Recombinant Human Cell cycle checkpoint protein RAD17(RAD17)

Code CSB-YP019253HU
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Source Yeast
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Code CSB-EP019253HU
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Source E.coli
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Code CSB-EP019253HU-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP019253HU
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Source Baculovirus
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Code CSB-MP019253HU
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Source Mammalian cell
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Product Details

Purity >85% (SDS-PAGE)
Target Names RAD17
Uniprot No. O75943
Alternative Names CCYC; Cell cycle checkpoint protein; Cell cycle checkpoint protein RAD17; FLJ41520; HRAD 17; hRad17; R24L; Rad 17; Rad 24; RAD1 (S. pombe) homolog; RAD1 homolog; RAD17; RAD17 homolog (S. pombe); RAD17 homolog; Rad17 like protein; RAD17; S. pombe; homolog of; RAD17_HUMAN; RAD17Sp; Rad24; Rad24; mouse; homolog of; Rad24; S. cerevisiae; homolog of; RF C activator 1 homolog; RF C/activator 1 homolog; RF-C/activator 1 homolog
Species Homo sapiens (Human)
Expression Region 1-681
Target Protein Sequence MSKTFLRPKV SSTKVTDWVD PSFDDFLECS GVSTITATSL GVNNSSHRRK NGPSTLESSR FPARKRGNLS SLEQIYGLEN SKEYLSENEP WVDKYKPETQ HELAVHKKKI EEVETWLKAQ VLERQPKQGG SILLITGPPG CGKTTTLKIL SKEHGIQVQE WINPVLPDFQ KDDFKGMFNT ESSFHMFPYQ SQIAVFKEFL LRATKYNKLQ MLGDDLRTDK KIILVEDLPN QFYRDSHTLH EVLRKYVRIG RCPLIFIISD SLSGDNNQRL LFPKEIQEEC SISNISFNPV APTIMMKFLN RIVTIEANKN GGKITVPDKT SLELLCQGCS GDIRSAINSL QFSSSKGENN LRPRKKGMSL KSDAVLSKSK RRKKPDRVFE NQEVQAIGGK DVSLFLFRAL GKILYCKRAS LTELDSPRLP SHLSEYERDT LLVEPEEVVE MSHMPGDLFN LYLHQNYIDF FMEIDDIVRA SEFLSFADIL SGDWNTRSLL REYSTSIATR GVMHSNKARG YAHCQGGGSS FRPLHKPQWF LINKKYRENC LAAKALFPDF CLPALCLQTQ LLPYLALLTI PMRNQAQISF IQDIGRLPLK RHFGRLKMEA LTDREHGMID PDSGDEAQLN GGHSAEESLG EPTQATVPET WSLPLSQNSA SELPASQPQP FSAQGDMEEN IIIEDYESDG T
Protein Length Full length protein
Tag Info The following tags are available.
N-terminal His-tagged
Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form Lyophilized powder
Buffer before Lyophilization Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting
and FAQs
Protein FAQs
Storage Condition Store at -20°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet Please contact us to get it.

