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| Item number | Size | Datasheet | Manual | SDS | Delivery time | Quantity | Price |
|---|---|---|---|---|---|---|---|
| ELK-ES18299.50 | 50 µl | - | - |
10 - 15 business days* |
173.00€
|
||
| ELK-ES18299.100 | 100 µl | - | - |
10 - 15 business days* |
290.00€
|
If you have any questions, please use our Contact Form.
You can also order by e-mail: info@biomol.com
Larger quantity required? Request bulk
You can also order by e-mail: info@biomol.com
Larger quantity required? Request bulk
Apurinic/apyrimidinic (AP) sites occur frequently in DNA molecules by spontaneous hydrolysis, by... more
Product information "Anti-APEX2"
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 a protein shown to have a weak class II AP endonuclease activity. Most of the encoded protein is located in the nucleus but some is also present in mitochondria. This protein may play an important role in both nuclear and mitochondrial base excision repair. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, Nov 2012], Protein 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. Required for proper cell cycle progression during proliferation of peripheral lymphocytes. [The UniProt Consortium] Recommended dilutions: WB 1:500-2000. Cellular localization: Nucleus. Cytoplasm. Mitochondrion . Together with PCNA, is redistributed in discrete nuclear foci in presence of oxidative DNA damaging agents.
| Keywords: | Anti-APE2, Anti-APEX2, Anti-APEX nuclease 2, Anti-AP endonuclease 2, Anti-AP endonuclease XTH2, Anti-APEX nuclease-like 2, Anti-Apurinic-apyrimidinic endonuclease 2, Anti-DNA-(apurinic or apyrimidinic site) endonuclease 2, APEX2 rabbit pAb |
| Supplier: | ELK Biotechnology |
| Supplier-Nr: | ES18299 |
Properties
| Application: | WB |
| Antibody Type: | Polyclonal |
| Conjugate: | No |
| Host: | Rabbit |
| Species reactivity: | human, mouse |
| Immunogen: | Synthesized peptide derived from human APEX2 AA range: 196-246 |
| Format: | Purified |
Database Information
| KEGG ID : | K10772 | Matching products |
| UniProt ID : | Q9UBZ4 | Matching products |
| Gene ID : | GeneID 27301 | Matching products |
Handling & Safety
| Storage: | -20°C |
| Shipping: | +4°C (International: +4°C) |
Caution
Our products are for laboratory research use only: Not for administration to humans!
Our products are for laboratory research use only: Not for administration to humans!
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