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ELISA Kit for Bovine DNA-(apurinic or apyrimidinic site) lyase

SKU : BHE13801345

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EIAAB SCIENCE INC, WUHAN

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Mfr.No.	E1939b
Alternative Names	APEX nuclease ; APEN ; Apurinic-apyrimidinic endonuclease 1 ; AP endonuclease 1 ; REF-1 ; Redox factor-1 ; APE ; APEX ; BAP1 ; REF1
Categories	Elisa
Function	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 to 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.
Specificity	Natural and recombinant Bovine DNA-(apurinic or apyrimidinic site) lyase
Subcellular Location	DNA-(apurinic or apyrimidinic site) lyase, mitochondrial Mitochondrion Translocation from the cytoplasm to the mitochondria is mediated by ROS signaling and cleavage mediated by granzyme A. Tom20-dependent translocated mitochondrial APEX1 level is significantly increased after genotoxic stress (By similarity). The cleaved APEX2 is only detected in mitochondria.
Entryname	APEX1_BOVIN
Platform	PF03372
Protein Name	DNA-(apurinic or apyrimidinic site) lyase
Sequence	50: MPKRGKKGAV ; VEDAEEPKTE ; PEAKKSKAGA ; KKNEKEAVGE ; GAVLYEDPPD ; 100: QKTSPSGKSA ; TLKICSWNVD ; GLRAWIKKKG ; LDWVKEEAPD ; ILCLQETKCS ; 150: ENKLPVELQE ; LSGLSHQYWS ; APSDKEGYSG ; VGLLSRQCPL ; KVSYGIGEEE ; 200: HDQEGRVIVA ; EYDAFVLVTA ; YVPNAGRGLV ; RLEYRQRWDE ; AFRKFLKGLA ; 250: SRKPLVLCGD ; LNVAHEEIDL ; RNPKGNKKNA ; GFTPQERQGF ; GELLQAVPLT ; 300: DSFRHLYPNT ; AYAYTFWTYM ; MNARSKNVGW ; RLDYFLLSQS ; VLPALCDSKI ; 318: RSKALGSDHC ; PITLYLAL
Sequence Length	318
String	P23196
Sub Unit	Monomer. Homodimer; disulfide-linked. Component of the SET complex, composed at least of APEX1, GZMA, SET, ANP32A, HMGB2 and NME1. Associates with the dimer XRCC5/XRCC6 in a DNA-dependent manner. 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. Interacts with XRCC1; the interaction is induced by SIRT1 and increased with the APEX1 acetylated form. Interacts with NPM1 (via N-terminal domain); the interaction is RNA-dependent and decreases in hydrogen peroxide-damaged cells. Interacts (via N-terminus) with YBX1 (via C-terminus); the interaction is increased in presence of APEX1 acetylated at Lys-6 and Lys-7. Interacts with HNRNPL; the interaction is DNA-dependent. Interacts (via N-terminus) with KPNA1 and KPNA2. Interacts with TXN; the interaction stimulates the FOS/JUN AP-1 complex DNA-binding activity in a redox-dependent manner. Interacts with GZMA, KRT8, MDM2, POLB, PRDX6, PRPF19, RPLP0, TOMM20 and WDR77 (By similarity). Binds to CDK5.

Uniprot	P23196
Gene Name	APEX1
Immunogen Species	Bos Taurus (Cattle)
Kegg	bta:281630
Unigene	Bt.1302

Reference	1. "Isolation of cDNA clones encoding an enzyme from bovine cells that repairs oxidative DNA damage in vitro: homology with bacterial repair enzymes." Robson C.N., Milne A.M., Pappin D.J.C., Hickson I.D. Nucleic Acids Res.19:1087-1092(1991) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA];PROTEIN SEQUENCE OF 2-19 tissue: Thymus. 2. NIH - Mammalian Gene Collection (MGC) project Submitted (2006-08) to the EMBL/GenBank/DDBJ databases [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] strain: Hereford. tissue: Basal ganglia. 3. "Purification and amino-terminal amino acid sequence of an apurinic/apyrimidinic endonuclease from calf thymus." Henner W.D., Kiker N.P., Jorgensen T.J., Munck J.-N. Nucleic Acids Res.15:5529-5544(1987) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PROTEIN SEQUENCE OF 2-23 tissue: Thymus. 4. "Identification and characterization of mitochondrial abasic (AP)-endonuclease in mammalian cells." Chattopadhyay R., Wiederhold L., Szczesny B., Boldogh I., Hazra T.K., Izumi T., Mitra S. Nucleic Acids Res.34:2067-2076(2006) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PROTEIN SEQUENCE OF 34-38;FUNCTION;SUBCELLULAR LOCATION;TISSUE SPECIFICITY tissue: Liver. 5. "Three-dimensional structure prediction of bovine AP lyase, BAP1: prediction of interaction with DNA and alterations as a result of Arg176->Ala, Asp282->Ala, and His308->Asn mutations." Khurshid R., Salim A., Abbasi A. Biochem. Biophys. Res. Commun.326:711-717(2005) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: 3D-STRUCTURE MODELING OF 40-318

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