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

SKU : BHE13800980

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EIAAB SCIENCE INC, WUHAN

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Mfr.No.	E1939r
Alternative Names	APEX nuclease ; APEN ; Apurinic-apyrimidinic endonuclease 1 ; AP endonuclease 1 ; REF-1 ; Redox factor-1 ; Ape ; Apex ; 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, 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 Rat DNA-(apurinic or apyrimidinic site) lyase
Subcellular Location	DNA-(apurinic or apyrimidinic site) lyase, mitochondrial Mitochondrion The cleaved APEX2 is only detected in mitochondria. 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.
Detection Range	0.156-10ng/ml
Entryname	APEX1_RAT
Method Type	Sandwich
Platform	PF03372
Protein Name	DNA-(apurinic or apyrimidinic site) lyase
Sensitivity	0.081ng/mL
Sequence	50: MPKRGKRAAA ; EDGEEPKSEP ; ETKKSKGAAK ; KTEKEAAGEG ; PVLYEDPPDQ ; 100: KTSASGKSAT ; LKICSWNVDG ; LRAWIKKKGL ; DWVKEEAPDI ; LCLQETKCSE ; 150: NKLPAELQEL ; PGLTHQYWSA ; PSDKEGYSGV ; GLLSRQCPLK ; VSYGIGEEEH ; 200: DQEGRVIVAE ; FESFILVTAY ; VPNAGRGLVR ; LEYRQRWDEA ; FRKFLKDLAS ; 250: RKPLVLCGDL ; NVAHEEIDLR ; NPKGNKKNAG ; FTPQERQGFG ; EMLQAVPLAD ; 300: SFRHLYPNTA ; YAYTFWTYMM ; NARSKNVGWR ; LDYFLLSHSL ; LPALCDSKIR ; 317: SKALGSDHCP ; ITLYLAL
Sequence Length	317
String	P43138
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. 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	P43138
Gene Name	Apex1
Immunogen Species	Rattus norvegicus (Rat)
Kegg	rno:79116
Unigene	Rn.5949

Reference	1. "Cloning of the multifunctional rat apurinic/apyrimidinic endonuclease (rAPEN)/redox factor from an immature T cell line." Wilson T.M., Carney J.P., Kelley M.R. Nucleic Acids Res.22:530-531(1994) [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] strain: Sprague-Dawley. tissue: Testis. 2. "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)." Yao M., Akiyama K., Tan Y., Sarker A.H., Ikeda S., Alam S.S., Tsutsui K., Yoshida M.C., Seki S. Acta Med. Okayama53:245-252(1999) [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 [GENOMIC DNA] 3. "cDNA and deduced amino acid sequence of rat APEX nuclease." Tan Y., Akiyama K., Seki S., Tabayashi T., Taniyama M. Submitted (1994-12) 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 [MRNA] strain: Sprague-Dawley. tissue: Brain. 4. "Cloning of APEX cDNA gene from PC12 cell line." Xie Z.H., Liu C.Z., Wang A.M., Ma C. Submitted (2000-09) 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 [MRNA] tissue: Pheochromocytoma. 5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res.14:2121-2127(2004) [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 [LARGE SCALE MRNA] tissue: Kidney. 6. "Mitochondrial localization of APE/Ref-1 in thyroid cells." Tell G., Crivellato E., Pines A., Paron I., Pucillo C., Manzini G., Bandiera A., Kelley M.R., Di Loreto C., Damante G. Mutat. Res.485:143-152(2001) [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: SUBCELLULAR LOCATION 7. "Identification of apurinic/apyrimidinic endonuclease 1 (APE1) as the endoribonuclease that cleaves c-myc mRNA." Barnes T., Kim W.C., Mantha A.K., Kim S.E., Izumi T., Mitra S., Lee C.H. Nucleic Acids Res.37:3946-3958(2009) [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: FUNCTION;IDENTIFICATION BY MASS SPECTROMETRY

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