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Mouse UNG Recombinant Protein (N-His) (MY404012)

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Overview
Catalog No.MY404012
Description
Recombinant Mouse UNG Protein, N-His (MY404012) expressed in E. coli, spanning Ser60-Leu306. Purity: >90% by SDS-PAGE.
Highlights
  • His-Tagged — N-terminal 6×His tag for IMAC purification.
  • E. coli Expression — High-yield, cost-effective production.
  • High Purity — >90% purity verified by SDS-PAGE.
Expression systemE. coli
AccessionP97931
Protein lengthSer60-Leu306
ApplicationsELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress
SpeciesMus musculus (Mouse)
Nature Recombinant
Endotoxin level Please contact with the lab for this information.
Purity >90% as determined by SDS-PAGE.
Predicted molecular weight 30.14 kDa
Form Lyophilized
Storage buffer Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol.

Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA.

Reconstitution Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details.
Shipping In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise.
Stability and Storage Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt.
Alternate NamesDGU, EC:3.2.2.27, UDG, UNG, UNG1, UNG15, Uracil-DNA glycosylase
Background

Uracil-DNA glycosylase is a ~33 kDa protein. Uracil-DNA glycosylase that hydrolyzes the N-glycosidic bond between uracil and deoxyribose in single- and double-stranded DNA (ssDNA and dsDNA) to release a free uracil residue and form an abasic (apurinic/apyrimidinic; AP) site. Excises uracil residues arising as a result of misincorporation of dUMP residues by DNA polymerase during replication or due to spontaneous or enzymatic deamination of cytosine. Mediates error-free base excision repair (BER) of uracil at replication forks. According to the model, it is recruited by PCNA to S-phase replication forks to remove misincorporated uracil at U:A base mispairs in nascent DNA strands. Via trimeric RPA it is recruited to ssDNA stretches ahead of the polymerase to allow detection and excision of deaminated cytosines prior to replication.

1. Torseth, K. et al. (2012) DNA repair 11, 559-69. PMID: 22521144
2. Nilsen, H. et al. (1997) Nucleic acids research 25, 750-5. PMID: 9016624
3. Rada, C. et al. (2002) Current biology : CB 12, 1748-55. PMID: 12401169
4. Maul, RW. et al. (2011) Nature immunology 12, 70-6. PMID: 21151102
5. Schrader, CE. et al. (2005) The Journal of experimental medicine 202, 561-8. PMID: 16103411
Note For research use only
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