HEL308 Antibody (Center) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | Q8TDG4 |
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Gene ID | 113510 |
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Other Names | Helicase POLQ-like, Mus308-like helicase, POLQ-like helicase, HELQ, HEL308 |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
Name | HELQ {ECO:0000303|PubMed:24005041, ECO:0000312|HGNC:HGNC:18536} |
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Function | Single-stranded 3'-5' DNA helicase that plays a key role in homology-driven double-strand break (DSB) repair (PubMed:11751861, PubMed:19995904, PubMed:21398521, PubMed:24005041, PubMed:24005565, PubMed:34316696, PubMed:34937945). Involved in different DSB repair mechanisms that are guided by annealing of extensive stretches of complementary bases at break ends, such as microhomology-mediated end- joining (MMEJ), single-strand annealing (SSA) or synthesis-dependent strand annealing (SDSA) (PubMed:34937945). Possesses both DNA unwinding and annealing activities (PubMed:34937945). Forms a complex with RAD51, stimulating HELQ DNA helicase activity and ability to unwing DNA (PubMed:34937945). Efficiently unwinds substrates containing 3' overhangs or a D-loop (PubMed:21398521, PubMed:34937945). In contrast, interaction with the replication protein A (RPA/RP-A) complex inhibits DNA unwinding by HELQ but strongly stimulates DNA strand annealing (PubMed:34937945). Triggers displacement of RPA from single-stranded DNA to facilitate annealing of complementary sequences (PubMed:34316696, PubMed:34937945). |
Cellular Location | Nucleus. Chromosome Note=Localizes to sites of DNA damage; localizes to damaged replication forks. |
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Provided below are standard protocols that you may find useful for product applications.
Background
HEL308 is a single-stranded DNA-dependent ATPase and DNA helicase.
References
Bethke, L., et al. J. Natl. Cancer Inst. 100(4):270-276(2008)Marini, F., et al. J. Biol. Chem. 278(34):32014-32019(2003)
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