Recombinant Human Wee1 Protein

Beta LifeScience SKU/CAT #: BLA-9700P

Recombinant Human Wee1 Protein

Beta LifeScience SKU/CAT #: BLA-9700P
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Product Overview

Host Species Human
Accession P30291
Synonym DKFZp686I18166 EC 2.7.10.2 FLJ16446 MGC105683 OTTHUMP00000231338 OTTHUMP00000231339 Wee 1 WEE 1 homolog 1 (S. pombe) WEE1 Wee1 homolog WEE1 homolog (S. pombe) WEE1 homolog S. pombe Wee1 like protein kinase Wee1 tyrosine kinase Wee1+ homolog Wee1+ S. pombe homolog WEE1, S. pombe, homolog of WEE1, somatic Wee1-like protein kinase WEE1_HUMAN WEE1A Wee1A kinase WEE1hu
Description Recombinant Human Wee1 Protein was expressed in E.coli. It is a Protein fragment
Source E.coli
Molecular Weight 115 kDa including tags
Purity >75% SDS-PAGE.Assessed by densitometry.
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Liquid Solution
Stability The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution See related COA
Unit Definition For Research Use Only
Storage Buffer Shipped on dry ice. Upon delivery aliquot and store at -80°C. Avoid freeze / thaw cycle.

Target Details

Target Function Acts as a negative regulator of entry into mitosis (G2 to M transition) by protecting the nucleus from cytoplasmically activated cyclin B1-complexed CDK1 before the onset of mitosis by mediating phosphorylation of CDK1 on 'Tyr-15'. Specifically phosphorylates and inactivates cyclin B1-complexed CDK1 reaching a maximum during G2 phase and a minimum as cells enter M phase. Phosphorylation of cyclin B1-CDK1 occurs exclusively on 'Tyr-15' and phosphorylation of monomeric CDK1 does not occur. Its activity increases during S and G2 phases and decreases at M phase when it is hyperphosphorylated. A correlated decrease in protein level occurs at M/G1 phase, probably due to its degradation.
Subcellular Location Nucleus.
Protein Families Protein kinase superfamily, Ser/Thr protein kinase family, WEE1 subfamily
Database References

