Recombinant Human CDC25C Protein

Beta LifeScience SKU/CAT #: BL-0222SG

Recombinant Human CDC25C Protein

Beta LifeScience SKU/CAT #: BL-0222SG
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Product Overview

Tag GST
Host Species Human
Accession BC019089
Synonym CDC25
Background CDC25C (also known as cell division cycle 25 homolog C) is a member of the CDC25 phosphatase family. CDC25C is highly conserved during evolution and it plays a key role in the regulation of cell division. CDC25C activates the partially purified p34 (cdc2)/cyclin B complex and directs the dephosphorylation of cyclin B-bound CDC2 and triggers entry into mitosis (1). CDC25C also suppresses p53-induced growth arrest. The regulation of CDC25B phosphorylation by p38 is a critical event for initiating the G2/M checkpoint after ultraviolet radiation (2).
Description Full-length recombinant human CDC25C was produced in Sf9 insect cells, fused with a GST tag at N-terminus. This protein is purified with our unique purification methods. This protein is purified with our unique purification methods.
Source Sf9 insect cells
AA Sequence Full Length
Molecular Weight ~84 kDa
Purity For specific purity information on a given lot, see related COA.
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity Active
Formulation Recombinant protein is supplied in 50mM Tris-HCl, pH 7.5, 50mM NaCl, 10mM Glutathione, 0.25mM DTT, 0.1mM EDTA, 0.1mM PMSF and 25% glycerol.
Stability The recombinant protein is stable for up to 12 months at -70°C
Usage For Research Use Only
Storage Recombinant Human CDC25C Protein should be stored should be stored at < -70°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function Functions as a dosage-dependent inducer in mitotic control. Tyrosine protein phosphatase required for progression of the cell cycle. When phosphorylated, highly effective in activating G2 cells into prophase. Directly dephosphorylates CDK1 and activates its kinase activity.
Subcellular Location Nucleus.
Protein Families MPI phosphatase family
Database References

