Recombinant Mouse Uracil-DNA glycosylase (Ung)

Code CSB-YP025641MO
MSDS
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Source Yeast
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Code CSB-EP025641MO
MSDS
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Source E.coli
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Code CSB-EP025641MO-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP025641MO
MSDS
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Source Baculovirus
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Code CSB-MP025641MO
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Ung
Uniprot No.
Alternative Names
Ung; Ung1; Uracil-DNA glycosylase; UDG; EC 3.2.2.27
Species
Mus musculus (Mouse)
Expression Region
1-306
Target Protein Sequence
MIGQKTLYSF FSPTPTGKRT TRSPEPVPGS GVAAEIGGDA VASPAKKARV EQNEQGSPLS AEQLVRIQRN KAAALLRLAA RNVPAGFGES WKQQLCGEFG KPYFVKLMGF VAEERNHHKV YPPPEQVFTW TQMCDIRDVK VVILGQDPYH GPNQAHGLCF SVQRPVPPPP SLENIFKELS TDIDGFVHPG HGDLSGWARQ GVLLLNAVLT VRAHQANSHK ERGWEQFTDA VVSWLNQNLS GLVFLLWGSY AQKKGSVIDR KRHHVLQTAH PSPLSVHRGF LGCRHFSKAN ELLQKSGKKP INWKEL
Protein Length
Full length protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

Customer Reviews and Q&A

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Target Background

Function
Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
Gene References into Functions
  1. Pms2/Mlh1 and multiple uracil glycosylases act jointly, each one with a distinct strand bias, to enlarge the immunoglobulin gene mutation spectrum from G-C to A-T bases. PMID: 28283534
  2. UNG deficiency reduces B cell clonal expansion in the germinal center in mice and blocks the proliferation of tumor B cells expressing AID. PMID: 27697833
  3. UNG might be involved in Tet-mediated DNA demethylation. PMID: 26620559
  4. Study showed elevated levels of homocysteine via dietary folic acid deficiency and chronic hypoperfusion negatively affect learning in Ung deficient mice, while increasing GFAP immunoreactivity within the dentate gyrus of the hippocampus PMID: 25655513
  5. Ung and Pms2 may exert a mutual backup function for the DNA incision that promotes synthesis by Poleta, each with a distinct strand bias. PMID: 24710273
  6. Differential regulation of S-region hypermutation and class-switch recombination by noncanonical functions of uracil DNA glycosylase. PMID: 24591630
  7. Our results uncover a specific need for UNG in class-switch recombination for timely and efficient acute Ab responses in vivo PMID: 23667108
  8. Compared with WT mice, UNG deficiency caused elevated frequency of C:G mutations, suggesting that UNG-mediated U excision led to error-free as well as error-prone repair. PMID: 22960197
  9. we show that AID binds cooperatively with UNG and the mismatch repair proteins Msh2-Msh6 to Ig Smu and Sgamma3 regions PMID: 21804017
  10. analysis of species specific differences between mouse and humans in regulation of SMUG1 and UNG2 PMID: 21454529
  11. The frequency of the D-1 mitochondrial (mt)DNA deletion in mtDNA is significantly increased in Ung-deficient mice, hence folate deficiency may contribute to neurodegeneration via mtDNA damage. PMID: 21281628
  12. Immunoglobulin isotype switching is inhibited and somatic hypermutation perturbed in mice deficient in this enzyme. PMID: 12401169
  13. Results provide compelling evidence that uracil-DNA glycosylase is of major importance for tissue repair after brain ischemia. PMID: 15199406
  14. results indicate UNG is involved in the repair step of immunoglobulin class switch recombination (CSR) yet by an unknown mechanism; dispensability of U removal in the DNA cleavage step of CSR requires reconsideration of the model of DNA deamination by AID PMID: 15326357
  15. Data show that protein synthesis but not uracil DNA glycosylase is required for the DNA cleavage step of immunoglobulin somatic hypermutation. PMID: 15684068
  16. Ung-proteins, directly or indirectly, have important functions in the immune system, not only in the process of antibody maturation, but also for production and functions of immunologically important cell types PMID: 16174566
  17. uracil-excision repair in oocytes is likely to be mediated by Udg2v2, or alternatively that Udg2v2 is involved in a process related to oocyte-specific maturation by virtue of its cyclin-like domains PMID: 16697536
  18. Inactivating Ung alone reduced mutations from A and T, suggesting that, depending on the DNA sequence, varying proportions of A,T mutations arise by error-prone long-patch base excision repair PMID: 17015724
  19. AID and Ung generate staggered double-strand DNA breaks (DSBs) not only by cleaving intact double-strand DNA, but also by processing blunt DSB ends. PMID: 18760480
  20. The concerted action of Msh2 and UNG in stimulating A . T mutations also may have implications for mutagenesis at sites of spontaneous cytidine deamination. PMID: 19596785
  21. Dependence of nucleotide substitutions on Ung2, Msh2, and PCNA-Ub during somatic hypermutation. PMID: 19901081

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Subcellular Location
[Isoform 1]: Mitochondrion.; [Isoform 2]: Nucleus.
Protein Families
Uracil-DNA glycosylase (UDG) superfamily, UNG family
Database Links
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