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APEX2 Antibody
Rabbit Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC-P |
|---|---|
| Primary Accession | Q9UBZ4 |
| Reactivity | Human, Rabbit, Monkey, Pig, Bovine, Dog |
| Host | Rabbit |
| Clonality | Polyclonal |
| Calculated MW | 57kDa |
| Dilution | IHC-P (10 µg/ml), WB (1:500-1:1000), |
| Gene ID | 27301 |
|---|---|
| Other Names | DNA-(apurinic or apyrimidinic site) lyase 2, 3.1.-.-, 4.2.99.18, AP endonuclease XTH2, APEX nuclease 2, APEX nuclease-like 2, Apurinic-apyrimidinic endonuclease 2, AP endonuclease 2, APEX2, APE2, APEXL2, XTH2 |
| Target/Specificity | Synthetic peptides of human APEXL2. |
| Reconstitution & Storage | Store at 4°C for short term applications. For long term storage, aliquot and store at -20°C. |
| Precautions | APEX2 Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | APEX2 |
|---|---|
| Synonyms | APE2, APEXL2, XTH2 |
| Function | Functions as a weak apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents (PubMed:16687656). 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. Also displays double-stranded DNA 3'-5' exonuclease, 3'-phosphodiesterase activities (PubMed:16687656, PubMed:19443450, PubMed:32516598). Shows robust 3'-5' exonuclease activity on 3'-recessed heteroduplex DNA and is able to remove mismatched nucleotides preferentially (PubMed:16687656, PubMed:19443450). Also exhibits 3'-5' exonuclease activity on a single nucleotide gap containing heteroduplex DNA and on blunt-ended substrates (PubMed:16687656). Shows fairly strong 3'-phosphodiesterase activity involved in the removal of 3'-damaged termini formed in DNA by oxidative agents (PubMed:16687656, PubMed:19443450). In the nucleus functions in the PCNA-dependent BER pathway (PubMed:11376153). Plays a role in reversing blocked 3' DNA ends, problematic lesions that preclude DNA synthesis (PubMed:32516598). Required for somatic hypermutation (SHM) and DNA cleavage step of class switch recombination (CSR) of immunoglobulin genes (By similarity). Required for proper cell cycle progression during proliferation of peripheral lymphocytes (By similarity). |
| Cellular Location | Nucleus {ECO:0000255|PROSITE-ProRule:PRU00764, ECO:0000269|PubMed:11376153, ECO:0000269|PubMed:19443450}. Cytoplasm Mitochondrion. Note=Together with PCNA, is redistributed in discrete nuclear foci in presence of oxidative DNA damaging agents. |
| Tissue Location | Highly expressed in brain and kidney. Weakly expressed in the fetal brain. |
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Provided below are standard protocols that you may find useful for product applications.
Background
Function as a weak 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. Displays also double-stranded DNA 3'-5' exonuclease, 3'-phosphodiesterase activities. Shows robust 3'-5' exonuclease activity on 3'-recessed heteroduplex DNA and is able to remove mismatched nucleotides preferentially. Shows fairly strong 3'-phosphodiesterase activity involved in the removal of 3'-damaged termini formed in DNA by oxidative agents. In the nucleus functions in the PCNA-dependent BER pathway. Required for somatic hypermutation (SHM) and DNA cleavage step of class switch recombination (CSR) of immunoglobulin genes. Required for proper cell cycle progression during proliferation of peripheral lymphocytes.
References
Tsuchimoto D.,et al.Nucleic Acids Res. 29:2349-2360(2001).
Luna L.,et al.Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
Akiyama K.,et al.Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
Hadi M.Z.,et al.Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
Ross M.T.,et al.Nature 434:325-337(2005).
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