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NTHL1 Antibody (Center R103)

Affinity Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - NTHL1 Antibody (Center R103) AP11554c
    All lanes : Anti-NTHL1 Antibody (Center R103) at 1:1000 dilution Lane 1: DU145 whole cell lysate Lane 2: Hela whole cell lysate Lysates/proteins at 20 µg per lane. Secondary Goat Anti-Rabbit IgG, (H+L), Peroxidase conjugated at 1/10000 dilution. Predicted band size : 34 kDa Blocking/Dilution buffer: 5% NFDM/TBST.
  • 1 - NTHL1 Antibody (Center R103) AP11554c
    NTHL1 Antibody (Center R103) (Cat. #AP11554c) western blot analysis in Hela,NCI-H460 cell line lysates (35ug/lane).This demonstrates the NTHL1 antibody detected the NTHL1 protein (arrow).
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, E
Primary Accession P78549
Other Accession NP_002519.1
Reactivity Human
Host Rabbit
Clonality Polyclonal
Isotype Rabbit IgG
Calculated MW 33570 Da
Antigen Region 88-117 aa
Additional Information
Gene ID 4913
Other Names Endonuclease III-like protein 1 {ECO:0000255|HAMAP-Rule:MF_03183}, hNTH1, 322- {ECO:0000255|HAMAP-Rule:MF_03183}, 429918 {ECO:0000255|HAMAP-Rule:MF_03183}, Bifunctional DNA N-glycoslyase/DNA-(apurinic or apyrimidinic site) lyase {ECO:0000255|HAMAP-Rule:MF_03183}, DNA glycoslyase/AP lyase {ECO:0000255|HAMAP-Rule:MF_03183}, NTHL1 {ECO:0000255|HAMAP-Rule:MF_03183}, NTH1, OCTS3
Target/Specificity This NTHL1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 88-117 amino acids from the Central region of human NTHL1.
Dilution WB~~1:1000
E~~Use at an assay dependent concentration.
Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.
StorageMaintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsNTHL1 Antibody (Center R103) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name NTHL1 {ECO:0000255|HAMAP-Rule:MF_03183}
Synonyms NTH1, OCTS3
Function Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage (PubMed:29610152, PubMed:9927729). The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta- elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines. Also has 8-oxo-7,8-dihydroguanine (8-oxoG) DNA glycosylase activity. Acts preferentially on DNA damage opposite guanine residues in DNA. Is able to process lesions in nucleosomes without requiring or inducing nucleosome disruption.
Cellular Location Nucleus {ECO:0000255|HAMAP-Rule:MF_03183, ECO:0000269|PubMed:10882850, ECO:0000269|PubMed:12531031, ECO:0000269|PubMed:9611236}. Mitochondrion {ECO:0000255|HAMAP- Rule:MF_03183, ECO:0000269|PubMed:9611236}
Tissue Location Widely expressed with highest levels in heart and lowest levels in lung and liver.
Research Areas

For Research Use Only. Not For Use In Diagnostic Procedures.

BACKGROUND

The protein encoded by this gene is a DNA N-glycosylase of the endonuclease III family. Like a similar protein in E. coli, the encoded protein has DNA glycosylase activity on DNA substrates containing oxidized pyrimidine residues and has apurinic/apyrimidinic lyase activity.

REFERENCES

Wang, W., et al. Nucleic Acids Res. (2010) In press :
Arora, M., et al. Leukemia 24(8):1470-1475(2010)
Thyagarajan, B., et al. Biol. Blood Marrow Transplant. 16(8):1084-1089(2010)
Briggs, F.B., et al. Am. J. Epidemiol. 172(2):217-224(2010)
Goto, M., et al. Carcinogenesis 30(8):1345-1352(2009)

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