Recombinant Human APE1 protein is a Human Full Length protein, in the 1 to 318 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, MS.
M A S M T G G Q Q M G R G S M P K R G K K G A V A E D G D E L R T E P E A K K S K T A A K K N D K E A A G E G P A L Y E D P P D Q K T S P S G K P A T L K I C S W N V D G L R A W I K K K G L D W V K E E A P D I L C L Q E T K C S E N K L P A E L Q E L P G L S H Q Y W S A P S D K E G Y S G V G L L S R Q C P L K V S Y G I G E E E H D Q E G R V I V A E F D S F V L V T A Y V P N A G R G L V R L E Y R Q R W D E A F R K F L K G L A S R K P L V L C G D L N V A H E E I D L R N P K G N K K N A G F T P Q E R Q G F G E L L Q A V P L A D S F R H L Y P N T P Y A Y T F W T Y M M N A R S K N V G W R L D Y F L L S H S L L P A L C D S K I R S K A L G S D H C P I T L Y L A L
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Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 are DNA repair and redox regulation of transcriptional factors. Functions as an 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. Also incises 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 3'-5' exoribonuclease activity on mismatched deoxyribonucleotides at the 3' termini of nicked or gapped DNA molecules during short-patch BER. Possesses 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 protection from granzyme-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.
APE, APE1, APEX, APX, HAP1, REF1, APEX1, DNA repair nuclease/redox regulator APEX1, APEX nuclease, Apurinic-apyrimidinic endonuclease 1, DNA-(apurinic or apyrimidinic site) endonuclease, Redox factor-1, APEN, AP endonuclease 1, APE-1, REF-1
Recombinant Human APE1 protein is a Human Full Length protein, in the 1 to 318 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, MS.
pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 1.16% Sodium chloride, 0.316% Tris HCl, 0.0308% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
ab103260 was purified using conventional chromatography techniques.
Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 are DNA repair and redox regulation of transcriptional factors. Functions as an 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. Also incises 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 3'-5' exoribonuclease activity on mismatched deoxyribonucleotides at the 3' termini of nicked or gapped DNA molecules during short-patch BER. Possesses 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 protection from granzyme-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.
Belongs to the DNA repair enzymes AP/ExoA family.
Phosphorylated. Phosphorylation by kinase PKC or casein kinase CK2 results in enhanced redox activity that stimulates binding of the FOS/JUN AP-1 complex to its cognate binding site. AP-endodeoxyribonuclease activity is not affected by CK2-mediated phosphorylation. Phosphorylation of Thr-233 by CDK5 reduces AP-endodeoxyribonuclease activity resulting in accumulation of DNA damage and contributing to neuronal death.
APE1 also known as APEX1 or apurinic/apyrimidinic endonuclease 1 functions as an important DNA repair enzyme. It plays a pivotal role in the base excision repair (BER) pathway where it recognizes and processes apurinic/apyrimidinic sites in DNA. APE1 has a molecular mass of about 37 kDa. It is expressed primarily in the nucleus with detectable levels in the cytoplasm. The expression of APE1 spans across various tissue types indicating its essential role in maintaining genomic stability.
APE1 enzymatically cleaves the phosphodiester bond at abasic sites creating a nick in the DNA backbone for further repair steps. This action prevents mutations and maintains DNA integrity. APE1 also functions as a redox factor regulating the transcriptional activity of several transcription factors. It is not part of a larger complex but interacts with various BER pathway proteins such as DNA polymerase beta and XRCC1. This interaction is important for the effective repair of damaged DNA and cellular response to oxidative stress.
APE1 is integrated within the base excision repair and redox signaling pathways. These pathways are fundamental for repairing single-strand breaks and modulating the cellular oxidative stress response. APE1 coordinates closely with other proteins like PNKP and OGG1 in the BER pathway ensuring precise and effective DNA repair. Through its redox activity APE1 influences pathways involving NF-kB and AP-1 demonstrating its multifaceted roles in cellular processes.
Alterations in APE1 function associate with cancer progression and neurodegenerative diseases. Overexpression or mutations in APE1 correlate with increased tumor resistance to chemotherapy in several cancers including lung and ovarian cancer. APE1's interaction with proteins like p53 and HMGB1 connects it to the etiology and progression of these malignancies. Furthermore impaired APE1 activity links to neurodegenerative disorders such as Alzheimer's disease where DNA repair deficiency contributes to neuronal damage and cognitive decline.
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15% SDS-PAGE analysis of 3μg ab103260.
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