APE1/APEX1 Recombinant Protein | APEX1 recombinant protein

APE1/APEX1 Protein, Human, Recombinant (His Tag)

Cat. Num. AAA8121156

• Gene Names: APEX1; APE; APX; APE1; APEN; APEX; HAP1; REF1
• Purity: >92% as determined by SDS-PAGE
• Synonyms: APE1/APEX1; APE1/APEX1 Protein; Human; Recombinant (His Tag); Human APEX1/AP/APEx/Ref-1 Protein (His Tag); APE Protein; APE1 Protein; APEN Protein; APEX Protein; APX Protein; HAP1 Protein; REF1 Protein; APEX nuclease (multifunctional DNA repair enzyme) 1; APEX1 recombinant protein

• Host: E Coli
• Purity/Purification: >92% as determined by SDS-PAGE
• Form/Format: Lyophilized from sterile PBS, pH7.5. Normally 5%-8% trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA.
• Sequence: Pro2-Leu318

• Species: Human
• Endotoxin: <1.0EU per ug of the protein as determined by the LAL method
• Predicted N Terminal: Met
• Tag: N-His
• Protein Construction: A DNA sequence encoding the human APEX1 (P27695)(Pro2-Leu 318) was expressed, with a polyhistidine tag at the N-terminus.
• Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
• Preparation and Storage: Samples are stable for up to twelve months from date of receipt at -20 degree C to -80 degree C. Store it under sterile conditions at -20 degree C to -80 degree C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.; In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid.; They are shipped out with blue ice.

SDS-Page

Related Product Information for APEX1 recombinant protein

Background: The enzyme is known to be a redox factor (Ref-1) stimulating DNA binding activity of AP-1 binding proteins such as Fos and Jun as well as a multifunctional DNA repair enzyme having 5' AP endonuclease, DNA 3' repair diesterase, 3'-5' exonuclease and DNA 3'-phosphatase activities.Although Apex mRNA was expressed ubiquitously, the levels varied significantly, suggesting organ- or tissue-specific expression of the Apex gene. The highest level was observed in the testis, relatively high levels in the thymus, spleen, kidney and brain, and the lowest level in the liver in rats. However, the present results suggested that APEX/Ref-1 gene product can interact with AP-1 binding proteins in brain, especially in the hippocampal formation, to regulate some brain functions by redox-activation.

References

Ono Y, et al. (1995) Developmental expression of APEX nuclease, a multifunctional DNA repair enzyme, in mouse brains. Brain Res Dev Brain Res.86 (1-2): 1-6.Tan Y, et al. (1996) cDNA cloning of rat major AP endonuclease (APEX nuclease) and analyses of its mRNA expression in rat tissues. Acta Med Okayama. 50 (1): 53-60.Yao M, et al. (1999) Genomic structure of the rat major AP endonuclease gene (Apex) with an adjacent putative O-sialoglycoprotease gene (Prsmg1/Gcpl1) and a processed Apex pseudogene (Apexp1). Acta Med Okayama. 53 (6): 245-52.

NCBI and Uniprot Product Information

• NCBI GI #: 346644849
• NCBI GeneID: 328
• NCBI Accession #: NP_001231178.1
• NCBI GenBank Nucleotide #: NM_001244249.1
• UniProt Accession #: P27695; Q969L5; Q99775
• Molecular Weight: 35,555 Da
• NCBI Official Full Name: DNA-(apurinic or apyrimidinic site) lyase
• NCBI Official Synonym Full Names: APEX nuclease (multifunctional DNA repair enzyme) 1
• NCBI Official Symbol: APEX1
• NCBI Official Synonym Symbols: APE; APX; APE1; APEN; APEX; HAP1; REF1
• NCBI Protein Information: DNA-(apurinic or apyrimidinic site) lyase; DNA-(apurinic or apyrimidinic site) lyase; AP lyase; protein REF-1; redox factor-1; AP endonuclease class I; apurinic-apyrimidinic endonuclease 1; apurinic/apyrimidinic (abasic) endonuclease; deoxyribonuclease (a
• UniProt Protein Name: DNA-(apurinic or apyrimidinic site) lyase
• Protein Family: DNA-(apurinic or apyrimidinic site) lyase
• UniProt Gene Name: APEX1
• UniProt Synonym Gene Names: APE; APE1; APEX; APX; HAP1; REF1; APEN; AP endonuclease 1; APE-1
• UniProt Entry Name: APEX1_HUMAN

NCBI Description

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]

Uniprot Description

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: DNA-binding; EC 4.2.99.18; Nuclear receptor co-regulator; Deoxyribonuclease; Nucleolus; DNA repair, damage; Hydrolase; Endoplasmic reticulum; Lyase; Transcription, coactivator/corepressor

Chromosomal Location of Human Ortholog: 14q11.2

Cellular Component: nucleoplasm; centrosome; transcription factor complex; mitochondrion; endoplasmic reticulum; perinuclear region of cytoplasm; cytoplasm; nucleolus; ribosome; nuclear speck; nucleus

Molecular Function: phosphodiesterase I activity; DNA-(apurinic or apyrimidinic site) lyase activity; phosphoric diester hydrolase activity; uracil DNA N-glycosylase activity; chromatin DNA binding; metal ion binding; transcription coactivator activity; oxidoreductase activity; endodeoxyribonuclease activity; NF-kappaB binding; protein binding; DNA binding; endonuclease activity; protein complex binding; damaged DNA binding; ribonuclease H activity; 3'-5' exonuclease activity; transcription corepressor activity; double-stranded DNA specific 3'-5' exodeoxyribonuclease activity; site-specific endodeoxyribonuclease activity, specific for altered base

Biological Process: response to drug; positive regulation of DNA repair; mismatch repair; transcription, DNA-dependent; negative regulation of smooth muscle cell migration; DNA strand elongation during DNA replication; DNA repair; regulation of mRNA stability; DNA catabolic process, endonucleolytic; double-strand break repair via homologous recombination; telomere maintenance via semi-conservative replication; regulation of transcription, DNA-dependent; cell redox homeostasis; nucleotide-excision repair; base-excision repair; transcription-coupled nucleotide-excision repair; double-strand break repair; telomere maintenance via recombination; nucleotide-excision repair, DNA gap filling; mitotic cell cycle; DNA catabolic process, exonucleolytic; telomere maintenance; aging