Recombinant Human NLK Protein (His & GST Tag)

Beta LifeScience SKU/CAT #: BLPSN-3529

Recombinant Human NLK Protein (His & GST Tag)

Beta LifeScience SKU/CAT #: BLPSN-3529
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Tag His&GST
Host Species Human
Accession Q9UBE8
Background Nemo-like kinase contains 1 protein kinase domain and belongs to the protein kinase superfamily, CMGC Ser/Thr protein kinase family and MAP kinase subfamily. It also contains a TQE activation loop motif in which autophosphorylation of the threonine residue (Thr-298) is sufficient for kinase activation. As a serine/threonine-protein kinase, nemo-like kinase regulates a number of transcription factors with key roles in cell fate determination. It is a positive effector of the non-canonical Wnt signaling pathway, acting downstream of WNT5A, MAP3K7/TAK1 and HIPK2. Activation of this pathway causes binding to and phosphorylation of the histone methyltransferase SETDB1. The NLK-SETDB1 complex subsequently interacts with PPARG, leading to methylation of PPARG target promoters at histone H3K9 and transcriptional silencing. The resulting loss of PPARG target gene transcription inhibits adipogenesis and promotes osteoblastogenesis in mesenchymal stem cells (MSCs). Nemo-like kinase also is a negative regulator of the canonical Wnt/beta-catenin signaling pathway.
Description A DNA sequence encoding the human NLK (Q9UBE8) (Val121-Glu527) was fused with the N-terminal His-tagged GST tag at the N-terminus.
Source Baculovirus-Insect Cells
Predicted N Terminal Met
AA Sequence Val121-Glu527
Molecular Weight The recombinant human NLK /GST chimera consists of 644 a.a. and has a calculated molecular mass of 74.1 kDa. The recombinant protein migrates as an approximately 73 kDa band in SDS-PAGE under reducing conditions.
Purity >91% as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity The specific activity was determined to be 3 nmol/min/mg using MBP as substrate.
Formulation Supplied as sterile 20mM Tris, 500mM NaCl, pH 8.0, 10% gly.
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function Serine/threonine-protein kinase that regulates a number of transcription factors with key roles in cell fate determination. Positive effector of the non-canonical Wnt signaling pathway, acting downstream of WNT5A, MAP3K7/TAK1 and HIPK2. Negative regulator of the canonical Wnt/beta-catenin signaling pathway. Binds to and phosphorylates TCF7L2/TCF4 and LEF1, promoting the dissociation of the TCF7L2/LEF1/beta-catenin complex from DNA, as well as the ubiquitination and subsequent proteolysis of LEF1. Together these effects inhibit the transcriptional activation of canonical Wnt/beta-catenin target genes. Negative regulator of the Notch signaling pathway. Binds to and phosphorylates NOTCH1, thereby preventing the formation of a transcriptionally active ternary complex of NOTCH1, RBPJ/RBPSUH and MAML1. Negative regulator of the MYB family of transcription factors. Phosphorylation of MYB leads to its subsequent proteolysis while phosphorylation of MYBL1 and MYBL2 inhibits their interaction with the coactivator CREBBP. Other transcription factors may also be inhibited by direct phosphorylation of CREBBP itself. Acts downstream of IL6 and MAP3K7/TAK1 to phosphorylate STAT3, which is in turn required for activation of NLK by MAP3K7/TAK1. Upon IL1B stimulus, cooperates with ATF5 to activate the transactivation activity of C/EBP subfamily members. Phosphorylates ATF5 but also stabilizes ATF5 protein levels in a kinase-independent manner.
Subcellular Location Nucleus. Cytoplasm.
Protein Families Protein kinase superfamily, CMGC Ser/Thr protein kinase family, MAP kinase subfamily
Database References