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Target Background

Function
(From Uniprot)
Essential for sustained cell growth, maintenance of chromosomal stability, and ATR-dependent checkpoint activation upon DNA damage. Has a weak ATPase activity required for binding to chromatin. Participates in the recruitment of the RAD1-RAD9-HUS1 complex and RHNO1 onto chromatin, and in CHEK1 activation. May also serve as a sensor of DNA replication progression, and may be involved in homologous recombination.
Gene References into Functions
  1. DDX11 orchestrates jointly with 9-1-1 and its loader, RAD17, DNA damage tolerance at sites of bulky lesions, and endogenous abasic sites. These functions may explain the essential roles of DDX11 and its similarity with 9-1-1 during development. PMID: 30061412
  2. The Rad17 C-terminal tail is a molecular switch that regulates the 9-1-1 interaction and the ATR pathway. PMID: 28666868
  3. These data indicate that the interaction with the 9-1-1 complex is not required for Rad17 protein to be an efficient substrate for the UV-induced phosphorylation. Our data also raise the possibility that the 9-1-1 complex plays a negative regulatory role in the Rad17 phosphorylation. We also show that the nucleotide-binding activity of Rad17 is required for its nuclear localization. PMID: 27387238
  4. In a Japanese population, the variant allele of hRAD17 is significantly associated with a decreased risk of Colorectal Cancer among light smokers and rectal cancer patients and with an increased risk of Colorectal Cancer among heavy smokers. PMID: 28238011
  5. Authors show that BRCA1 and RAD17 genes, whose derived proteins play a pivotal role in DNA damage repair, are transcriptional targets of gain-of-function mutant p53 proteins. PMID: 25650659
  6. USP20 and Rad17 interact, and that this interaction is enhanced by UV exposure. We show that USP20 regulation of Rad17 is at the protein level in a proteasome-dependent manner. USP20 depletion results in poor activation of Chk1 protein by phosphorylation PMID: 24923443
  7. Rad17 is phosphorylated by ATM at Thr622 resulting in a direct interaction of Rad17 with NBS1, facilitating recruitment of MRE11, RAD50 and ATM to the DNA double-strand breaks. PMID: 24534091
  8. Our data suggest RAD17 as a novel target protein for gemcitabine combination therapy supplementing or complementing inhibition of CHK1. PMID: 23687379
  9. Knockdown of Rad17 with two independent siRNAs significantly reduced Chk1 phosphorylation and substantial RPA32 Ser33 phosphorylation. PMID: 23684611
  10. Data indicate that regulation of Rad17 turnover is through the Cdh1/anaphase-promoting complex pathway in breast cancer cells. PMID: 23637229
  11. Proteolysis of Rad17 by Cdh1/APC regulates checkpoint termination and recovery from genotoxic stress PMID: 20424596
  12. The four alternatively spliced forms differentially expressed in different tissues, in different phases of the cell cycle, and differentially responded to X-irradiation. PMID: 11602352
  13. upon replication block a Rad17/RF-C complex is recruited to sites of DNA lesions in late S phase, binds the Rad9/Hus1/Rad1 complex and enables it to interact with PCNA. An interaction of Rad17/RF-C with PCNA is mediated by the small RF-C p37 subunit PMID: 12400013
  14. Rad17 localizes to DNA replication sites and interacts with DNA polymerase epsilon. PMID: 14500819
  15. replication protein A (RPA) stimulates the binding of the Rad17-Rfc2-5 complex to single-stranded DNA PMID: 14605214
  16. we show a requirement for Rad17 and Hus1 to induce G(2) arrest as well as Vpr-induced phosphorylation of histone 2A variant X (H2AX) and formation of nuclear foci containing H2AX and breast cancer susceptibility protein 1 PMID: 15485898
  17. interacts with newly identified hMCM7 protein, a core component of the DNA replication apparatus PMID: 15538388
  18. Findings reveal a phosphorylation-dependent function of Rad17 in an ATR-Rad17-Claspin-Chk1-signaling cascade that responds to specific replication stress. PMID: 16885023
  19. Using siRNA to knock down Rad17 demonstrates that it is not essntial for the DNA replication checkpoint in Hela cells. PMID: 16951182
  20. Loss of hRAD17 expression occurs frequently in HNSCC, is often due to genomic deletion, and may facilitate genomic instability in HNSCC PMID: 17657792
  21. hRAD17 delayed growth of NIH3T3 fibroblasts transformed by the H-ras oncogene in nude mice. PMID: 18378394

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Subcellular Location Nucleus
Protein Families Rad17/RAD24 family
Tissue Specificity Overexpressed in various cancer cell lines and in colon carcinoma (at protein level). Isoform 2 and isoform 3 are the most abundant isoforms in non irradiated cells (at protein level). Ubiquitous at low levels. Highly expressed in testis, where it is expr
Database Links

HGNC: 9807

OMIM: 603139

KEGG: hsa:5884

STRING: 9606.ENSP00000370151

UniGene: Hs.16184

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