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WRN Antibody (Center T802)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS: 1
- PROTOCOLS
- BACKGROUND
Application 
| FC, WB, IHC-P, E |
|---|---|
| Primary Accession | Q14191 |
| Other Accession | NP_000544.2 |
| Reactivity | Human |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 162461 Da |
| Antigen Region | 787-816 aa |
| Gene ID | 7486 |
|---|---|
| Other Names | Werner syndrome ATP-dependent helicase, DNA helicase, RecQ-like type 3, RecQ3, Exonuclease WRN, 31--, RecQ protein-like 2, WRN, RECQ3, RECQL2 |
| Target/Specificity | This WRN antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 787-816 amino acids from the Central region of human WRN. |
| Dilution | WB~~1:1000 IHC-P~~1:100 FC~~1:10~50 |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | WRN Antibody (Center T802) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | WRN |
|---|---|
| Synonyms | RECQ3, RECQL2 |
| Function | Multifunctional enzyme that has magnesium and ATP-dependent 3'-5' DNA-helicase activity on partially duplex substrates (PubMed:9611231, PubMed:9224595, PubMed:9288107). Also has 3'->5' exonuclease activity towards double-stranded DNA with a 5'-overhang (PubMed:11863428). Has no nuclease activity towards single-stranded DNA or blunt-ended double-stranded DNA (PubMed:11863428). Helicase activity is most efficient with (d)ATP, but (d)CTP will substitute with reduced efficiency; strand displacement is enhanced by single-strand binding- protein (heterotrimeric replication protein A complex, RPA1, RPA2, RPA3) (PubMed:9611231). Binds preferentially to DNA substrates containing alternate secondary structures, such as replication forks and Holliday junctions. May play an important role in the dissociation of joint DNA molecules that can arise as products of homologous recombination, at stalled replication forks or during DNA repair. Alleviates stalling of DNA polymerases at the site of DNA lesions. Important for genomic integrity. Plays a role in the formation of DNA replication focal centers; stably associates with foci elements generating binding sites for RP-A (By similarity). Plays a role in double-strand break repair after gamma-irradiation (PubMed:9288107, PubMed:9224595, PubMed:9611231). Depletion leads to chromosomal breaks and genome instability (PubMed:33199508). |
| Cellular Location | Nucleus, nucleolus. Nucleus. Nucleus, nucleoplasm. Chromosome. Note=Gamma-irradiation leads to its translocation from nucleoli to nucleoplasm and PML regulates the irradiation-induced WRN relocation (PubMed:21639834). Localizes to DNA damage sites (PubMed:27063109). |
Provided below are standard protocols that you may find useful for product applications.
Background
This gene encodes a member of the RecQ subfamily and the DEAH (Asp-Glu-Ala-His) subfamily of DNA and RNA helicases. DNA helicases are involved in many aspects of DNA metabolism, including transcription, replication, recombination, and repair. This protein contains a nuclear localization signal in the C-terminus and shows a predominant nucleolar localization. It possesses an intrinsic 3' to 5' DNA helicase activity, and is also a 3' to 5' exonuclease. Based on interactions between this protein and Ku70/80 heterodimer in DNA end processing, this protein may be involved in the repair of double strand DNA breaks. Defects in this gene are the cause of Werner syndrome, an autosomal recessive disorder characterized by premature aging.
References
Bailey, S.D., et al. Diabetes Care 33(10):2250-2253(2010)
Perry, J.J., et al. J. Biol. Chem. 285(33):25699-25707(2010)
Briggs, F.B., et al. Am. J. Epidemiol. 172(2):217-224(2010)
Kobayashi, J., et al. Mech. Ageing Dev. 131(6):436-444(2010)
Ehrenberg, M., et al. Mol. Vis. 16, 1771-1775 (2010) :
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