Rabbit anti-Human APEX1 / APE1 Polyclonal Antibody | anti-APEX1 antibody

Rabbit Polyclonal (IgG) to Human APEX1 / APE1

Cat. Num. AAA247844

• Gene Names: APEX1; APE; APX; APE1; APEN; APEX; HAP1; REF1
• Reactivity: Human
• Applications: Immunohistochemistry, Western Blot
• Synonyms: APEX1 / APE1; Polyclonal Antibody; Rabbit Polyclonal (IgG) to Human APEX1 / APE1; Anti-APEX1 / APE1 Antibody IHC-plus; APEX1; AP endonuclease class I; AP lyase; APE; APE-1; APEN; APE1; APEX nuclease; Redox factor-1; AP endonuclease 1; APEX; APX; Protein REF-1; REF-1; REF1; Human APEX1; anti-APEX1 antibody

• Host: Rabbit
• Reactivity: Human
• Clonality: Polyclonal
• Isotype: IgG
• Specificity: Full length human APE1 purified from E Coli.
• Form/Format: Antiserum, no preservative
• Sequence Length: 318

• Applicable Applications for anti-APEX1 antibody: Immunohistochemistry (IHC - Paraffin), Western Blot (WB)
• Application Notes: IHC-P (1:100), WB
• Target Species: Human
• Preparation and Storage: Store at -20 degree C or lower. Aliquot to avoid repeated freezing and thawing.

Immunohistochemistry (IHC)

(Anti-APEX1 / APE1 antibody IHC of human skin. Immunohistochemistry of formalin-fixed, paraffin-embedded tissue after heat-induced antigen retrieval. Antibody dilution 1:100.)

Immunohistochemistry (IHC)

(Anti-APEX1 / APE1 antibody IHC of human tonsil. Immunohistochemistry of formalin-fixed, paraffin-embedded tissue after heat-induced antigen retrieval. Antibody dilution 1:100.)

Related Product Information for anti-APEX1 antibody

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.

NCBI and Uniprot Product Information

• NCBI GI #: 18375501
• NCBI GeneID: 328
• NCBI Accession #: NP_001632.2
• NCBI GenBank Nucleotide #: NM_001641.3
• 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 (apurinic or apyrimidinic)
• 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 repair, damage; Nuclear receptor co-regulator; DNA-binding; Lyase; Nucleolus; Hydrolase; EC 4.2.99.18; Deoxyribonuclease; Transcription, coactivator/corepressor; Endoplasmic reticulum

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; uracil DNA N-glycosylase activity; phosphoric diester hydrolase activity; chromatin DNA binding; metal ion binding; transcription coactivator activity; oxidoreductase activity; endodeoxyribonuclease activity; NF-kappaB binding; protein binding; DNA binding; endonuclease activity; damaged DNA binding; protein complex 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; DNA strand elongation during DNA replication; negative regulation of smooth muscle cell migration; 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