Recombinant Human Checkpoint protein HUS1(HUS1),partial

Code CSB-EP010909HU
Size US$1726Purchase it in Cusabio online store
(only available for customers from the US)
  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Product Details

Purity Greater than 90% as determined by SDS-PAGE.
Target Names HUS1
Uniprot No. O60921
Research Area Epigenetics and Nuclear Signaling
Alternative Names Checkpoint protein HUS1; hHUS1; HUS1 (S. pombe) checkpoint homolog; Hus1; HUS1 checkpoint homolog (S. pombe); HUS1 Checkpoint Protein; HUS1 protein; HUS1+ - like protein; HUS1_HUMAN; Hydroxyurea-sensitive 1, S. pombe, homolog of
Species Homo sapiens (Human)
Source E.coli
Expression Region 2-280aa
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight 47.6kDa
Protein Length Partial
Tag Info N-terminal 6xHis-SUMO-tagged
Form Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is 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°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
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.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA Please contact us to get it.

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Target Background

(From Uniprot)
Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates. The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase.
Gene References into Functions
  1. These results suggest that p21(Waf1/CIP1) and Hus1 play crucial roles in the generation and transmission of bystander damage signals after low-dose alpha-particle irradiation. PMID: 26600172
  2. adenine glycosylase activity, mismatch recognition properties and interaction with protein partners of MUTYH and 5 MAP variants were examined; P502L and R520Q had reduced affinity for PCNA; only Q324H was found to have reduced affinity for Hus1 PMID: 26377631
  3. Intramolecular binding of the rad9 C-terminus in the checkpoint clamp Rad9-Hus1-Rad1 is closely linked with its DNA binding. PMID: 26088138
  4. these pockets were not required for 9-1-1 chromatin localization or ATR-mediated CHK1 activation but were necessary for interactions between HUS1 and its binding partner MYH PMID: 25911100
  5. Expression of cell cycle regulatory factors hus1, gadd45a, rb1, cdkn2a and mre11a correlates with expression of clock gene per2 in human colorectal carcinoma tissue. PMID: 24062075
  6. HUS1 polymorphisms act as risk breast cancer modifiers in the group of non-carriers of BRCA1/2 mutations. PMID: 22926736
  7. Data show models for the ternary PCNA/FEN1/DNA and Rad9-Rad1-Hus1 (9-1-1 complex)/FEN1/DNA assemblies. PMID: 22586102
  8. The HUS1 is loaded to damaged sites where it serves as a platform for the selective recruitment of checkpoint and repair proteins. PMID: 21978893
  9. The HUS1 protein interacts with casein kinase 2. PMID: 20545769
  10. 9-1-1 complex is a component of the mismatch repair involved in MNNG-induced damage response. PMID: 20188637
  11. Rad9-Rad1-Hus1 complex enhances in vitro activity of 8-oxoguanine DNA glycosylase. PMID: 19615952
  12. downregulation by specific antisense oligonucleotides sensitizes human lung carcinoma cells to treatment with the DNA-damaging agent cisplatin PMID: 11920544
  13. Rad9, Hus1, and Rad1 heterotrimeric complex chromatin binding is a proximal event in the checkpoint signaling cascade PMID: 12228248
  14. HUS1 is an unstable protein that is actively degraded via the ubiquitin-proteasome pathway. Its expression can be stabilized by treating cells with proteasome-specific inhibitors. PMID: 15122316
  15. The human Rad9/Rad1/Hus1 complex interacts with and stimulates DNA polymerase beta activity. PMID: 15314187
  16. complex with rad1 and rad9 is a damage-specific activator of flap endonuclease 1 PMID: 15556996
  17. The long-patch base excision machinery is an important target of the Rad9-Rad1-Hus1 complex, thus enhancing the quality control of DNA. PMID: 15871698
  18. PCNA and the Rad9/Rad1/Hus1 complex can independently bind and activate Fen1; acetylation of Fen1 by p300-HAT abolished the stimulatory effect of the complex but not that of PCNA, suggesting a possible mechanism of regulation of this repair pathway PMID: 16216273
  19. human DNA ligase I is stimulated by the Rad9-rad1-Hus1 checkpoint complex PMID: 16731526
  20. These data provide in vivo evidence that the human 9-1-1 complex participates in DNA repair in addition to its previously described role in DNA damage sensing. PMID: 16814252
  21. Human NEIL1 DNA glycosylase activity is significantly stimulated by Hus1 and by the Rad9/Rad1/Hus1 heterotrimer. PMID: 17395641
  22. we report successful tri-cistronic cloning, overexpression and purification of a three-protein complex of Rad9, Rad1 and Hus1 using a single hexa-histidine tag. PMID: 17493829
  23. Jab1 physically associates with the 9-1-1 complex (Rad1-Rad9-Hus1) PMID: 17583730
  24. Human thymine DNA glycosylase activity is significantly stimulated by hHus1, hRad1, hRad9 separately, and by the 9-1-1 complex. PMID: 17855402
  25. Hus1 levels correlated significantly with the clinicopathologic factors of bad prognosis in epithelial ovarian tumors PMID: 18156970
  26. Loss of HUS1 sensitizes cells to etopside-induced apoptosis by regulating BH3-only proteins. PMID: 18794804
  27. The DNA binding domain (DBD) within the hLigI catalytic fragment interacts with both PCNA and the heterotrimeric cell-cycle checkpoint clamp, hRad9-hRad1-hHus1 (9-1-1). PMID: 19523882
  28. The interdomain connecting loops (IDC loop) of hRad9, hHus1, and hRad1 are largely divergent and unique structural features of the 9-1-1 complex that are proposed to contribute to DNA damage recognition. PMID: 19535328
  29. Functional study of the yeast homolog. PMID: 9524127

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Subcellular Location Nucleus, Cytoplasm, cytosol
Protein Families HUS1 family
Tissue Specificity Ubiquitous.
Database Links

HGNC: 5309

OMIM: 603760

KEGG: hsa:3364

STRING: 9606.ENSP00000258774

UniGene: Hs.152983


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