Recombinant Human Uracil-DNA glycosylase (UNG)

Code CSB-YP025641HU
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Source Yeast
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Code CSB-EP025641HU
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Source E.coli
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Code CSB-EP025641HU-B
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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-BP025641HU
MSDS
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Source Baculovirus
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Code CSB-MP025641HU
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
UNG
Uniprot No.
Alternative Names
DGU; DKFZp781L1143; HIGM 4; HIGM4; OTTHUMP00000240527; OTTHUMP00000240528; OTTHUMP00000240529; UDG; UNG 1; UNG 15; ung; UNG_HUMAN; UNG1; UNG15; UNG2; Uracil DNA glycosylase 1; Uracil DNA glycosylase 2; Uracil DNA glycosylase; Uracil-DNA glycosylase
Species
Homo sapiens (Human)
Expression Region
1-313
Target Protein Sequence
MIGQKTLYSF FSPSPARKRH APSPEPAVQG TGVAGVPEES GDAAAIPAKK APAGQEEPGT PPSSPLSAEQ LDRIQRNKAA ALLRLAARNV PVGFGESWKK HLSGEFGKPY FIKLMGFVAE ERKHYTVYPP PHQVFTWTQM CDIKDVKVVI LGQDPYHGPN QAHGLCFSVQ RPVPPPPSLE NIYKELSTDI EDFVHPGHGD LSGWAKQGVL LLNAVLTVRA HQANSHKERG WEQFTDAVVS WLNQNSNGLV FLLWGSYAQK KGSAIDRKRH HVLQTAHPSP LSVYRGFFGC RHFSKTNELL QKSGKKPIDW KEL
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. UDG depleted cancer cells displayed sustained DNA damage following 5-FdU treatment PMID: 27517750
  2. Uracil excision by bacterial UDG and human hUNG2 is reduced at uracils positioned directly 5' or 3' of a G-quadruplex DNA structures. PMID: 26671821
  3. The UNG1-PRDX3 interaction protected UNG1 from reactive oxygen species-mediated degradation and prevented mitochondrial DNA oxidation. PMID: 27480846
  4. Characterization of the ability of hUNG2 to translocate on DNA. PMID: 29036472
  5. Data indicate that DNA glycosylases MYH, UNG2, MPG, NTH1, NEIL1, 2 and 3 on nascent DNA. PMID: 28575236
  6. Although the N-terminal domain has minimal effects on DNA binding and uracil excision kinetics, this study reports that this domain enhances the ability of human UNG2 to translocate on DNA chains as compared to the catalytic domain alone. PMID: 28787572
  7. Over-expression of uracil DNA glycosylase 2 in HepG2 protect cells against oxidative stress damage. PMID: 28395718
  8. Results suggest that the UNG2 N-terminus may serve as a flexible scaffold to tether PCNA and RPA at the replication fork, and that post-translational modifications on the UNG2 N-terminus disrupt formation of the PCNA-UNG2-RPA protein complex. PMID: 28746850
  9. HIV-1 vpr reprograms CRL4(DCAF1) E3 to direct HLTF for proteasome-dependent degradation independent from previously reported Vpr interactions with base excision repair enzyme uracil DNA glycosylase (UNG2) and crossover junction endonuclease MUS81, which Vpr also directs for degradation via CRL4(DCAF1) E3. PMID: 27335459
  10. Uracil DNA glycosylase (UNG) is the primary glycosylase responsible for the removal of uracils adjacent to cisplatin ICLs, whereas other uracil glycosylases can process uracils in the context of undamaged DNA. PMID: 28110804
  11. find that the energetic nature of the observed binding free energies of human 8-oxoguanine DNA glycosylase (hOGG1) and human uracil DNA glycosylase (hUNG) for undamaged DNA are derived from different sources. Although hOGG1 uses primarily nonelectrostatic binding interactions with nonspecific DNA, hUNG uses a salt-dependent electrostatic binding mode PMID: 27571472
  12. The authors show that Vpr can form a trimolecular complex with UNG2 and RPA32 and the positive effect of UNG2 and RPA32 on the reverse transcription process leading to optimal virus replication and dissemination between the primary target cells of HIV-1. PMID: 27068393
  13. Data suggest novel mechanism in innate immunity allows cytokine TGF-beta to restrict viral circular DNA in hepatocyte nuclei via innate immunity; AID deaminates circular DNA of hepatitis B virus leading to DNA degradation; mechanism depends on UNG. PMID: 26867650
  14. UNG rs246079 G/A contributes to decreased risk of esophageal cancer in a Chinese population. PMID: 25301111
  15. base excision by UNG1/2 perturbs transcription of the affected gene PMID: 24951587
  16. UNG interaction with damaged DNA is dominated by the nonelectrostatic free energy term (DeltaGnon = -7.2 +/- 0.1 kcal mol(-1)), yet retains the nonspecific electrostatic contribution (DeltaGelect = -2.3 +/- 0.2 kcal mol(-1)). PMID: 25408964
  17. Data shows that cancer cells express UNG2 gene at levels similar to or higher than those seen with peripheral B cells. PMID: 25154417
  18. UNG specifically interacts with Vpr forming a heterotrimeric complex with DCAF1. PMID: 20870715
  19. UNG2 colocalizes with CENP-A and H2AX phosphorylation at centromeres in normally cycling cells. PMID: 21399697
  20. Thus, in experimental models, uracil-DNA glycosylase is a critical mediator of pemetrexed sensitivity that warrants evaluation to determine clinical value PMID: 23873851
  21. The results obtained suggest the potential role of the g.4235T>C and the c.-31A>G polymorphisms in AMD pathogenesis. PMID: 23714858
