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Anti-APEX1 Antibody

品牌：Antibodies

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規(guī)格：50μl

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Anti-APEX1 Antibody

商品詳情參考文獻(xiàn) 相關(guān)資料

Overview

Name:	Anti-APEX1 Antibody See all APEX1 primary antibodies
Description:	Rabbit polyclonal antibody to APEX1.
Applications:	WB, IHC, IF
Dilutions:	WB: 1:500 - 1:2000, IHC: 1:50 - 1:200, IF: 1:50 - 1:200.
Reactivity:	Human, Mouse, Rat
Immunogen:	Recombinant protein of human APEX1.
Protein Length:	318
Host:	Rabbit
Clonality:	Polyclonal
Isotype:	IgG
Conjugate:	Unconjugated
Purification:	Affinity purification.
Product Form:	Liquid
Formulation:	Supplied in Phosphate Buffered Saline, pH 7.30, with 0.02% Sodium Azide and 50% Glycerol.
Storage:	Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.

Target

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 in 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.
Sequence Similarities:	Belongs to the DNA repair enzymes AP/ExoA family.
Post-Translational Modification:	Phosphorylated. Phosphorylation by kinase PKC or casein kinase CK2 results in enhanced redox activity that stimulates binding of the FOS/JUN AP-1 complex to its cognate . AP-endodeoxyribonuclease activity is not affected by CK2-mediated phosphorylation. Phosphorylation of Thr-233 by CDK5 reduces AP-endodeoxyribonuclease activity resulting in accumulation of DNA damage and contributing to neuronal death.
Cellular Location:	Nucleus. Nucleus > Nucleolus. Nucleus speckle. Endoplasmic reticulum. Cytoplasm. Detected in the cytoplasm of B-cells stimulated to switch (By similarity). Colocalized with SIRT1 in the nucleus. Colocalized with YBX1 in nuclear speckles after genotoxic stress. Together with OGG1 is recruited to nuclear speckles in UVA-irradiated cells. Colocalized with nucleolin and NPM1 in the nucleolus. Its nucleolar localization is cell cycle dependent and requires active rRNA transcription. Colocalized with calreticulin in the endoplasmic reticulum. Translocation from the nucleus to the cytoplasm is stimulated in presence of nitric oxide (NO) and function in a CRM1-dependent manner, possibly as a consequence of demasking a nuclear export signal (amino acid position 64-80). S-nitrosylation at Cys-93 and Cys-310 regulates its nuclear-cytosolic shuttling. Ubiquitinated form is localized predominantly in the cytoplasm.
Database Links:	Entrez Gene: 328?Human Entrez Gene: 11792?Mouse Entrez Gene: 79116?Rat Omim: 107748?Human SwissProt: P27695?Human SwissProt: P28352?Mouse SwissProt: P43138?Rat Unigene: 73722?Human Unigene: 203?Mouse Unigene: 239117?Mouse Unigene: 5949?Rat
Synonyms:	AP endonuclease 1 Antibody AP endonuclease class I Antibody AP lyase Antibody APE Antibody APE 1 Antibody APE-1 Antibody APE1 Antibody APEN Antibody APEX Antibody APEX 1 Antibody APEX nuclease Antibody APEX nuclease (multifunctional DNA repair enzyme) 1 Antibody Apex nuclease 1 Antibody APEX1 Antibody APEX1_HUMAN Antibody Apurinic endonuclease Antibody Apurinic-apyrimidinic endonuclease 1 Antibody Apurinic/apyrimidinic (abasic) endonuclease Antibody Apurinic/apyrimidinic endonuclease 1 Antibody Apurinic/apyrimidinic exonuclease Antibody APX Antibody BAP1 Antibody Deoxyribonuclease (apurinic or apyrimidinic) Antibody DNA (apurinic or apyrimidinic site) lyase Antibody DNA-(apurinic or apyrimidinic site) lyase, mitochondrial Antibody EC 4.2.99.18 Antibody HAP 1 Antibody HAP1 Antibody Human Apurinic endonuclease 1 Antibody MGC139790 Antibody Multifunctional DNA repair enzyme Antibody Redox factor 1 Antibody Redox factor-1 Antibody REF 1 Antibody REF 1 protein Antibody REF-1 Antibody REF1 Antibody REF1 protein Antibody
Information:	Target information shown above is from the UniProt Consortium.