Phospho-Ku70 (Ser520) Antibody - #AF4405
製品: | Phospho-Ku70 (Ser520) Antibody |
カタログ: | AF4405 |
タンパク質の説明: | Rabbit polyclonal antibody to Phospho-Ku70 (Ser520) |
アプリケーション: | WB IF/ICC |
反応性: | Human, Mouse, Rat |
予測: | Pig, Horse, Rabbit, Dog |
分子量: | 70kDa; 70kD(Calculated). |
ユニプロット: | P12956 |
RRID: | AB_2844470 |
製品説明
*The optimal dilutions should be determined by the end user.
*Tips:
WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.
引用形式: Affinity Biosciences Cat# AF4405, RRID:AB_2844470.
折りたたみ/展開
5''-deoxyribose-5-phosphate lyase Ku70; 5''-dRP lyase Ku70; 70 kDa subunit of Ku antigen; ATP dependent DNA helicase 2 subunit 1; ATP dependent DNA helicase II 70 kDa subunit; ATP-dependent DNA helicase 2 subunit 1; ATP-dependent DNA helicase II 70 kDa subunit; CTC box binding factor 75 kDa subunit; CTC box-binding factor 75 kDa subunit; CTC75; CTCBF; DNA repair protein XRCC6; G22P1; Ku 70; Ku autoantigen p70 subunit; Ku autoantigen, 70kDa; Ku p70; Ku70; Ku70 DNA binding component of DNA-dependent proteinkinase complex (thyroid autoantigen 70 kDa; Kup70; Lupus Ku autoantigen protein p70; ML8; Thyroid autoantigen 70kD (Ku antigen); Thyroid autoantigen; Thyroid lupus autoantigen; Thyroid lupus autoantigen p70; Thyroid-lupus autoantigen; TLAA; X ray repair complementing defective repair in Chinese hamster cells 6; X-ray repair complementing defective repair in Chinese hamster cells 6; X-ray repair cross-complementing protein 6; XRCC 6; Xrcc6; XRCC6_HUMAN;
免疫原
- P12956 XRCC6_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MSGWESYYKTEGDEEAEEEQEENLEASGDYKYSGRDSLIFLVDASKAMFESQSEDELTPFDMSIQCIQSVYISKIISSDRDLLAVVFYGTEKDKNSVNFKNIYVLQELDNPGAKRILELDQFKGQQGQKRFQDMMGHGSDYSLSEVLWVCANLFSDVQFKMSHKRIMLFTNEDNPHGNDSAKASRARTKAGDLRDTGIFLDLMHLKKPGGFDISLFYRDIISIAEDEDLRVHFEESSKLEDLLRKVRAKETRKRALSRLKLKLNKDIVISVGIYNLVQKALKPPPIKLYRETNEPVKTKTRTFNTSTGGLLLPSDTKRSQIYGSRQIILEKEETEELKRFDDPGLMLMGFKPLVLLKKHHYLRPSLFVYPEESLVIGSSTLFSALLIKCLEKEVAALCRYTPRRNIPPYFVALVPQEEELDDQKIQVTPPGFQLVFLPFADDKRKMPFTEKIMATPEQVGKMKAIVEKLRFTYRSDSFENPVLQQHFRNLEALALDLMEPEQAVDLTLPKVEAMNKRLGSLVDEFKELVYPPDYNPEGKVTKRKHDNEGSGSKRPKVEYSEEELKTHISKGTLGKFTVPMLKEACRAYGLKSGLKKQELLEALTKHFQD
種類予測
Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.
