 50 µM; is used as a marker for mitochondrial complex I activity in perfused tissue and subcellular fractions
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Cayman Chemical N-Oleoyl-L-SerIn 5mg
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An endogenous lipid that has been reported to stimulate bone formation and to inhibit bone resorption
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Cayman Chemical Coenzyme Q1 1mg
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An electron acceptor and a derivative of the mitochondrial electron transport chain cofactor CoQ10; induces the permeability transition pore opening and induces apoptosis in clone 9 cells at 50 µM; is used as a marker for mitochondrial complex I activity in perfused tissue and subcellular fractions
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Worthington Biochemical Corporation DEOXYRIBONUCLEASE I
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Ribonuclease And Protease Free
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Sigma Aldrich Fine Chemicals Biosciences Deoxyribonuclease I bovine2MG
Deoxyribonuclease I bovine2MG
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INTACT GENOMICS INC Taq DNA Ligase 10,000 Units
Taq DNA Ligase catalyzes the formation of a phosphodiester bond in duplex DNA containing adjacent 5′-phosphoryl and 3′-hydroxyl termini, using NAD+ as a cofactor. The ligation will occur only if the oligonucleotides are perfectly paired to the complementary target DNA and have no gaps between them; therefore, a single-base substitution can be detected. This product is active at elevated temperatures (45°C-70°C) (1, 2).Applications Allele-specific gene detection by using Ligase Detection Reaction (LDR) and Ligase Chain Reaction (LCR) (1). Mutagenesis by incorporation of a phosphorylated oligonucleotide during primer extension amplification(3).
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COMPLEMENT TECHNOLOGY INC IC3B PROTEIN
NC0472948 IC3B PROTEIN
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New England Biolabs, Inc. EarI – 2500 units
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A restriction endonuclease that recognizes the sequence CTCTTCN^NNN_.
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New England Biolabs, Inc. Factor Xa Protease – 50 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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New England Biolabs, Inc. Endonuclease VIII – 1000 units
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Endonuclease VIII from E. coli acts as both an N-glycosylase and an AP-lyase. The N-glycosylase activity releases damaged pyrimidines from double-stranded DNA, generating an apurinic (AP site). The AP-lyase activity cleaves 3' and 5' to the AP site leaving a 5' phosphate and a 3' phosphate. Damaged bases recognized and removed by Endonuclease VIII include urea, 5, 6- dihydroxythymine, thymine glycol, 5-hydroxy-5- methylhydantoin, uracil glycol, 6-hydroxy-5, 6-dihydrothymine and methyltartronylurea. While Endonuclease VIII is similar to Endonuclease III, Endonuclease VIII has and lyase activity while Endonuclease III has only lyase activity.
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New England Biolabs, Inc. PNGase F (Glycerol-free) – 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 (Glycerol-free) is an amidase, which cleaves between the innermost GlcNAc and asparagine residues of high mannose, hybrid, and complex oligosaccharides.
- Glycerol-free for optimal performance in HPLC and mass spectrometry analysis
- >= 95% purity, as determined by SDS-PAGE and intact ESI-MS
- Non-recombinant with no detectable endoglycosidase F1, F2 or F3 contamination
- Optimal activity and stability for up to 24 months
- Can be used under native or denaturing conditions
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INTACT GENOMICS INC Endonuclease IV (Nfo) 5000 Units (10 units/µl)
Endonuclease IV (Nfo) from Escherichia coli is a 32-kD metalloprotein that aids in the repair of damaged DNA. The enzyme functions both as an apurinic/apyrimidinic nuclease (1) and as a 3′-terminal di-esterase (1-4). Its 3′-terminal di-esterase activity is important in the repair of DNA strand breaks generated by oxidation and ionic radiation (2, 3). In such events, the strand breaks terminate with either a 3′ phosphate or a deoxyribose fragment, preventing repair by DNA polymerase I or DNA ligase. Endonuclease IV removes the blocking groups, leaving a free 3′-hydroxyl terminus. This enzyme does not have detectable associated exonuclease or DNA N-glycosylase activity (1).Applications• Single cell gel electrophoresis (Comet assay) (5, 6)• Alkaline elution (7)• Alkaline unwinding (8)Product SourceE. coli BL21 (DE3) strain expressing E. coli Endonuclease IV gene.Product Includes• Endonuclease IV (Nfo)• 10x Endonuclease IV reaction buffer
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INTACT GENOMICS INC T4 DNA Ligase 100,000 Units (2000 units/µl)
Intact Genomics T4 DNA Ligase catalyzes the formation of a phosphodiester bond between juxtaposed 5’-phosphate and 3’-hydroxyl termini in duplex DNA or RNA. This enzyme joins DNA fragments with either cohesive or blunt termini and repairs single stranded nicks in duplex DNA, RNA or DNA/RNA hybrids (1).Applications• Cloning of restriction enzyme generated DNA fragments• Cloning of PCR products• Next-gen library preparation• Joining linkers and adapters to cohesive or blunt-ended DNA• Nick repair in duplex DNA, RNA or DNA/RNA hybrids• Self-circularization of linear DNA
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