Key features and details
- PE Rabbit monoclonal [EPR3468] to Ku80
- Suitable for: Flow Cyt
- Reacts with: Human
- Conjugation: PE. Ex: 488nm, Em: 575nm
Product namePE Anti-Ku80 antibody [EPR3468]
See all Ku80 primary antibodies
DescriptionPE Rabbit monoclonal [EPR3468] to Ku80
ConjugationPE. Ex: 488nm, Em: 575nm
Tested applicationsSuitable for: Flow Cytmore details
Species reactivityReacts with: Human
Synthetic peptide within Human Ku80 aa 700-800. The exact sequence is proprietary.
Database link: P13010
- Flow Cyt: HeLa cells
This product is a recombinant monoclonal antibody, which offers several advantages including:
- - High batch-to-batch consistency and reproducibility
- - Improved sensitivity and specificity
- - Long-term security of supply
- - Animal-free production
Storage instructionsShipped at 4°C. Upon delivery aliquot. Store at +4°C. Do Not Freeze. Store In the Dark.
Storage bufferpH: 7.40
Preservative: 0.02% Sodium azide
Constituents: 1% BSA, PBS
Concentration information loading...
PurityProtein A purified
Our Abpromise guarantee covers the use of ab225046 in the following tested applications.
The cellular localisation of this product has been verified in ICC/IF.
FunctionSingle stranded DNA-dependent ATP-dependent helicase. Has a role in chromosome translocation. The DNA helicase II complex binds preferentially to fork-like ends of double-stranded DNA in a cell cycle-dependent manner. It works in the 3'-5' direction. Binding to DNA may be mediated by XRCC6. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The XRCC5/6 dimer acts as regulatory subunit of the DNA-dependent protein kinase complex DNA-PK by increasing the affinity of the catalytic subunit PRKDC to DNA by 100-fold. The XRCC5/6 dimer is probably involved in stabilizing broken DNA ends and bringing them together. The assembly of the DNA-PK complex to DNA ends is required for the NHEJ ligation step. In association with NAA15, the XRCC5/6 dimer binds to the osteocalcin promoter and activates osteocalcin expression. The XRCC5/6 dimer probably also acts as a 5'-deoxyribose-5-phosphate lyase (5'-dRP lyase), by catalyzing the beta-elimination of the 5' deoxyribose-5-phosphate at an abasic site near double-strand breaks. XRCC5 probably acts as the catalytic subunit of 5'-dRP activity, and allows to 'clean' the termini of abasic sites, a class of nucleotide damage commonly associated with strand breaks, before such broken ends can be joined. The XRCC5/6 dimer together with APEX1 acts as a negative regulator of transcription.
Sequence similaritiesBelongs to the ku80 family.
Contains 1 Ku domain.
Developmental stageExpression increases during promyelocyte differentiation.
DomainThe EEXXXDDL motif is required for the interaction with catalytic subunit PRKDC and its recruitment to sites of DNA damage.
modificationsPhosphorylated on serine residues. Phosphorylation by PRKDC may enhance helicase activity.
Cellular localizationNucleus. Chromosome.
- Information by UniProt
- 86 kDa subunit of Ku antigen antibody
- ATP dependent DNA helicase 2 subunit 2 antibody
- ATP dependent DNA helicase II 80 kDa subunit antibody
Overlay histogram showing HeLa cells stained with ab225046 (red line). The cells were fixed with 4% formaldehyde (10 min) and then permeabilized with 0.1% PBS-Triton X-100 for 15 min. The cells were then incubated in 1x PBS / 10% normal goat serum to block non-specific protein-protein interactions followed by the antibody (ab225046, 1/5000 dilution) for 30 min at 22°C.
Isotype control antibody (black line) was Rabbit IgG (monoclonal) Phycoerythrin (ab209478) used at the same concentration and conditions as the primary antibody. Unlabelled sample (blue line) was also used as a control.
Acquisition of >5,000 events were collected using a 50 mW Yellow/Green laser (561nm) and 586/15 bandpass filter.
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
ab225046 has not yet been referenced specifically in any publications.