High(score>80) Medium(80>score>50) Low(score<50) No confidence
PTMs - P12956 基板として
Site | PTM Type | Enzyme | Source |
---|---|---|---|
S2 | Acetylation | Uniprot | |
S2 | Phosphorylation | Uniprot | |
S6 | Phosphorylation | P78527 (PRKDC) | Uniprot |
Y7 | Phosphorylation | Uniprot | |
Y8 | Phosphorylation | Uniprot | |
K9 | Sumoylation | Uniprot | |
S27 | Phosphorylation | P78527 (PRKDC) , Q13315 (ATM) | Uniprot |
Y30 | Phosphorylation | Uniprot | |
K31 | Acetylation | Uniprot | |
K31 | Sumoylation | Uniprot | |
K31 | Ubiquitination | Uniprot | |
S33 | Phosphorylation | Q13315 (ATM) , P78527 (PRKDC) | Uniprot |
S37 | Phosphorylation | Uniprot | |
S45 | Phosphorylation | Uniprot | |
S51 | Phosphorylation | P78527 (PRKDC) | Uniprot |
S53 | Phosphorylation | Uniprot | |
K92 | Acetylation | Uniprot | |
K92 | Methylation | Uniprot | |
K92 | Ubiquitination | Uniprot | |
K94 | Ubiquitination | Uniprot | |
K100 | Acetylation | Uniprot | |
K100 | Ubiquitination | Uniprot | |
Y103 | Phosphorylation | Uniprot | |
K114 | Acetylation | Uniprot | |
K114 | Methylation | Uniprot | |
K114 | Ubiquitination | Uniprot | |
K123 | Methylation | Uniprot | |
K123 | Sumoylation | Uniprot | |
K123 | Ubiquitination | Uniprot | |
K129 | Ubiquitination | Uniprot | |
S155 | Phosphorylation | Uniprot | |
S180 | Phosphorylation | Uniprot | |
K182 | Ubiquitination | Uniprot | |
K189 | Ubiquitination | Uniprot | |
R194 | Methylation | Uniprot | |
K206 | Ubiquitination | Uniprot | |
K207 | Methylation | Uniprot | |
K207 | Ubiquitination | Uniprot | |
S222 | Phosphorylation | Uniprot | |
R230 | Methylation | Uniprot | |
S237 | Phosphorylation | Uniprot | |
K238 | Ubiquitination | Uniprot | |
R244 | Methylation | Uniprot | |
K265 | Ubiquitination | Uniprot | |
K282 | Acetylation | Uniprot | |
K282 | Ubiquitination | Uniprot | |
K287 | Acetylation | Uniprot | |
K287 | Ubiquitination | Uniprot | |
T292 | Phosphorylation | Uniprot | |
K297 | Sumoylation | Uniprot | |
K297 | Ubiquitination | Uniprot | |
K299 | Ubiquitination | Uniprot | |
R301 | Methylation | Uniprot | |
T302 | Phosphorylation | Uniprot | |
S306 | Phosphorylation | Uniprot | |
S314 | Phosphorylation | Uniprot | |
K317 | Acetylation | Uniprot | |
K317 | Sumoylation | Uniprot | |
K317 | Ubiquitination | Uniprot | |
R318 | Methylation | Uniprot | |
S324 | Phosphorylation | Uniprot | |
K331 | Acetylation | Uniprot | |
K331 | Sumoylation | Uniprot | |
K331 | Ubiquitination | Uniprot | |
K338 | Acetylation | Uniprot | |
K338 | Ubiquitination | Uniprot | |
K351 | Ubiquitination | Uniprot | |
K357 | Ubiquitination | Uniprot | |
K358 | Ubiquitination | Uniprot | |
K392 | Acetylation | Uniprot | |
K392 | Ubiquitination | Uniprot | |
K424 | Sumoylation | Uniprot | |
T428 | Phosphorylation | Uniprot | |
K443 | Sumoylation | Uniprot | |
K443 | Ubiquitination | Uniprot | |
K445 | Ubiquitination | Uniprot | |
K451 | Ubiquitination | Uniprot | |
T455 | Phosphorylation | P24941 (CDK2) | Uniprot |
K461 | Acetylation | Uniprot | |
K461 | Ubiquitination | Uniprot | |
K463 | Ubiquitination | Uniprot | |
K468 | Acetylation | Uniprot | |
K468 | Ubiquitination | Uniprot | |
R474 | Methylation | Uniprot | |
S475 | Phosphorylation | Uniprot | |
S477 | Phosphorylation | O14757 (CHEK1) | Uniprot |
K510 | Sumoylation | Uniprot | |
K516 | Ubiquitination | Uniprot | |
