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anti-APEX1 antibody :: Rabbit APEX1 Polyclonal Antibody

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Catalog # MBS9606912
Unit / Price
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  0.1 mL  /  $255 +1 FREE 8GB USB
  0.2 mL  /  $295 +1 FREE 8GB USB
Product Name

APEX1, Polyclonal Antibody

Popular Item
Full Product Name

APEX1 Antibody

Product Synonym Names
AP endonuclease 1; AP endonuclease class I; AP lyase; APE 1; APE; APE-1; APEN; APEX 1; APEX; APEX nuclease (multifunctional DNA repair enzyme) 1; Apex nuclease 1; APEX nuclease; APEX1; APEX1_HUMAN; Apurinic endonuclease; Apurinic-apyrimidinic endonuclease 1; Apurinic/apyrimidinic (abasic) endonuclease; Apurinic/apyrimidinic endonuclease 1; Apurinic/apyrimidinic exonuclease; APX; BAP1; Deoxyribonuclease (apurinic or apyrimidinic); DNA (apurinic or apyrimidinic site) lyase; DNA-(apurinic or apyrimidinic site) lyase, mitochondrial; EC 4.2.99.18; HAP 1; HAP1; Human Apurinic endonuclease 1; MGC139790; Multifunctional DNA repair enzyme; Redox factor 1; Redox factor-1; REF 1; REF 1 protein; REF-1; REF1; REF1 protein
Research Use Only
For Research Use Only. Not for use in diagnostic procedures.
3D Structure
ModBase 3D Structure for P27695
Clonality
Polyclonal
Isotype
IgG
Host
Rabbit
Species Reactivity
Human, Mouse, Rat
Specificity
APEX1 antibody detects endogenous levels of total APEX1
Purity/Purification
The antiserum was purified by peptide affinity chromatography using SulfoLink Coupling Resin.
Form/Format
Liquid
Phosphate buffered saline, pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
Concentration
1mg/ml (lot specific)
Immunogen
A synthesized peptide derived from human APEX1
Subcellular Location
Mitochondrion. The cleaved APEX2 is only detected in mitochondria (By similarity). 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 and 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.
Tissue Specificity
Up-regulated in presence of reactive oxygen species (ROS), like bleomycin, H2O2 and phenazine methosulfate.
Predicted Cross Reactivity
Pig, Bovine, Horse, Sheep, Rabbit, Dog
Similarity
Pig (91%), Bovine (91%), Horse (100%), Sheep (91%), Rabbit (91%), Dog (82%)
Conjugation
Unconjugated
Preparation and Storage
Store at -20 degree C. Stable for 12 months from date of receipt.
ISO Certification
Manufactured in an ISO 9001:2015 Certified Laboratory.
Supply Chain Verification
Manufactured in a lab with traceable raw materials manufactured on site. Coordinated product portfolio of antibodies, pairs, conjugates, recombinant proteins, and immunoassay materials available, please inquire.
Other Notes
Small volumes of anti-APEX1 antibody vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.
Related Product Information for
anti-APEX1 antibody
Description: Ape1 (Apurinic/ApyrimidiceEndonuclease 1), also known as Ref1 (Redox effector factor 1), is a multifunctional protein with several biological activities. These include roles in DNA repair and in the cellular response to oxidative stress. Ape1 initiates the repair of abasic sites and is essential for the base excision repair (BER) pathway (1). Repair activities of Ape1 are stimulated by interaction with XRCC1 (2), another essential protein in BER. Ape1 functions as a redox factor that maintains transcription factors in an active, reduced state but can also function in a redox-independent manner as a transcriptional cofactor to control different cellular fates such as apoptosis, proliferation and differentiation (3). Increased expression of Ape1 is associated with many types of cancers including cervical, ovarian, prostate, rhabdomyosarcomas and germ cell tumors (4). Ape1 has been shown to stimulate DNA binding of several transcription factors known to be involved in tumor progression such as Fos, Jun, NF-kappaB, PAX, HIF-1, HLF and p53 (4). Mutation of the Ape1 gene has also been associated with amyotrophic lateral sclerosis (ALS) (5, 6).
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.
Subunit Structure: Monomer. Homodimer; disulfide-linked. Component of the SET complex, composed of at least APEX1, SET, ANP32A, HMGB2, NME1 and TREX1. 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. Binds to CDK5.
Post-translational Modifications: 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 binding site. 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. Acetylated on Lys-6 and Lys-7. Acetylation is increased by the transcriptional coactivator EP300 acetyltransferase, genotoxic agents like H2O2 and methyl methanesulfonate (MMS). Acetylation increases its binding affinity to the negative calcium response element (nCaRE) DNA promoter. The acetylated form induces a stronger binding of YBX1 to the Y-box sequence in the MDR1 promoter than the unacetylated form. Deacetylated on lysines. Lys-6 and Lys-7 are deacetylated by SIRT1. Cleaved at Lys-31 by granzyme A to create the mitochondrial form; leading in reduction of binding to DNA, AP endodeoxynuclease activity, redox activation of transcription factors and to enhanced cell death. Cleaved by granzyme K; leading to intracellular ROS accumulation and enhanced cell death after oxidative stress. Cys-65 and Cys-93 are nitrosylated in response to nitric oxide (NO) and lead to the exposure of the nuclear export signal (NES). Ubiquitinated by MDM2; leading to translocation to the cytoplasm and proteasomal degradation.
Similarity: The N-terminus contains the redox activity while the C-terminus exerts the DNA AP-endodeoxyribonuclease activity; both function are independent in their actions. An unconventional mitochondrial targeting sequence (MTS) is harbored within the C-terminus, that appears to be masked by the N-terminal sequence containing the nuclear localization signal (NLS), that probably blocks the interaction between the MTS and Tom proteins. Belongs to the DNA repair enzymes AP/ExoA family.
Applications Tested/Suitable for anti-APEX1 antibody
Western Blot (WB), Immunohistochemisty (IHC), Immunofluorescence (IF), Immunocytochemistry (ICC), ELISA (EIA)
Application Notes for anti-APEX1 antibody
WB: 1:500-1:2000
IHC: 1:50-1:200
IF: 1:100-400
Peptide ELISA: 1:20000-1:40000