Gene Functions References

  1. ATR inhibition synergizes with WEE1 inhibition in TNBC. PMID: 29605721
  2. Inhibition of Wee1 by its specific inhibitor MK1775 in combination with sorafenib restored the KRAS mutated cells' response to the multi-target tyrosine kinase inhibitor. PMID: 29343688
  3. miR-26b governed temozolomide (TMZ)-resistance-mediate epithelial-mesenchymal transition partly due to governing its target Wee1. PMID: 28898169
  4. the data suggest the importance of WEE1 as an enabler of branching vascularisation in colorectal cancer liver metastases. PMID: 28178688
  5. WEE1 is over-expressed and could enhance gastric cancer cell proliferation and metastasis PMID: 27363019
  6. Wee1 is identified as a novel direct target of miR-194. Ectopic expression of Wee1 at least in part overcomes the suppressive impacts of miR-194 on the malignant phenotypes of human laryngeal squamous cell carcinoma PMID: 28122647
  7. High WEE1 expression is associated with non-small cell lung cancer. PMID: 28652249
  8. miR-503 could function as an enhancer of radiation responses in laryngeal carcinoma cells by inhibiting WEE1 PMID: 29019284
  9. Data suggest that SMURF1 is required for S phase progression; SMURF1 promotes ubiquitination-dependent degradation of WEE1; these functions of SMURF1 appear to be linked and may be important in cell proliferation and tumorigenesis. (SMURF1 = SMAD specific E3 ubiquitin protein ligase 1; WEE1 = wee 1 homolog [S pombe] protein) PMID: 28294307
  10. Date show that when Wee1 alone is inhibited, Chk1 suppresses CDC45 loading and thereby limits the extent of unscheduled replication initiation and subsequent S-phase DNA damage, despite very high CDK-activity. PMID: 28030798
  11. we overexpressed CKS1B in multiple cell lines and found increased sensitivity to PLK1 knockdown and PLK1 drug inhibition. Finally, combined inhibition of WEE1 and PLK1 results in less apoptosis than predicted based on an additive model of the individual inhibitors, showing an epistatic interaction and confirming a prediction of the yeast data. PMID: 27558135
  12. Wee1 staining intensity was a predictor of favorable metastasis-free and overall survival compared to strong intensity and no or weak staining PMID: 27220319
  13. These results highlight the key role of WEE1 suppression to combat glioblastomas. Moreover, it showed beneficial possibilities of WEE1 suppression with different anticancer approaches for neurological malignancies. PMID: 27072241
  14. Wee1 inhibition potentiates Wip1-dependent tumor sensitization effect by reducing levels of Hipk2 kinase, a negative regulator of Wip1 pathway. PMID: 27077811
  15. High nuclear expression of WEE1 protein is associated with all glioma grades and types. PMID: 26738845
  16. Consistent with these findings, a genome-scale pooled RNA interference screen revealed that toxic doses of MK-1775 are suppressed by CDK2 or Cyclin A2 knockdown. These findings support G2 exit as the more significant effect of Wee1 inhibition in pancreatic cancers. PMID: 26890070
  17. WEE1 is regulated at the translational level by CPEB1 and miR-15b in a coordinated and cell-cycle-dependent manner. PMID: 27027998
  18. Data show that proto-oncogene protein Mdm2 inactivation successfully protects tumor suppressor protein (p53)-proficient cells against the cytotoxic effects of Wee1 protein inhibition. PMID: 26431163
  19. nasopharyngeal carcinoma cells depend on CHK1 and WEE1 activity for growth PMID: 26025928
  20. data indicate that the activity of the DNA replication machinery, beyond TP53 mutation status, determines Wee1 inhibitor sensitivity, and could serve as a selection criterion for Wee1-inhibitor eligible patients PMID: 26598692
  21. These results suggest that the G2 checkpoint inhibitor MK-1775 can enhance the sensitivity of human NSCLC cells to C ions as well as X rays. PMID: 26645158
  22. Data show that H3K36me3-deficient cancers can be targeted by inhibition of WEE1 protein. PMID: 26602815
  23. Report strong synergism observed by combining Chk1 and Wee1 inhibitors in preclinical models of mantle cell lymphoma. PMID: 25428911
  24. These data provide a rationale for further evaluation of the combination of Wee1 and Chk1/2 inhibitors in malignant melanoma. PMID: 26054341
  25. This study showed that WEE1 (rs10770042; coding) associated with Alzheimer disease. PMID: 25649652
  26. WEE1 is a valid target of the miR-17-92 cluster in leukemia. PMID: 25732734
  27. Study shows that CHD5 is a Nucleosome remodeling and deacetylase complex-associated transcriptional repressor and identifies WEE1 as one of the CHD5-regulated genes that may link CHD5 to tumor suppression. PMID: 25247294
  28. identified the PI3K/Akt pathway, the cell-cycle regulator Wee1 kinase, and protein kinase C (PKC) as prospective regulatory nodes of neuronal excitability through modulation of the FGF14:Nav1.6 complex. PMID: 25659151
  29. These results suggest that specific inhibition of Wee1 has deleterious effects on the proliferation and survival of p53 inactive tumors. PMID: 24927813
  30. Regulation of the mitotic inhibitor Wee1 by TOR signalling is a conserved mechanism that helps to couple cell cycle and growth controls. PMID: 24424027
  31. High WEE1 expression is associated with breast cancer. PMID: 24377575
  32. Wee1 is frequently expressed in ovarian serous carcinoma effusions, and its expression is significantly higher following exposure to chemotherapy and it is an independent prognostic marker in serous ovarian carcinoma. PMID: 25093290
  33. Taken together, these findings highlight mitotic kinases and, in particular, WEE1 as a rational therapeutic target for medulloblastoma. PMID: 24661910
  34. role for CK1delta in controlling the cell cycle PMID: 24817118
  35. Inhibition of WEE1 counters the defective apoptosis of tumor cells expressing high levels of brachyury. PMID: 24626094
  36. miR-16 and miR-26a target checkpoint kinases Wee1 and Chk1 in response to p53 activation by genotoxic stress. PMID: 24336073
  37. A novel mechanism that pancreatic ductal adenocarcinoma cells use to protect against DNA damage in which HuR posttranscriptionally regulates the expression and downstream function of WEE1 upon exposure to DNA-damaging agents. PMID: 24536047
  38. Together, these studies have identified Wee1 as a key target of XL888, suggesting novel therapeutic strategies for NRAS-mutant melanoma. PMID: 23538902
  39. Our results suggest that Wee1 may be involved in the progression of vulvar carcinomas PMID: 23767999
  40. study shows WEE1 expression in malignant melanoma is directly regulated by miR-195; miR-195-mediated downregulation of WEE1 in metastatic lesions may help to overcome cell cycle arrest under stress conditions in the local tissue microenvironment to allow unrestricted growth of tumour cells PMID: 22847610
  41. AURKB and WEE1 are targets and biomarkers of therapeutic efficacy, lying downstream of (V600E)B-RAF in melanomas. PMID: 23416158
  42. miR-497 is a candidate tumor suppressor in neuroblastoma, through the direct targeting of WEE1. PMID: 23531080
  43. These data support the hypothesis that Cdc14A counteracts Cdk1-cyclin B1 activity through Wee1 dephosphorylation. PMID: 23051732
  44. WEE1 accumulation and deregulation of S-phase proteins mediate MLN4924 potent inhibitory effect on Ewing sarcoma cells. PMID: 22641220
  45. Loss-of-function and gain-of-function studies showed that miR-15 family members controlled the expression of WEE1 and CHK1. PMID: 22942255
  46. Wee1 inhibition sensitizes cancer cells to Hsp90 inhibitors. PMID: 22935698
  47. The results suggested that deregulated CDK1 activity, such as that occurring following inhibition of WEE1 kinase, induces replication stress and loss of genomic integrity through increased firing of replication origins and subsequent nucleotide shortage. PMID: 22907750
  48. results reveal the importance of Wee1 as a prognostic biomarker in melanomas, and indicate a potential role for targeted therapy, alone or in combination with other agents PMID: 22719872
  49. Data identify Cdc20, USP44, and Wee1 as relevant Fcp1 targets. PMID: 22692537
  50. Elevated WEE1 expression is associated with acute myeloid leukemia. PMID: 22289989

FAQs

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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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