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DNA polymerase/3'-5' exonuclease

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Strictly DNA-template-directed DNA polymerase, preferentially acting on DNA structures containing gaps from one to a few nucleotides and bearing a phosphate group at the 5' end of the downstream DNA. The fact that PolX is able to conduct filling of a single-nucleotide gap, allowing further sealing of the resulting nick by a DNA ligase, points to a putative role in base excision repair (BER) during the B.subtilis life cycle. Moreover, also possesses a 3'-5' exonuclease activity able to edit unpaired 3'-termini in a gapped DNA substrate and likely involved in resecting unannealed 3'-termini during DNA repair. The same PolX molecule could perform the subsequent gap-filling step. Does not display 5'-deoxyribose 5'-phosphate (dRP) lyase activity, as predicted by the lack of the lysine and tyrosine residues responsible for the dRP lyase activity in some other PolX members.

Below are the list of possible DNA polymerase/3'-5' exonuclease products. If you cannot find the target and/or product is not available in our catalog, please click here to contact us and request the product or submit your request for custom elisa kit production, custom recombinant protein production or custom antibody production. Custom ELISA Kits, Recombinant Proteins and Antibodies can be designed, manufactured and produced according to the researcher's specifications.
 

DNA polymerase/3'-5' exonuclease PolX

 DNA polymerase/3'-5' exonuclease PolX ELISA Kit
 DNA polymerase/3'-5' exonuclease PolX Recombinant
 DNA polymerase/3'-5' exonuclease PolX Antibody
Strictly DNA-template-directed DNA polymerase, preferentially acting on DNA structures containing gaps from one to a few nucleotides and bearing a phosphate group at the 5' end of the downstream DNA. The fact that PolX is able to conduct filling of a single-nucleotide gap, allowing further sealing of the resulting nick by a DNA ligase, points to a putative role in base excision repair (BER) during the B.subtilis life cycle. Moreover, also possesses a 3'-5' exonuclease activity able to edit unpaired 3'-termini in a gapped DNA substrate and likely involved in resecting unannealed 3'-termini duri
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ng DNA repair. The same PolX molecule could perform the subsequent gap-filling step. Does not display 5'-deoxyribose 5'-phosphate (dRP) lyase activity, as predicted by the lack of the lysine and tyrosine residues responsible for the dRP lyase activity in some other PolX members.
 polX ELISA Kit
 polX Recombinant
 polX Antibody
 yshC ELISA Kit
 yshC Recombinant
 yshC Antibody
 BSU28590 ELISA Kit
 BSU28590 Recombinant
 BSU28590 Antibody
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