Gene Functions References

  1. overexpression of miR-221 decreased LEF1 phosphorylation but increased the expression of MYCN via targeting of NLK and further regulated cell cycle, particularly in S-phase. This study provides a novel insight for miR-221 in the control of neuroblastoma cell proliferation and tumorigenesis, suggesting potentials of miR-221 as a prognosis marker and therapeutic target for patients with MYCN overexpressing neuroblastoma. PMID: 28003306
  2. NLK is a novel signaling molecule for proper lung development through the interconnection between epithelial and endothelial cells during lung morphogenesis PMID: 27035511
  3. Our results suggest that NLK inhibits transcriptional activation of Nurr1 gene by impeding CBP's role as a co-activator of NF-kappaB and CREB in prostate cancer. PMID: 27036119
  4. The expression of NLK was negatively correlated with TCF4 expression in lung cancers PMID: 26823848
  5. NLK overexpression is an independent prognostic factor in colorectal cancer and knockdown of NLK expression inhibits colorectal cancer progression and metastasis. PMID: 26269673
  6. Further experiments demonstrated that the overexpression of miR3623p resulted in decrease expression levels of nemo-like kinase PMID: 26647877
  7. NLK was involved in miR-92b-induced cell proliferation, and its protein level was obviously downregulated in the miR-92b-overexpressing xenograft tumors. PMID: 26503628
  8. Data show that metformin inhibits nemo like kinase (NLK) expression and might be a potential treatment strategy for non-small cell lung cancer (NSCLC). PMID: 26503334
  9. Down-regulation of NLK inhibited tumorigenesis and up-regulated the expression of cell cycle proteins in laryngeal cancer cells. PMID: 26252054
  10. In this review, we will make a summary on the comprehensive roles of NLK in the regulation of various cancers PMID: 26427665
  11. NLK was an identified miR-199a-3p target gene and functioned as a tumor suppressor gene in colorectal cancer. PMID: 24972723
  12. NLK overexpression is associated with poor overall survival in patients with hepatocellular carcinoma(HCC), it might be an independent poor prognostic marker for HCC. PMID: 26022162
  13. NLK phosphorylates Raptor on S863 to disrupt its interaction with the Rag GTPase, which is important for mTORC1 lysosomal recruitment. PMID: 26588989
  14. our work first demonstrated that miR-197 can confer drug resistance to Taxol, by regulating tumor suppressor, NLK expression in ovarian cancer cells. PMID: 25833695
  15. Data indicate that heat-shock protein 27 HSP27) binds to Nemo-like kinase (NLK) in the nucleus. PMID: 24816797
  16. NLK is an important p53 regulator that responds to DNA damage. NLK interacts with p53 and stabilizes p53 by blocking MDM2-mediated p53 ubiquitination and degradation. PMID: 24926618
  17. High nemo-like kinase expression is associated with drug resistance in laryngeal cancer. PMID: 24460265
  18. NLK is a negative regulator in cell proliferation of non-small-cell lung cancer by modulating the activity of Wnt/beta-catenin signaling. PMID: 23904219
  19. NLK functions as a pivotal negative regulator of NF-kappaB via disrupting the interaction of TAK1 with IKKbeta. PMID: 24721172
  20. The results suggest that NLK silencing by lentivirus-mediated RNA interference would be a potential therapeutic method to control oral squamous carcinoma growth. PMID: 23983589
  21. NLK suppressed proliferation, induced apoptosis and mediated c-Myb degradation in MCF-7 cells. PMID: 23935942
  22. Data indicate that overexpression of nemo-like kinase (NLK) is closely related to progression of gallbladder cancer (GBC), and NLK could be used as a potential prognostic marker for GBC patients. PMID: 23857283
  23. Reduced expression of NLK is associated with glioma. PMID: 23416699
  24. Our results suggested that NLK is a key regulator involved in proliferation and migration of GBC, and it could be used as a potential therapeutic target for gallbladder carcinoma cells. PMID: 22733362
  25. Single nucleotide polymorphisms in NLK is associated with ovarian cancer. PMID: 22253297
  26. expression suppressed in the development of ovarian cancer PMID: 22027747
  27. NLK induces apoptosis in glioma cells via activation of caspases; NLK may be a useful independent prognostic indicator for glioma. PMID: 21177110
  28. ZIPK may serve as a transcriptional regulator of canonical Wnt/beta-catenin signaling through interaction with NLK/TCF4. PMID: 21454679
  29. dimerization is an initial key event required for the functional activation of NLK PMID: 21118996
  30. NLK is aberrantly regulated in hepatocellular carcinoma and this process appears to involve the induction of CDK2 and cyclin D1 PMID: 20512928
  31. findings provide the first evidence that TAK1-NLK pathway is a novel regulator of FOXO1 PMID: 20061393
  32. NLK negatively regulates Notch-dependent transcriptional activation by phosphorylating Notch1ICD. Phosphorylated Notch1ICD is impaired in its ability to form a transcriptionally active ternary complex. PMID: 20118921
  33. threonine 9 (Thr9) and Serine 138 (Ser138) within the N-terminal Mad homology1 (MH1) domain of Smad4 could be phosphorylated by NLK PMID: 19690946
  34. The induction of wild-type NLK in DLD-1 human colon cancer cells caused suppression of cell growth whereas the kinase-negative mutant did not. PMID: 12901858
  35. Nemo-like kinase is activated by Wnt PMID: 14960582
  36. STAT3 enhances the efficiency of its own Ser-727 phosphorylation by acting as a scaffold for the TAK1-NLK kinases PMID: 15764709
  37. These results strongly suggest that unlike cytokine signaling, Tax-induced NFkappaB activation does not involve K63 polyubiquitination-mediated MAP3K activation. PMID: 17418100
  38. Fbxw7, the F-box protein of an SCF complex, targets c-Myb for degradation in a Wnt-1- and NLK-dependent manner. PMID: 18765672
  39. NLK expression is altered during prostate cancer progression and it is involved in regulation of AR signaling in these cells PMID: 19514049

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.

Recently viewed