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APE1 Antibody

Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - APE1 Antibody AP50982
    All lanes : Anti-APE1 Antibody at 1:1000 dilution Lane 1: Hela whole cell lysates Lane 2: A431 whole cell lysates Lysates/proteins at 20 µg per lane. Secondary Goat Anti-Rabbit IgG, (H+L),Peroxidase conjugated at 1/10000 dilution Predicted band size : 36 kDa Blocking/Dilution buffer: 5% NFDM/TBST.
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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
Primary Accession P27695
Reactivity Human, Mouse, Rat
Host Rabbit
Clonality Polyclonal
Calculated MW 37 KDa
Additional Information
Other Names DNA-(apurinic or apyrimidinic site) lyase, 31--, APEX nuclease, APEN, Apurinic-apyrimidinic endonuclease 1, AP endonuclease 1, APE-1, REF-1, Redox factor-1, DNA-(apurinic or apyrimidinic site) lyase, mitochondrial, APEX1, APE, APE1, APEX, APX, HAP1, REF1
Target/Specificity KLH-conjugated synthetic peptide encompassing a sequence within the center region of human APE1. The exact sequence is proprietary.
Dilution WB~~ 1:1000
Format 0.01M PBS, pH 7.2, 0.09% (W/V) Sodium azide, Glycerol 50%
StorageStore at -20 °C.Stable for 12 months from date of receipt
Protein Information
Research Areas

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

BACKGROUND

Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 in DNA repair and redox regulation of transcriptional factors. Functions as a apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Does also incise at AP sites in the DNA strand of DNA/RNA hybrids, single-stranded DNA regions of R-loop structures, and single-stranded RNA molecules. Has a 3'-5' exoribonuclease activity on mismatched deoxyribonucleotides at the 3' termini of nicked or gapped DNA molecules during short-patch BER. Possesses a DNA 3' phosphodiesterase activity capable of removing lesions (such as phosphoglycolate) blocking the 3' side of DNA strand breaks. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation. Acts as a loading factor for POLB onto non-incised AP sites in DNA and stimulates the 5'-terminal deoxyribose 5'- phosphate (dRp) excision activity of POLB. Plays a role in the protection from granzymes-mediated cellular repair leading to cell death. Also involved in the DNA cleavage step of class switch recombination (CSR). On the other hand, APEX1 also exerts reversible nuclear redox activity to regulate DNA binding affinity and transcriptional activity of transcriptional factors by controlling the redox status of their DNA-binding domain, such as the FOS/JUN AP-1 complex after exposure to IR. Involved in calcium-dependent down-regulation of parathyroid hormone (PTH) expression by binding to negative calcium response elements (nCaREs). Together with HNRNPL or the dimer XRCC5/XRCC6, associates with nCaRE, acting as an activator of transcriptional repression. Stimulates the YBX1-mediated MDR1 promoter activity, when acetylated at Lys-6 and Lys-7, leading to drug resistance. Acts also as an endoribonuclease involved in the control of single-stranded RNA metabolism. Plays a role in regulating MYC mRNA turnover by preferentially cleaving in between UA and CA dinucleotides of the MYC coding region determinant (CRD). In association with NMD1, plays a role in the rRNA quality control process during cell cycle progression. Associates, together with YBX1, on the MDR1 promoter. Together with NPM1, associates with rRNA. Binds DNA and RNA.

REFERENCES

Robson C.N.,et al.Nucleic Acids Res. 19:5519-5523(1991).
Demple B.,et al.Proc. Natl. Acad. Sci. U.S.A. 88:11450-11454(1991).
Seki S.,et al.Biochim. Biophys. Acta 1131:287-299(1992).
Xanthoudakis S.,et al.EMBO J. 11:3323-3335(1992).
Cheng X.B.,et al.Nucleic Acids Res. 20:370-370(1992).

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