| Description | Storage buffer: 50mM Tris, 50mM KCl, 1mM DTT, 0.05mM EDTA, 50% Glycerol, 200 µg/ml HSA, pH 8.0Exonuclease III has 3 '→5' exonuclease activity on double-stranded DNA, which can degrade flat end, 3 'end dented and incised DNA, and degrade DNA molecules from the 3' end. For 3 'protruding Storage buffer: 50mM Tris, 50mM KCl, 1mM DTT, 0.05mM EDTA, 50% Glycerol, 200 µg/ml HSA, pH 8.0Exonuclease III has 3 '→5' exonuclease activity on double-stranded DNA, which can degrade flat end, 3 'end dented and incised DNA, and degrade DNA molecules from the 3' end. For 3 'protruding ends, especially protruding DNA molecules 4 nt or longer cannot be cut at all. In addition, the active site of the enzyme depends on the helical structure and varies according to the sequence (C>A=T>G).Product composition:rp216608Component5KU25KUStoragerp216608AExonuclease III50 µL250 µL-20°C. Avoid freeze/thaw cyclerp216608B10×Exonuclease III Reaction Buffer750 µL3.75 mL-20°C. Avoid freeze/thaw cycleSourceE.coliEnzyme Activity DefinitionThe amount of enzyme required to catalyze the production of 1 nmol acid-soluble total nucleotide in a 50 µl reaction system at 37℃ for 30 min is defined as 1 unit (U).Applications(1) Non-directional nested deletion;(2) Site-directed mutagenesis;(3) Preparation of chain specific probes;(4) Preparation of single-stranded substrates for dideoxy sequencing.Protocol(1) Configure the reaction system, as shown in the following tableComponentVolumeDNA5 µg10×Exonuclease III Reaction Buffer5 µlExonuclease III0.5 µlNuclease-free WaterUp to 50 µl(2) Incubation at 37 "C for 30min.(3) Incubation at 75°C for 10 min terminated the reaction.Cautions(1) The reaction temperature, the concentration of salt ions in the system and the ratio of enzyme to DNA will affect the activity of the enzyme.(2) This product is for scientific research only and shall not be used for other purposes... Read More | Amyloid β-Protein Fragment 25-35 (Aβ25-35) is derived from the amyloid-β protein.amyloid-β protein, which is mapped to human chromosome 21q21.Aβ25-35 lacks the N-terminal domain and the metal binding site and is majorly generated by proteolytic cleavage of Aβ(1−40Amyloid β-Protein Fragment 25-35 (Aβ25-35) is derived from the amyloid-β protein.amyloid-β protein, which is mapped to human chromosome 21q21.Aβ25-35 lacks the N-terminal domain and the metal binding site and is majorly generated by proteolytic cleavage of Aβ(1−40) peptides. It has a β-sheet and β-turn structure. Amino Acid Sequence Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-MetFunctional domain of Aβ required for both neurotrophic and neurotoxic effects... Read More | Biochemical Test:SDS-PAGE (purity > 80%); Western blot with patient sample.Calculated Isoelectric Point:pH 4.19 | Purity>95% (SDS-PAGE) Endotoxin level<1.0 EU/µgFunctionInhibits the synthesis of a number of cytokines, including IFN-gamma, IL-2, IL-3, TNF and GM-CSF produced by activated macrophages and by helper T-cells | Protein:BSA-Free |