Recombinant Human Claspin(CLSPN) ,partial

Code CSB-YP888014HU
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Source Yeast
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Code CSB-EP888014HU
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Source E.coli
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Code CSB-EP888014HU-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-BP888014HU
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Source Baculovirus
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Code CSB-MP888014HU
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Source Mammalian cell
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Product Details

Purity >85% (SDS-PAGE)
Target Names CLSPN
Uniprot No. Q9HAW4
Alternative Names Claspin; claspin homolog (Xenopus laevis); Claspin homolog; CLSPN; CLSPN protein; CLSPN_HUMAN; hClaspin; Hu Claspin
Species Homo sapiens (Human)
Protein Length Partial
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)
Required for checkpoint mediated cell cycle arrest in response to inhibition of DNA replication or to DNA damage induced by both ionizing and UV irradiation. Adapter protein which binds to BRCA1 and the checkpoint kinase CHEK1 and facilitates the ATR-dependent phosphorylation of both proteins. Can also bind specifically to branched DNA structures and may associate with S-phase chromatin following formation of the pre-replication complex (pre-RC). This may indicate a role for this protein as a sensor which monitors the integrity of DNA replication forks.
Gene References into Functions
  1. The functions of claspin are discussed and how its deregulation may contribute to cancer initiation and progression. [REVIEW] PMID: 28942358
  2. Results unveil a new aspect of PERK function and previously unknown roles for Claspin and Chk1 as negative regulators of DNA replication in the absence of genotoxic stress. PMID: 27375025
  3. found that USP9X regulated the expression and stability of CLASPIN in an S-phase-specific manner. USP9X depletion profoundly impairs the progression of DNA replication forks, causing unscheduled termination events with a frequency similar to CLASPIN depletion, resulting in excessive endogenous DNA damage PMID: 26921344
  4. Functional analyses indicat that the expression TopBP1 and Claspin positively affects the survival of brain cancer cells after exposure to radiation. PMID: 25216549
  5. And-1 coordinates with Claspin for efficient Chk1 activation in response to replication stress. PMID: 26082189
  6. Rad9, Rad17, TopBP1 and claspin play essential roles in heat-induced activation of ATR kinase and heat tolerance. PMID: 23383325
  7. findings identify claspin as an in vivo substrate for the BRCA1 E3 ligase and suggest that its modification selectively triggers CHK1 activation for the homology-directed repair of a subset of genotoxic lesions PMID: 22863316
  8. analysis of claspin expression could be clinically relevant in the diagnosis of HPV-related cervical lesions, in particular when applied to cervico-vaginal cytology PMID: 22731782
  9. The conserved C terminus of Claspin interacts with Rad9 and ensures timely activation of the ATR-Chk1 pathway. PMID: 22732499
  10. the functions of Claspin and the functional relationship between Claspin and Rad17 were studied. PMID: 21945441
  11. In the presence of BRCA1, endogenous HERC2 interacts with Claspin, a protein essential for G(2)-M checkpoint activation and replication fork stability. PMID: 21775519
  12. The multiple protein-DNA and protein-protein interactions is important for Claspin function during DNA replication and DNA replication checkpoint signaling. PMID: 21478680
  13. Tethering DNA damage checkpoint mediator proteins topoisomerase IIbeta-binding protein 1 (TopBP1) and Claspin to DNA activates ataxia-telangiectasia mutated and RAD3-related (ATR) phosphorylation of checkpoint kinase 1 (Chk1). PMID: 21502314
  14. Here, the authors demonstrate that both the NF-kappaB family of transcription factors and their upstream kinase IKK can regulate Claspin levels by controlling its mRNA expression. PMID: 20657549
  15. Rad9A-mediated Claspin localization is a vital step during checkpoint activation. PMID: 20081369
  16. Data show that the ATR-dependent phosphorylation of Chk1, but not p53, is strongly stimulated by Claspin. PMID: 19828454
  17. Resequenced CLSPN from the germline of selected cancer families; eight nonsynonymous variants, including a recurrent mutation, were id'd from the germline of two cancer-prone individuals and 5 cancer cell lines of breast, ovarian, & hematopoietic origin. PMID: 19737971
  18. Claspin has a potentially critical role in replication checkpoint control in mammalian cells PMID: 12766152
  19. determination of properties of both a tumor suppressor and an oncogene PMID: 15096610
  20. has a ring-like structure and binds with high affinity to branched DNA molecules. PMID: 15226314
  21. Claspin has roles in the Chk1 pathway and functions in checkpoint control [review] PMID: 15279790
  22. cleavage of Claspin by caspase-7 inactivates the Chk1 signaling pathway PMID: 16123041
  23. Claspin and Chk1 proteins regulate each other and thus ensure the proper cell cycle progression and replication checkpoint control. PMID: 16501606
  24. the Chk1 pathway is regulated through both phosphorylation of Claspin and its controlled degradation. PMID: 16828751
  25. These results suggest that while TopBP1 is a general regulator of ATR, Claspin operates downstream of TopBP1 to selectively regulate the Chk1-controlled branch of the genotoxic stress response. PMID: 16880517
  26. Data suggest that degradation of Claspin by SCFbetaTrCP restrains Chk1 activation. PMID: 16885021
  27. The SCFbetaTrCP-dependent degradation of claspin is necessary for the efficient and timely termination of the DNA replication checkpoint. PMID: 16885022
  28. The degradation of Claspin at the onset of mitosis is an essential step for the recovery of a cell from a DNA-damage-induced cell-cycle arrest. PMID: 16934469
  29. Chk1 can be activated in a claspin-dependent manner leading to cyclin B1 down-regulation and providing the cells of an additional mechanism to inhibit mitosis entry in Hela cells. PMID: 16951182
  30. phosphorylation of Claspin repeats in human Claspin is important for Claspin function and the regulation of Claspin-Checkpoint kinase 1 interaction in human cells PMID: 16963448
  31. human Claspin is found in complex with PCNA, an essential component of the DNA replication machinery, and is released upon DNA replication arrest. dissociation of Claspin-PCNA could be part of the signal leading to Chk1 activation. PMID: 17274954
  32. downregulation of Claspin protein levels by short interfering RNA resulted in an increase in apoptotic induction both in the presence and absence of DNA damage PMID: 17431426
  33. Altogether seven different sequence changes were observed, but none of them appeared to associate with breast cancer susceptibility. PMID: 18077083
  34. These results demonstrate that phosphorylation of Claspin within the Chk1-binding domain is catalysed by an ATR-dependent kinase distinct from Chk1. PMID: 18331829
  35. Depletion of Chk1 and Claspin together doubled the percentage of very slow forks, compared with depletion of either protein alone. PMID: 18353973
  36. Data show that Chk1 and the Claspin-Timeless module of replication forks not only participate in ATR signaling, but also protect stressed forks independently of ATR. PMID: 18451105
  37. Claspin plays a role regulating replication fork stability that is independent of its function in mediating Chk1 phosphorylation. PMID: 19270516
  38. Cdh1 reciprocally regulates the Rb pathway through competing with E2F1 to bind the hypophosphorylated form of Rb. PMID: 19477924

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Subcellular Location Nucleus
Protein Families Claspin family
Database Links

HGNC: 19715

OMIM: 605434

KEGG: hsa:63967

STRING: 9606.ENSP00000312995

UniGene: Hs.175613

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