Ku80 Antibody
Purified Rabbit Polyclonal Antibody (Pab)
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Application
| WB, IF, IHC |
|---|---|
| Primary Accession | P13010 |
| Reactivity | Human |
| Host | Rabbit |
| Clonality | polyclonal |
| Calculated MW | 82705 Da |
| Gene ID | 7520 |
|---|---|
| Other Names | X-ray repair cross-complementing protein 5, 364-, 86 kDa subunit of Ku antigen, ATP-dependent DNA helicase 2 subunit 2, ATP-dependent DNA helicase II 80 kDa subunit, CTC box-binding factor 85 kDa subunit, CTC85, CTCBF, DNA repair protein XRCC5, Ku80, Ku86, Lupus Ku autoantigen protein p86, Nuclear factor IV, Thyroid-lupus autoantigen, TLAA, X-ray repair complementing defective repair in Chinese hamster cells 5 (double-strand-break rejoining), XRCC5, G22P2 |
| Dilution | WB~~ 1:1000 IF~~1:100 IHC~~1:50-1:100 |
| Format | Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.09% (W/V) sodium azide and 50% glycerol. |
| Storage Conditions | -20℃ |
| Name | XRCC5 (HGNC:12833) |
|---|---|
| Synonyms | G22P2 |
| Function | DNA-binding protein critical for the DNA damage response, specifically in repairing double-strand breaks (DSBs) via the classical non-homologous end joining (NHEJ) pathway. It forms a heterodimer with XRCC6 (Ku70), creating the Ku70:Ku80 heterodimer (Ku complex), which serves as a DNA end-binding complex. It primarily binds DSBs and recruits essential repair factors, assembling the core long-range NHEJ complex to facilitate the alignment and ligation of broken DNA ends (PubMed:11493912, PubMed:33854234, PubMed:34352203). This pathway ensures the rapid repair of cytotoxic and mutagenic DSBs and contributes to the generation of diversity in T-cell receptors and antibodies through mechanisms such as V(D)J recombination (PubMed:9742108). Likely acts as a 5'-deoxyribose-5-phosphate lyase (5'-dRP lyase), catalyzing the beta-elimination of the 5'-deoxyribose- 5-phosphate at abasic sites near DSBs. This activity cleans the termini of abasic sites, a common form of nucleotide damage, preparing broken ends for ligation (PubMed:20383123). It may also possess 3'-5' DNA helicase activity, although this has not been confirmed in vivo, and its physiological significance remains unclear (PubMed:7957065). Beyond DNA repair, the protein contributes to telomere maintenance (PubMed:29490055). It is also implicated in transcriptional regulation, acting as a cofactor for various transcription factors (PubMed:12145306, PubMed:8621488). It plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP- RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (PubMed:28712728). Can also bind RNAs and recruits PRKDC to a wide range of cellular RNAs, including the U3 small nucleolar RNA, playing a role in the biogenesis of ribosomal RNAs (PubMed:32103174). |
| Cellular Location | Nucleus. Nucleus, nucleolus Chromosome |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
Single-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.
REFERENCES
Yaneva M.,et al.J. Biol. Chem. 264:13407-13411(1989).
Mimori T.,et al.Proc. Natl. Acad. Sci. U.S.A. 87:1777-1781(1990).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Suzuki Y.,et al.Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
Mural R.J.,et al.Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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