Recombinant Human XLF protein
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Recombinant Human XLF protein is a Human Fragment protein, in the 1 to 224 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, Mass Spec.
View Alternative Names
XLF, NHEJ1, Non-homologous end-joining factor 1, Protein cernunnos, XRCC4-like factor
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human XLF protein (AB131670)
15% SDS-PAGE showing ab131670 at approximately 27.8 kDa (3μg).
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
XLF participates in the critical process of maintaining genomic stability. It is part of the NHEJ complex alongside XRCC4 and DNA ligase IV ensuring efficient repair of DNA breaks. This repair process is essential for preventing genomic instability and protecting cells from deleterious mutations. XLF helps tether DNA ends together providing structural support necessary for effective repair and its function is vital for cell survival especially in rapidly dividing cells.
Pathways
This protein integrates into the NHEJ pathway a primary mechanism for repairing DNA double-strand breaks. XLF collaborates directly with other proteins like Ku70/80 and DNA-PKcs facilitating their functions in the DNA damage response. Additionally it plays a role in the V(D)J recombination process which is vital for the development of immune system diversity by allowing the rearrangement of variable (V) diversity (D) and joining (J) gene segments.
Specifications
Form
Liquid
Additional notes
Purified using conventional chromatography techniques.
General info
Function
DNA repair protein involved in DNA non-homologous end joining (NHEJ); required for double-strand break (DSB) repair and V(D)J recombination (PubMed : 16439204, PubMed : 16439205, PubMed : 17317666, PubMed : 17470781, PubMed : 17717001, PubMed : 18158905, PubMed : 18644470, PubMed : 20558749, PubMed : 26100018). Plays a key role in NHEJ by promoting the ligation of various mismatched and non-cohesive ends (PubMed : 17470781, PubMed : 17717001, PubMed : 19056826). Together with PAXX, collaborates with DNA polymerase lambda (POLL) to promote joining of non-cohesive DNA ends (PubMed : 25670504, PubMed : 30250067). May act in concert with XRCC5-XRCC6 (Ku) to stimulate XRCC4-mediated joining of blunt ends and several types of mismatched ends that are non-complementary or partially complementary (PubMed : 16439204, PubMed : 16439205, PubMed : 17317666, PubMed : 17470781). In some studies, has been shown to associate with XRCC4 to form alternating helical filaments that bridge DNA and act like a bandage, holding together the broken DNA until it is repaired (PubMed : 21768349, PubMed : 21775435, PubMed : 22228831, PubMed : 22287571, PubMed : 26100018, PubMed : 27437582, PubMed : 28500754). Alternatively, it has also been shown that rather than forming filaments, a single NHEJ1 dimer interacts through both head domains with XRCC4 to promote the close alignment of DNA ends (By similarity). The XRCC4-NHEJ1/XLF subcomplex binds to the DNA fragments of a DSB in a highly diffusive manner and robustly bridges two independent DNA molecules, holding the broken DNA fragments in close proximity to one other (PubMed : 27437582, PubMed : 28500754). The mobility of the bridges ensures that the ends remain accessible for further processing by other repair factors (PubMed : 27437582). Binds DNA in a length-dependent manner (PubMed : 17317666, PubMed : 18158905).
Sequence similarities
Belongs to the XRCC4-XLF family. XLF subfamily.
Post-translational modifications
Phosphorylated by PRKDC at the C-terminus in response to DNA damage (PubMed:18644470, PubMed:22228831, PubMed:28500754). Phosphorylations by PRKDC at the C-terminus of XRCC4 and NHEJ1/XLF are highly redundant and regulate ability of the XRCC4-NHEJ1/XLF subcomplex to bridge DNA (PubMed:22228831, PubMed:28500754). Phosphorylation does not prevent interaction with XRCC4 but disrupts ability to bridge DNA and promotes detachment from DNA (PubMed:22228831, PubMed:28500754).
Subcellular localisation
Nucleus
Target data
Product promise
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