Seattle Genova offers our customers excellent protein production services that keep the bioactivities of your proteins just as they were in nature. To achieve this, we can offer both nature protein purification services and recombinant protein production services. We have developed very specialized protocols to make sure the produced proteins will maintain their biological activities. And our well-developed bioassays can ensure comprehensive activity validations before we release the proteins.
A nuclearse (also archaically recognized as nucleodepolymerase or polynucleotidase) is an enzyme capable of cutting the phosphodiester bonds between nucleotides of nucleic acids. Nucleases variously affect single and double-stranded cuts in their target molecules. Living organisms are important machinery for several aspects of DNA repair. Defects in certain nucleases can affect genetic instability or immunodeficiency. Nucleases are also largely utilized in molecular cloning. There are two primary categories based on the locus of activity. Exonucleases eat nucleic acids from the ends. Endonucleases act on areas in the middle of target molecules. They are categorised as deoxyribonucleases and ribonucleases. The former acts on DNA, and the last on RNA.
Metal ion dependence and independent nucleases classes
Two-metal-ion dependent nuclease Superfamilies
DnaQ-like 3´- 5´ exonucleases with the DEDD motif, RNase H-like endonuclease, The major REase fold with the D-(D/E)XK motif
One-metal-ion dependent nuclease Superfamilies
The ββα-Me superfamily, GIY-YIG endonucleases, The HUH superfamily
Partial metal ion dependence
TOP RIM topoisomerases, Ser recombinases
RNase T1, Barnase and microbial RNases, Colicin D and E5,
RNase A, RNase T2,tRNA splicing endonuclease, Ferredoxin-fold Cas6
Metal-ion independent DNases
DNases with phospholipase D (PLD) fold, Type IB topoisomerase and Tyr recombinase, Halfpipe restriction endonuclease
√The bioactivity Long-term data
√The purified proteins are also shipped to our customers for them to test internally
1.Friedhoff P, Gimadutdinow O, et al. 1994, Protein Expr Purif, 5 (1): 37-43
2.Nishino T, Morikawa K (December 2002). "Structure and function of nucleases in DNA repair: shape, grip and blade of the DNA scissors". Oncogene. 21 (58): 9022–32.
3.Arber W, Linn S (1969). "DNA modification and restriction". Annual Review of Biochemistry. 38: 467–500.
4.Nestle M, Roberts WK. 1969, J Biol Chem, 10, 244 (19): 5213-5218
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