Gene Functions References

  1. Cells lacking ARID1A show enhanced AURKA transcription, which leads to the persistent activation of CDC25C, a key protein for G2/M transition and mitotic entry. PMID: 30097580
  2. FHL1 increase inhibitory CDC25 phosphorylation by forming a complex with CHK2 and CDC25, and sequester CDC25 in the cytoplasm by forming another complex with 14-3-3 and CDC25, resulting in increased radioresistance in cancer cells. PMID: 28094252
  3. CDC25A plays a novel role in regulating the malignant behavior of glioma stem cells as a part of Linc00152/miR-103a-3p/FEZF1/CDC25A axis. PMID: 28651608
  4. Overexpression of the CDK1 and CDC25A may have a role in the pathogenesis of the NFPA. PMID: 28004354
  5. Mdm2 overexpression and Cdc25C downregulation delay cell cycle progression through the G2/M phase. PMID: 28806397
  6. Xanthatin functions as a DNA-damaging agent in non-small cell lung carcinomas by activating Chk1-mediated DDR and lysosome-mediated degradation of Cdc25C. PMID: 29074359
  7. Myelodysplastic syndrome -related P95 point mutants of SRSF2 lead to alternative splicing of CDC25C in a manner that is not dependent on the DNA damage response. PMID: 27552991
  8. The aim of this review is to shed light on the role of four different phosphatases (PTEN, PP2A, CDC25 and DUSP1) in five different solid tumors (breast cancer, lung cancer, pancreatic cancer, prostate cancer and ovarian cancer), in order to better understand the most frequent and aggressive primary cancer of the central nervous system, glioblastoma. PMID: 28801478
  9. Data show that TRIB2-mediated degradation of CDC25C is associated with lysine-48-linked CDC25C polyubiquitination driven by the TRIB2 kinase-like domain. PMID: 27563873
  10. High expression of pCHK2-Thr68 was associated with decreased patient survival (p = 0.001), but was not an independent prognostic factor. Our results suggest that pCHK2-Thr68 and pCDC25C-Ser216 play important roles in breast cancer and may be potential treatment targets PMID: 27801830
  11. the biology of the activation/deactivation of CDC25 by kinases/phosphatases to maintain the level of CDK-cyclin activities and thus the genomic stability PMID: 27038604
  12. the knockdown of CDC25C can reduce both the radiotherapy sensitivity and the proliferation activity of EC9706 cells. PMID: 27188256
  13. results identify CDC25C as a downstream target of the mutated tyrosine kinase FLT3-ITD affecting cell-cycle regulation in a model of AML PMID: 27919943
  14. Suggest that the p53-p21-DREAM-CDE/CHR pathway regulates p53-dependent repression of Survivin, CDC25C, and PLK1 in HCT116 cells. PMID: 26595675
  15. These miR-142-3p functioned as a tumor suppressor by targeting CDC25C. PMID: 26805039
  16. Cdc25C negatively regulates proapoptotic ASK1 in a cell cycle-dependent manner and may play a role in G2/M checkpoint-mediated apoptosis. PMID: 25633196
  17. Recurrent CDC25C mutations drive malignant transformation in familial platelet disorder to acute myelogenous leukaemia. PMID: 25159113
  18. we conclude that inhibition of KIF22 suppresses cancer cell proliferation by delaying mitotic exit through the transcriptional upregulation of CDC25C. PMID: 24626146
  19. These findings indicate that DHM inhibits the growth of hepatocellular carcinoma (HCC) cells via G2/M phase cell cycle arrest through Chk1/Chk2/Cdc25C pathway PMID: 24002546
  20. Purification and biochemical analysis of catalytically active human cdc25C dual specificity phosphatase PMID: 23567337
  21. protein plays a role in regulating PCa cell growth, and androgen treatments, but not EGF, greatly increase Cdc25C protein levels in AS PCa cells, which is in part by decreasing its degradation. PMID: 23637932
  22. dose-dependent Cdc25c phosphatase acts as an early G2-phase checkpoint, thus indicating mechanistic importance in the low-dose hyper-radiosensitivity and induced radioresistance transition PMID: 22843362
  23. data suggest that the maintenance of CDC25 activity does not fully rely on the thioredoxin reductase system in breast cancer cells, even in the presence of a major oxidative stress PMID: 22360685
  24. cloning and functional analysis of Cdc25C PMID: 22394631
  25. MMEQ induced G2/M arrest through the promotion of cdc25c in TSGH8301 cells. PMID: 22021033
  26. Inhibition of CK2 activity by three different inhibitors led to a down-regulation of the level of cdc25C. PMID: 21750987
  27. Two additional sites other than Ser216 in the widely studied cell division cycle (Cdc) protein 25C, whose function depends on 14-3-3 binding, were identified. PMID: 21189416
  28. The results show for the first time that in human mitosis, distinct phospho-isoforms of cdc25C exist with different localizations and interacting partners. PMID: 20668692
  29. ATM and Chk1/2 mediated phosphorylation of cdc25c plays a major role in cell cycle arrest induced by pectenotoxin2. PMID: 20514472
  30. CDC25C and phospho-CDC25C (Ser216) play a crucial role in the pathogenesis and/or progression of vulvar squamous cell carcinomas. PMID: 20500813
  31. Adventitious arsenate reductase activity of the catalytic domain of the human and Cdc25C phosphatases PMID: 20025242
  32. Analysis of cell cycle profile and cell cycle regulatory proteins indicated that arsenite arrested cell cycle at G(2)/M phase, partially through induction of cell division cycle 25 (Cdc25) isoform C (Cdc25C) degradation via ubiquitin-proteasome pathways PMID: 11842186
  33. results suggest that Plk1 phosphorylates Cdc25C on Ser198 and regulates nuclear translocation of Cdc25C during prophase PMID: 11897663
  34. role of degradation by oxidative stress in induction of cell cycle arrest PMID: 11925443
  35. Human CDC25B and CDC25C differ by their ability to restore a functional checkpoint response after gene replacement in fission yeast PMID: 12099692
  36. Ca2+ promotes erythrocyte band 3 tyrosine phosphorylation via dissociation of phosphotyrosine phosphatase from band 3. PMID: 12175337
  37. phosphorylation by Chk2 PMID: 12386164
  38. CDC25C is phosphorylated on Ser 214 during mitosis which, in turn, prevents phosphorylation of Ser 216. HeLa cells depeleted of endogenous CDC25C, when treated with exogenous CDC25C, had a substantial delay to mitotic entry. PMID: 12766774
  39. cdc25C not only plays a role at the G2/M transition but also in the modulation of DNA replication PMID: 12857880
  40. CDC25C translocation to the cell nucleus upon entry into mitosis is coordinated by Plk3 PMID: 14968113
  41. binding to VPR protein in human cell lines correlates with G2 arrest PMID: 14972559
  42. downregulation of Cdc25C is mediated by p53 via two independent mechanisms, one involving direct binding to the cdc25C promoter PMID: 15574328
  43. Vpr promotes cell cycle arrest at the G(2)/M phase by facilitating association of 14-3-3 and Cdc25C PMID: 15708996
  44. Vitamin C transiently arrests cancer cell cycle progression in S phase and G2/M boundary by modulating the kinetics of activation of CDC25C. PMID: 15887239
  45. Data suggests that CDC25C might play an important role in prostate cancer progression and could be used to monitor and predict the aggressiveness of this disease. PMID: 16000564
  46. Data suggest that Pim-1 activates Cdc25C by a direct phosphorylation and can thereby assume the function of a positive cell cycle regulator at the G2/M transition. PMID: 16356754
  47. Crystallization experiments of PLK1 protein in complex with an unphosphorylated and a phosphorylated target peptide from Cdc25C yield crystals suitable for X-ray diffraction analysis. PMID: 16582488
  48. These results demonstrate that the MAPK ERK signaling pathway contributes to the p53-independent antiproliferative functions of p14ARF. Furthermore, they identify a new mechanism by which phosphorylation at serine 216 participates to Cdc25C inactivation. PMID: 16582626
  49. Phosphorylation of cdc25c can be used to test whether a pharmacologic inhibitor of Plk1 would exert the same cellular effects as interference with Plk1 on an mRNA level. PMID: 16648550
  50. Chk1-mediated phosphorylation of Cdc25C plays a major role in response to LOR-mediated G(2)/M arrest. Although the Chk1-mediated cell growth arrest in a tumor cell line. PMID: 16649252

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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