Human CLSPN ELISA Kit (V2LY-0626-LY3520)

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Tested Data
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Basic Information

Sensitivity
0.026 ng/mL
Detection Range
0.05-20 ng/mL
Sample Type
Serum, Plasma, cell culture supernates
Specificity
Human
Assay Type
Sandwich
Reactivity
Human
Assay Time
1.5 h
Molecule Mass
151.1 kDa
Components
  • Pre-coated ELISA Plate: 12 wells * 8 detachable strips
  • Standard solution: 0.5ml x1
  • Standard diluent: 3ml x1
  • Streptavidin-HRP: 6ml x1
  • Stop solution: 6ml x1
  • Substrate solution A: 6ml x1
  • Substrate solution B: 6ml x1
  • Wash buffer concentrate (25x): 20ml x1
  • Biotinylated antibody: 1ml x1

Formulations & Storage [For reference only, actual COA shall prevail!]

Storage
Store at 2-8°C
More Infomation

Target

Full Name
Claspin
Function
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.
Biological Process
Activation of protein kinase activity Source: UniProtKB
DNA damage checkpoint Source: UniProtKB
DNA repair Source: UniProtKB-KW
DNA replication Source: Reactome
DNA replication checkpoint Source: MGI
Mitotic DNA replication checkpoint Source: UniProtKB
Mitotic G2 DNA damage checkpoint Source: UniProtKB
Peptidyl-serine phosphorylation Source: UniProtKB
Protein deubiquitination Source: Reactome
Cellular Location
Nucleus
PTM
Phosphorylated. Undergoes ATR-dependent phosphorylation by CHEK1 during activation of DNA replication or damage checkpoints. Phosphorylation by CSNK1G1/CK1 promotes CHEK1 binding.
Ubiquitinated by the anaphase promoting complex/cyclosome (APC/C) during G1 phase, leading to its degradation by the proteasome. Ubiquitination is mediated via its interaction with FZR1/CDH1. Following DNA damage, it is deubiquitinated by USP28 in G2 phase, preventing its degradation.

Cai, C., Luo, J., Liu, Q., Liu, Z., Zhao, Y., Wu, X., ... & Liu, Y. (2021). Claspin overexpression promotes tumor progression and predicts poor clinical outcome in prostate cancer. Genetic Testing and Molecular Biomarkers, 25(2), 131-139.

Babasaki, T., Sentani, K., Sekino, Y., Kobayashi, G., Thang Pham, Q., Katsuya, N., ... & Yasui, W. (2021). Overexpression of claspin promotes docetaxel resistance and is associated with prostate‐specific antigen recurrence in prostate cancer. Cancer Medicine, 10(16), 5574-5588.

Mamoor, S. (2021). Differential expression of claspin in triple negative breast cancer.

Kobayashi, G., Sentani, K., Babasaki, T., Sekino, Y., Shigematsu, Y., Hayashi, T., ... & Yasui, W. (2020). Claspin overexpression is associated with high‐grade histology and poor prognosis in renal cell carcinoma. Cancer science, 111(3), 1020.

Azenha, D., Hernandez-Perez, S., Martin, Y., Viegas, M. S., Martins, A., Lopes, M. C., ... & Martins, T. C. (2020). Implications of CLSPN Variants in Cellular Function and Susceptibility to Cancer. Cancers, 12(9), 2396.

Kobayashi, G., Sentani, K., Hattori, T., Yamamoto, Y., Imai, T., Sakamoto, N., ... & Yasui, W. (2019). Clinicopathological significance of claspin overexpression and its association with spheroid formation in gastric cancer. Human pathology, 84, 8-17.

Bianco, J. N., Bergoglio, V., Lin, Y. L., Pillaire, M. J., Schmitz, A. L., Gilhodes, J., ... & Pasero, P. (2019). Overexpression of Claspin and Timeless protects cancer cells from replication stress in a checkpoint-independent manner. Nature communications, 10(1), 1-14.

Smits, V. A., Cabrera, E., Freire, R., & Gillespie, D. A. (2019). Claspin–checkpoint adaptor and DNA replication factor. The FEBS journal, 286(3), 441-455.

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For research use only. Not intended for any clinical use.

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