Ref-1 rabbit pAb - ES3337

Ref-1 rabbit pAb

Sizes: 50μL, 100μL

Catalogue Numbers: ES3337-50, ES3337-100

Citations, Manuals and MSDS Available upon request.

Background: 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],

Alternate Name: APEX1; APE; APE1; APEX; APX; HAP1; REF1; DNA- (apurinic or apyrimidinic site) lyase; APEX nuclease; APEN; Apurinic-apyrimidinic endonuclease 1; AP endonuclease 1; APE-1; REF-1; Redox factor-1

Source: Rabbit

Applications: WB; IHC; IF; ELISA

Dilution: Western Blot: 1/500 - 1/2000. IHC-p: 1:100-300 ELISA: 1/20000. Not yet tested in other applications.

Reactivity: Human; Mouse; Rat

Immunogen: The antiserum was produced against synthesized peptide derived from human APEX1. AA range:191-240

Storage and Stability: -20°C/1 year

Clonality: Polyclonal

Isotype: IgG

Concentration: 1 mg/ml

Observed Band (KD): 34kD

Human Gene ID: 328

Human SWISS Prot NO: P27695

Subcellular 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

Research Use Only