APEX1 Polyclonal AntibodyE-AB-33591
Product Type: Antibody
Descritpion: The role of transcription factors in the regulation of gene expression is well established. Although the activity of these factors can be regulated by phosphorylation,evidence has indicated regulation of DNA binding mediated by changes in reduction-oxidation (redox) status. Mutational analysis has identified a single conserved cysteine residue mapping within the DNA binding domains of Fos and Jun. Chemical oxidation or modification of this cysteine residue inhibits the DNA binding activity of Fos and Jun. A similar mode of regulation has been recently proposed for other nuclear transcription factors. Oxidation is reversible by these compounds or by a cellular redox/DNA repair protein identified originally as Ref-1 (redox factor 1). Ref-1 is identical to a previously characterized DNA repair enzyme designated HAP1, APE or APEX.
Research Areas: Cancer, Cardiovascular, Epigenetics and Nuclear Signaling
Recommended Dilutions: WB 1:500-1:2000, ELISA 1:20000
Size: 200 uL
Immunogen: Synthesized peptide derived from human Ref-1 around the non-acetylation site of K6.
Formulation: PBS with 0.02% sodium azide,0.5% BSA and 50% glycerol pH 7.4.
Purification: Affinity purification
Calculated MW: 36kDa
Tissue Specificity/Positive Control:
Cellular Localization: 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.
Storage: Store at -20C. Avoid freeze / thaw cycles.
Product Link: https://www.elabscience.com/p-apex1_polyclonal_antibody-29916.html
Manual Link: https://www.elabscience.com/viewpdf-29916-elabscience-E-AB-33591.PDF