S520 | Phosphorylation | Uniprot | |
K526 | Sumoylation | Uniprot | |
K526 | Ubiquitination | Uniprot | |
Y530 | Phosphorylation | P12931 (SRC) | Uniprot |
Y534 | Phosphorylation | Uniprot | |
K539 | Acetylation | Uniprot | |
K539 | Ubiquitination | Uniprot | |
T541 | Phosphorylation | Uniprot | |
K542 | Acetylation | Uniprot | |
K544 | Acetylation | Uniprot | |
S550 | Phosphorylation | Uniprot | |
K553 | Acetylation | Uniprot | |
K553 | Ubiquitination | Uniprot | |
K556 | Acetylation | Uniprot | |
K556 | Sumoylation | Uniprot | |
K556 | Ubiquitination | Uniprot | |
S560 | Phosphorylation | Uniprot | |
K565 | Ubiquitination | Uniprot | |
K570 | Acetylation | Uniprot | |
K570 | Ubiquitination | Uniprot | |
K575 | Acetylation | Uniprot | |
K575 | Ubiquitination | Uniprot | |
T577 | Phosphorylation | Uniprot | |
K582 | Ubiquitination | Uniprot | |
Y588 | Phosphorylation | Uniprot | |
K591 | Ubiquitination | Uniprot | |
S592 | Phosphorylation | Uniprot | |
K595 | Ubiquitination | Uniprot | |
K596 | Ubiquitination | Uniprot | |
T604 | Phosphorylation | Uniprot | |
K605 | Acetylation | Uniprot | |
K605 | Ubiquitination | Uniprot |
研究背景
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. Required for osteocalcin gene expression. 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. 5'-dRP lyase activity 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. 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.
Phosphorylation by PRKDC may enhance helicase activity. Phosphorylation of Ser-51 does not affect DNA repair.
ADP-ribosylated by PARP3.
Nucleus. Chromosome.
Heterodimer composed of XRCC5/Ku80 and XRCC6/Ku70. The dimer associates in a DNA-dependent manner with PRKDC to form the DNA-dependent protein kinase complex DNA-PK, and with the LIG4-XRCC4 complex to form the core of the non-homologous end joining (NHEJ) complex. Additional components of the NHEJ complex include NHEJ1/XLF and PAXX. The dimer also associates with NAA15, and this complex binds to the osteocalcin promoter and activates osteocalcin expression. In addition, XRCC6 interacts with the osteoblast-specific transcription factors MSX2, RUNX2 and DLX5. Interacts with ELF3. Interacts with ATP23. The XRCC5/6 dimer associates in a DNA-dependent manner with APEX1. Binds to CDK9 isoform 2. Identified in a complex with DEAF1 and XRCC5. Interacts with DEAF1 (via the SAND domain); the interaction is direct and may be inhibited by DNA-binding. Interacts with CLU (By similarity). Interacts with NR4A3; the DNA-dependent protein kinase complex DNA-PK phosphorylates and activates NR4A3 and prevents NR4A3 ubiquitinylation and degradation. Interacts with CYREN isoform 1 (CYREN-1) and isoform 4 (CYREN-2). Interacts (via N-terminus) with HSF1 (via N-terminus); this interaction is direct and prevents XRCC5/XRCC6 heterodimeric binding and non-homologous end joining (NHEJ) repair activities induced by ionizing radiation (IR). Part of the HDP-RNP complex composed of at least HEXIM1, PRKDC, XRCC5, XRCC6, paraspeckle proteins (SFPQ, NONO, PSPC1, RBM14, and MATR3) and NEAT1 RNA. Interacts with HMBOX1.
(Microbial infection) Interacts with human T-cell leukemia virus 1/HTLV-1 protein HBZ.
Belongs to the ku70 family.
研究領域
· Genetic Information Processing > Replication and repair > Non-homologous end-joining.
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