Western Blot (WB) of anti-APEX1 antibody
Western blot analysis of extracts of Hela, using APEX1 antibody. The lane on the left is treated with the antigen-specific peptide.
anti-APEX1 antibody Western Blot (WB) (WB) image
Immunofluorescene (IF) of anti-APEX1 antibody
MBS9606912 staining HEPG2 cells by ICC/IF. Cells were fixed with PFA and permeabilized in 0.1% saponin prior to blocking in 10% serum for 45 minutes at 37 degree C. The primary antibody was diluted 1/200 and incubated with the sample for 1 hour at 37 degree C. A Alexa Fluor 594 conjugated goat polyclonal to rabbit IgG (H+L), diluted 1/600 was used as secondary antibody.
anti-APEX1 antibody Immunofluorescene (IF) image
Immunofluorescence (IF) of anti-APEX1 antibody
MBS9606912 staining COLO205 cells by IF/ICC. The sample were fixed with PFA and permeabilized in 0.1% Triton X-100, then blocked in 10% serum for 45 minutes at 25 degree C. The primary antibody was diluted at 1/200 and incubated with the sample for 1 hour at 37 degree C. An Alexa Fluor 594 conjugated goat anti-rabbit IgG (H+L) antibody, diluted at 1/600, was used as secondary antibody.
anti-APEX1 antibody Immunofluorescence (IF) image
Immunohistochemistry (IHC) of anti-APEX1 antibody
MBS9606912 at 1/100 staining Mouse spleen tissue by IHC-P. The sample was formaldehyde fixed and a heat mediated antigen retrieval step in citrate buffer was performed. The sample was then blocked and incubated with the antibody for 1.5 hours at 22 degree C. An HRP conjugated goat anti-rabbit antibody was used as the secondary.
anti-APEX1 antibody Immunohistochemistry (IHC) (IHC) image
NCBI/Uniprot data below describe general gene information for APEX1. It may not necessarily be applicable to this product.
NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Primary Accession #
UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
Observed: 36 kDa
Predicted: 36 kDa
NCBI Official Full Name
DNA-(apurinic or apyrimidinic site) lyase
NCBI Official Synonym Full Names
apurinic/apyrimidinic endodeoxyribonuclease 1
NCBI Official Symbol
APEX1  [Similar Products]
NCBI Official Synonym Symbols
APE; APX; APE1; APEN; APEX; HAP1; REF1
  [Similar Products]
NCBI Protein Information
DNA-(apurinic or apyrimidinic site) lyase
UniProt Protein Name
DNA-(apurinic or apyrimidinic site) lyase
UniProt Synonym Protein Names
APEX nuclease; APEN
UniProt Gene Name
APEX1  [Similar Products]
UniProt Synonym Gene Names
APE; APE1; APEX; APX; HAP1; REF1; APEN; AP endonuclease 1; APE-1  [Similar Products]
NCBI Summary for APEX1
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 Comments for APEX1
Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 are 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.
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