  22. Performed are force-field based molecular dynamics (MD) simulations to explore the structural and dynamical properties of distinct UNG/dsDNA adducts, containing A:U, A:T, G:U, or G:C base pairs, at different stages of the base-flipping pathway. PMID: 23705837
  23. UNG excises uracil residues from the viral genome during or after cccDNA formation in the nucleus and imply that BER pathway activities decrease the antiviral effect of APOBEC3-mediated hypermutation. PMID: 23696735
  24. Loss of UNG did not alter cellular sensitivity to 5-FU in two human cell lines. PMID: 23253900
  25. the search mechanism of uracil DNA glycosylase is not predetermined but, instead, depends on the context in which the uracils are located PMID: 23506270
  26. the role of the charged DNA phosphate backbone in sliding and hopping by human uracil DNA glycosylase PMID: 23506309
  27. A comparison of haplotype frequencies between the case and the control revealed that rheumatoid arthritis patients with the Ht2 haplotype are at additional risk for rheumatoid arthritis development PMID: 22138674
  28. Data show that the R88C variant impairs binding of the R88C variant impairs binding of uracil-DNA glycosylase UNG2 to replication protein A RPA2. PMID: 22521144
  29. Data show that uracil-DNA glycosylases SMUG1 and UNG2 display widely different sequence preferences. PMID: 22483865
  30. Excision of AID-induced Uracil by UNG2 occurs predominantly during G1 phase, inducing faithful repair, mutagenic processing, and class switching. PMID: 22529268
  31. Local enrichment of UNG1 at DNA-bound mtSSB may furthermore facilitate rapid access to- and processing of the damage once the dsDNA conformation is restored. PMID: 22153281
  32. the first thermal stability analysis of Atlantic cod cUNG and human UNG by differential scanning calorimetry, is reported. PMID: 21959147
  33. Vpr acts to enhance constitutive DCAF1-dependent UNG2 turnover. PMID: 22292079
  34. Recruitment of the UNG2 into virus particles increased the infectivity of HIV-1. PMID: 22171270
  35. measured paramagnetic relaxation enhancements reveal dynamic hot spots in uracil DNA glycosylase that are highly correlated with substrate binding and recognition PMID: 22077282
  36. Study of the role of histidine-148 provides additional support for inclusion of this amino acid in the list of residues (aspartate-145 and His-268) essential to the chemical step of the UNG2 complete mechanism. PMID: 21473605
  37. analysis of species specific differences between mouse and humans in regulation of SMUG1 and UNG2 PMID: 21454529
  38. in the absence of CD40-CD154 interactions, there is a marked reduction in SHM and, specifically, mutations of AICDA-targeted G residues in RGYW motifs along with a decrease in transversions normally related to UNG2 activity. PMID: 19023113
  39. UNG2 is the major enzyme for removal of deaminated cytosine outside of replication foci in single stranded DNA PMID: 12161446
  40. More global salt bridges are found in human uracil DNA glycosylase (UDG) and are more stabilizing when compared to cod UDG, possibly playing a role in maintaining overall stability and reducing conformational entropy. PMID: 18004790
  41. XRCC1 complexes performed complete repair of uracil with higher efficacy than UNG2 complexes. PMID: 20466601
  42. the Vpr-induced decrease of UNG2 level is mainly related to a transcriptional effect PMID: 19625402
  43. X4 and R5 HIV-1 have distinct post-entry requirements for uracil DNA glycosylase during infection of primary cells PMID: 20371602
  44. Data indicate that the activity of UDG likely requires "trapping" transiently exposed states arising from the rotational dynamics of DNA on histones. PMID: 20176960
  45. The results indicated that there was a correlation between high level of UNG expression and the carcinogenesis of esophageal squamous cell carcinoma. PMID: 15969084
  46. crystal structure of free and DNA-bound enzyme PMID: 12136137
  47. Data report the characterization of a functional homologue (ung1) from Schizosaccharomyces pombe of the human uracil-DNA-glycosylase 2 (UNG2) gene. PMID: 12810074
  48. Nuclear uracil-DNA glycosylase expression was induced in activated B cells. PMID: 12958596
  49. crystallization reveals example of geometric strain, least atomic motion, and electrophile migration in biological catalysis PMID: 14580190
  50. Showed that UDG1A protein levels decrease during the S phase of the cell cycle and that it's in the ubiquitin-conjugated form when proteolysis is inhibited by inhibitors of proteosomal dependent protein degradation. PMID: 15084312

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Involvement in disease
Immunodeficiency with hyper-IgM 5 (HIGM5)
Subcellular Location
[Isoform 1]: Mitochondrion.; [Isoform 2]: Nucleus.
Protein Families
Uracil-DNA glycosylase (UDG) superfamily, UNG family
Tissue Specificity
Isoform 1 is widely expressed with the highest expression in skeletal muscle, heart and testicles. Isoform 2 has the highest expression levels in tissues containing proliferating cells.
Database Links

HGNC: 12572

OMIM: 191525

KEGG: hsa:7374

STRING: 9606.ENSP00000242576

UniGene: Hs.191334

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