Modifying Enzymes
![Chem-Impex International, Inc. Proteinase K from Tritirachium album [EC 3.4.21.64] | 39450-01-6 | MFCD00132129 | 1G](https://assets.fishersci.com/TFS-Assets/CCG/product-images/default.jpg-250.jpg)
Chem-Impex International, Inc. Proteinase K from Tritirachium album [EC 3.4.21.64] | 39450-01-6 | MFCD00132129 | 1G
Proteinase K from Tritirachium album [EC 3.4.21.64], 39450-01-6, MFCD00132129, 1G
New England Biolabs, Inc. Bacteroides Heparinase II – 200 units
Bacteroides Heparinase II (also called Heparin Lyase II) is cloned from Bacteroides eggerthii. It is a low specificity enzyme that is active on both heparin and heparan sulfate. Bacteroides Heparinase II cleaves the glycosidic bond between N-sulfated and glucuronic or iduronic acid residues. The reaction yields oligosaccharide products containing unsaturated uronic acids which can be detected by UV spectroscopy at 232 nm. When used alone this enzyme rarely yields complete depolymerization of a polysaccharide chain, however disaccharide analysis is enhanced when used in combination with Heparinase I and III.
New England Biolabs, Inc. Bacteroides Heparinase I – 240 units
Bacteroides Heparinase I, also called Heparin Lyase I, is active on heparin and the highly sulfated domains of heparan sulfate. The reaction yields oligosaccharide products containing unsaturated uronic acids which can be detected by UV spectroscopy at 232 nm.
Sigma Aldrich Fine Chemicals Biosciences Proteinase from Aspergillus melleus Type XXIII, >=3 units/mg solid | 9001-92-7 | MFCD00132092 | 25G
Proteinase from Aspergillus melleus Type XXIII, >=3 units/mg solid | 9001-92-7 | MFCD00132092 | 25G
ABclonal Technology T3 DNA Ligase
T3 DNA Ligase is an ATP-dependent ds DNA ligase from bacteriophage T3. It can catalyze the formation of a phosphodiester bond between juxtaposed 5 phosphate and 3 hydroxyl termini in duplex DNA or RNA. T3 DNA Ligase will join blunt end and cohesive end termini. It and can also repair single-stranded nicks in duplex DNA, RNA or DNA/RNA hybrids and close the gaps in these DNA substrates. In addition, T3 DNA Ligase is more tolerant to NaCl than T4 DNA Ligase (2-fold). As with T4 DNA Ligase , addition of PEG 6000 to the T3 DNA Ligase reaction system can improve the ligation efficiency of the blunt end. 1X T4 DNA Ligase Reaction Buffer can be used in some experiments where PEG 6000 is not available, but the activity of T3 DNA Ligase is reduced to 1/10. In applications where high concentrations of NaCl need to be maintained, we recommend the use of reaction buffers without PEG 6000.
Sigma Aldrich Fine Chemicals Biosciences Phosphatase, Acid from potato lyophilized powder, >=3.0 units/mg solid | 9001-77-8 | MFCD00131847 | 50UN
Phosphatase, Acid from potato lyophilized powder, >=3.0 units/mg solid | 9001-77-8 | MFCD00131847 | 50UN
Sigma Aldrich Fine Chemicals Biosciences Proteinase from Aspergillus melleus Type XXIII, >=3 units/mg solid | 9001-92-7 | MFCD00132092 | 5G
Proteinase from Aspergillus melleus Type XXIII, >=3 units/mg solid | 9001-92-7 | MFCD00132092 | 5G
Medchemexpress LLC α-amylase-IN-3 | 93944-58-2 | 99.5% | 267.24 g/mol | C15H9NO4 | 10 MG
α-Amylase-IN-3 is a small-molecule research reagent reported to inhibit α-amylase and acetylcholinesterase, and to exhibit antioxidant activity. It is supplied as a solid for laboratory research and is used in studies related to diabetes and oxidative stress-associated disease.
- Non-competitive α-amylase inhibitor with reported IC50 ≈ 18.04 μM.
- Acetylcholinesterase inhibitory activity with reported IC50s ≈ 21.04 μM and 22.2 μM.
- Demonstrates antioxidant activity in standard radical-scavenging assays.
- Supplied as a stable solid suitable for laboratory storage and handling.
- High reported purity (≈99.49% by HPLC).
- Molecular weight 267.24 g/mol; chemical formula C15H9NO4.
ABclonal Technology Endonuclease IV
Endonuclease IV derived from E. coli recognizes the depurine/depyrimidine (AP) site on the double- stranded DNA molecule, and cleaves the first phosphodiester bond at the 5 ?end of the AP site to form 3-OH and 5dRP . In addition, Endonuclease IV has 3?diesterase activity, which releases phosphoglyceraldehyde, intact deoxyribose 5 -phosphate, and phosphoric acid from the 3 ?end of DNA. The best substrate for this enzyme is AP double-stranded DNA, but it is also active against AP single-stranded DNA.
Sigma Aldrich Fine Chemicals Biosciences Neuraminidase from Clostridium perfringens (C. welchii) | 9001-67-6 | MFCD00131711 | 2.5un
Neuraminidase from Clostridium perfringens (C. welchii) | 9001-67-6 | MFCD00131711 | 2.5un
Bioss KD-Validated DNA ligase 4 Rabb
DNA Ligase 4 Primary Antibody Unconjugated Public Immunogen Range 504-685/911 Host Species Rabbit Target Species Human Clonality Monoclonal Applications WB FCM IC Concentration Lot dependent Size 50 ul Storage Buffer Supplied in PBS (pH 7 4) containing 50% glycerol and 0 02% sodium azide
STEMCELL Technologies DNase I, ACF, Size: 500000 U
Deoxyribonuclease I (DNase I), Animal Component-Free (ACF) is obtained from cultures free of animal-derived materials and purified by chromatography. DNase I is an endonuclease consisting of a single glycosylated polypeptide chain with two disulfide bonds. DNase is often included in tissue dissociation protocols to digest DNA that has leaked into the dissociation medium as a result of cell damage. DNase I, ACF preferentially cleaves phosphodiester linkages adjacent to pyrimidine nucleotides in both single- and double-stranded DNA, yielding polynucleotides with 5’-phosphate and 3’-hydroxyl groups (Bernardi et al.). DNase I has been used for the digestion of human tissues such as microglia (Klegeris & McGeer), cartilage (Dunham & Koch), colon (Fukushima & Fiocchi), epithelium l (Fukushima & Fiocchi), liver (Vatakis et al.), lung (Fujino et al.), neural (Fuja et al.), and stem cells (Kusuma et al.).