protein

Recombinant Human DNA-(apurinic or apyrimidinic site) lyase

MBS717553

0.05 mg (E-Coli)

190 USD

Recombinant Protein

Recombinant Human DNA-(apurinic or apyrimidinic site) lyase

DNA-(apurinic or apyrimidinic site) lyase

APEX nuclease; APEN; Apurinic-apyrimidinic endonuclease 1; AP endonuclease 1; APE-1; REF-1; Redox factor-1

DNA-(apurinic or apyrimidinic site) lyase; DNA-(apurinic or apyrimidinic site) lyase; DNA-(apurinic or apyrimidinic site) lyase; APEX nuclease (multifunctional DNA repair enzyme) 1; APEX nuclease; APEN

APEX1

APEX1; APEX1; APE; APX; APE1; APEN; APEX; HAP1; REF1; APE; APE1; APEX; APX; HAP1; REF1; APEN; AP endonuclease 1; APE-1

APEX1_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

32-318

318

KNDKEAAGEGPALYEDPPDQKTSPSGKPATLKICSWNVD
GLRAWIKKKGLDWVKEEAPDILCLQETKCSENKLPAELQ
ELPGLSHQYWSAPSDKEGYSGVGLLSRQCPLKVSYGIGD
EEHDQEGRVIVAEFDSFVLVTAYVPNAGRGLVRLEYRQR
WDEAFRKFLKGLASRKPLVLCGDLNVAHEEIDLRNPKGN
KKNAGFTPQERQGFGELLQAVPLADSFRHLYPNTPYAYT
FWTYMMNARSKNVGWRLDYFL

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Epigenetics and Nuclear Signaling

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 roving 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 dethylation. 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

Isolation of cDNA clones encoding a human apurinic/apyrimidinic endonuclease that corrects DNA repair and mutagenesis defects in E. coli xth (exonuclease III)

346644849

NP_001231178.1

NM_001244249.1

P27695

36.3kD

Abasic Sugar-phosphate Removal Via The Single-nucleotide Replacement Pathway (1270362); BER Complex Pathway (413429); BER Complex Pathway (468377); Base Excision Repair Pathway (1270351); Base Excision Repair Pathway (83043); Base Excision Repair Pathway (451); Cell Cycle Pathway (1269741); Cell Cycle, Mitotic Pathway (1269763); Chromosome Maintenance Pathway (1269853); DNA Repair Pathway (1270350)

Apurinic/apyrimidinic (AP) sites occur frequently in DNA molecules by spontaneous hydrolysis, by DNA damaging agents or by DNA glycosylases that remove specific abnormal bases. AP sites are pre-mutagenic lesions that can prevent normal DNA replication so the cell contains systems to identify and repair such sites. Class II AP endonucleases cleave the phosphodiester backbone 5' to the AP site. This gene encodes the major AP endonuclease in human cells. Splice variants have been found for this gene; all encode the same protein. [provided by RefSeq, Jul 2008]

APE1: a multifunctional enzyme that plays a central role in the cellular response to oxidative stress including DNA repair and redox regulation of transcriptional factors. Binds DNA and RNA. Functions as an apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway, a 3'-5' exoribonuclease for mismatched deoxyribonucleotides at the 3' termini of nicked or gapped DNA molecules, and a DNA 3' phosphodiesterase capable of removing lesions (such as phosphoglycolate) blocking the 3' side of DNA strand breaks. Is a loading factor for POLB onto non-incised AP sites in DNA, stimulates the 5'-terminal deoxyribose 5'- phosphate (dRp) excision activity of POLB, and involved in the DNA cleavage step of class switch recombination (CSR). Possesses 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. Binds to negative calcium response elements (nCaREs). Stimulates the YBX1-mediated MDR1 promoter activity, when acetylated at Lys-6 and Lys-7, leading to drug resistance. Is an endoribonuclease involved in the control of single-stranded RNA metabolism. Plays a role in regulating MYC mRNA turnover. In association with NMD1, plays a role in the rRNA quality control process during cell cycle progression. Interacts with SIRT1; the interaction is increased in the context of genotoxic stress. Interacts with HDAC1, HDAC2 and HDAC3; the interactions are not dependent on the APEX1 acetylation status. Up-regulated in presence of reactive oxygen species (ROS), like bleomycin, H2O2 and phenazine methosulfate. NPM1 stimulates endodeoxyribonuclease activity on double-stranded DNA with AP sites, but inhibits endoribonuclease activity on single-stranded RNA containing AP sites. Belongs to the DNA repair enzymes AP/ExoA family. Protein type: Endoplasmic reticulum; EC 4.2.99.18; DNA repair, damage; Lyase; Transcription, coactivator/corepressor; Nucleolus; Deoxyribonuclease; Nuclear receptor co-regulator; Hydrolase; DNA-binding. Chromosomal Location of Human Ortholog: 14q11.2. Cellular Component: centrosome; cytoplasm; endoplasmic reticulum; mitochondrion; nuclear chromosome, telomeric region; nuclear speck; nucleolus; nucleoplasm; nucleus; perinuclear region of cytoplasm; ribosome; transcription factor complex. Molecular Function: 3'-5' exonuclease activity; chromatin DNA binding; damaged DNA binding; DNA binding; DNA-(apurinic or apyrimidinic site) lyase activity; double-stranded DNA specific 3'-5' exodeoxyribonuclease activity; double-stranded DNA specific exodeoxyribonuclease activity; double-stranded telomeric DNA binding; endodeoxyribonuclease activity; endonuclease activity; metal ion binding; NF-kappaB binding; oxidoreductase activity; phosphodiesterase I activity; phosphoric diester hydrolase activity; protein binding; protein complex binding; ribonuclease H activity; site-specific endodeoxyribonuclease activity, specific for altered base; transcription coactivator activity; transcription corepressor activity; uracil DNA N-glycosylase activity. Biological Process: aging; base-excision repair; cell redox homeostasis; DNA repair; DNA strand elongation during DNA replication; mitotic cell cycle; negative regulation of smooth muscle cell migration; positive regulation of DNA repair; regulation of mRNA stability; regulation of transcription, DNA-dependent; response to drug; telomere maintenance; telomere maintenance via recombination; telomere maintenance via semi-conservative replication; transcription, DNA-dependent

0.05 mg (E-Coli)

190 USD

0.05 mg (Yeast)

190

0.2 mg (E-Coli)

460

0.2 mg (Yeast)

460

0.5 mg (Yeast)

750