Recombinant Human Lymphokine-Activated Killer T-Cell-Originated Protein Kinase (PBK) Protein (His)

Beta LifeScience SKU/CAT #: BLC-07803P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.

Recombinant Human Lymphokine-Activated Killer T-Cell-Originated Protein Kinase (PBK) Protein (His)

Beta LifeScience SKU/CAT #: BLC-07803P
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.

Product Overview

Description Recombinant Human Lymphokine-Activated Killer T-Cell-Originated Protein Kinase (PBK) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb Q96KB5
Target Symbol PBK
Synonyms Cancer/testis antigen 84 MAPKK-like protein kinase Nori-3 PDZ-binding kinase Spermatogenesis-related protein kinase T-LAK cell-originated protein kinase
Species Homo sapiens (Human)
Expression System E.coli
Tag N-10His
Target Protein Sequence MEGISNFKTPSKLSEKKKSVLCSTPTINIPASPFMQKLGFGTGVNVYLMKRSPRGLSHSPWAVKKINPICNDHYRSVYQKRLMDEAKILKSLHHPNIVGYRAFTEANDGSLCLAMEYGGEKSLNDLIEERYKASQDPFPAAIILKVALNMARGLKYLHQEKKLLHGDIKSSNVVIKGDFETIKICDVGVSLPLDENMTVTDPEACYIGTEPWKPKEAVEENGVITDKADIFAFGLTLWEMMTLSIPHINLSNDDDDEDKTFDESDFDDEAYYAALGTRPPINMEELDESYQKVIELFSVCTNEDPKDRPSAAHIVEALETDV
Expression Range 1-322aa
Protein Length Full Length
Mol. Weight 42.1 kDa
Research Area Signal Transduction
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function Phosphorylates MAP kinase p38. Seems to be active only in mitosis. May also play a role in the activation of lymphoid cells. When phosphorylated, forms a complex with TP53, leading to TP53 destabilization and attenuation of G2/M checkpoint during doxorubicin-induced DNA damage.
Protein Families Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase subfamily
Database References
Tissue Specificity Expressed in the testis and placenta. In the testis, restrictedly expressed in outer cell layer of seminiferous tubules.

Gene Functions References

  1. Results found that PBK/TOPK was upregulated and phosphorylated in HTLV1-transformed Tcell lines and ATLLderived Tcell lines. In addition, HTLV1 infection upregulated PBK/TOPK expression in PBMCs, suggesting that this kinase increases the rate of mitosis and expands malignant T cells. PMID: 29901068
  2. Findings strongly suggest that phosphorylated T-lymphokine-activated killer cell-originated protein kinase may be a potent biomarker to determine the outcome of patients with primary central nervous system lymphoma and to develop novel drugs to treat primary central nervous system lymphoma. PMID: 29575092
  3. the expression of TOPK be a novel alternative biomarker to categorize the malignancy of gliomas. PMID: 29271010
  4. CDK1-mediated mitotic phosphorylation of PDZ-binding kinase is involved in cytokinesis and inhibits its oncogenic activity. PMID: 28780319
  5. Data suggest that T-LAK cell-originated protein kinase (TOPK) might play a pivotal role in breast cancer invasion and metastasis. PMID: 28212583
  6. our study provide convincing evidences that FoxM1-regulated PBK exerts oncogenic activities towards HCC via the activation of beta-Catenin pathway. PMID: 28525379
  7. High TOPK expression is associated with liver cancer. PMID: 27582549
  8. The role of T-LAK cell-originated protein kinase directly promotes metastasis of colorectal cancer by modulating p53-related protein kinase. PMID: 28412249
  9. TOPK protein and transcriptional levels of FOXM1 were reduced by TOPK inhibitor treatment. PMID: 27334838
  10. Results indicate that src-family kinase (Src) is a upstream kinase of T-LAK cell-originated protein kinase (TOPK). PMID: 27016416
  11. Upregulation of proteasome subunit beta type 8 PSMB8 and PDZ binding kinase PBK was confirmed by real-time reverse transcription-PCR analysis. PMID: 26894977
  12. MiR-770-5p and PBK levels were inversely correlated in xenograft model mice. PMID: 28333152
  13. TOPK knockdown did not alter radiation response in normal tissues, but significantly enhanced radiosensitivity in cancer cells.These findings have clinical relevance, as elevated TOPK protein expression was associated with poorer clinical outcomes in prostate cancer patients treated with radical radiotherapy. TOPK disruption may cause tumour-specific radiosensitisation in multiple different tumour types. PMID: 28677687
  14. Determined the crystal structure of PBK, which has two phospho-mimicking mutations T9E and T198E. The structural data indicated that PBK may assemble into an inactive dimer in alkaline conditions. Analytical size-exclusion chromatography and analytical ultracentrifugation confirmed that PBK exists in a conformational transition between dimers and monomers at different pH conditions. PMID: 27262437
  15. PBK/TOPK plays a crucial role in tumour malignant potential through its overexpression and highlight its usefulness as a prognostic factor and potential therapeutic target in gastric cancer. PMID: 27898655
  16. A high PBK expression level was correlated with long overall survival in oral squamous cell carcinoma. PMID: 27347940
  17. findings suggest that PBK/TOPK plays a crucial role in tumor malignant potential through its overexpression in ESCC PMID: 27919968
  18. TOPK silencing sensitizes EGFR-TKI-resistant lung cancer cells to gefitinib and increases gefitinib efficacy in preclinical lung adenocarcinoma xenograft models. PMID: 26745678
  19. Study shows that BUB1beta and PDZ binding kinase are up-regulated in breast cancer tumors and their expression is associated with improved overall survival (OS) in basal-like tumors but worse OS in luminal and untreated patients. PMID: 26897635
  20. Overexpression of Nrf2 inhibited the PBK/TOPK KD-induced decrease in cdc2 and cyclin B expression and cell cycle arrest, and blocked ROS production and apoptosis. PMID: 26503118
  21. The in vitro data have been consistent with a role for PBK/TOPK in facilitating invasion in prostate cancer. PBK could be a prognostic biomarker for prostate cancer that would discriminate aggressive prostate cancer from indolent disease. PMID: 25909225
  22. TOPK was speculated to be one of a potential marker and therapeutic target in advanced prostate cancer PMID: 25881543
  23. Authors identified TOPK/PBK, in vitro and in vivo, as the master ZFP linker kinase. Furthermore, they show precise temporal correlation between TOPK activating phosphorylation by Cdk1 and linker phosphorylation in mitosis. PMID: 25575812
  24. PBK/TOPK expression is closely associated with cervical cancer and cervical intraepithelial neoplasia, which may be served as a useful target for tumor diagnosis and immunotherapy. PMID: 25550851
  25. TOPK, overexpressed in colorectal cancer, enhances the resistance of colorectal cancer cells to anoikis. PMID: 25687885
  26. PDZ-binding kinase/T-LAK cell-originated protein kinase correlates with mutant p53 and affects cell proliferation and viability as well as prognosis in lung adenocarcinoma PMID: 25466965
  27. Study findings suggest that the PBK/TOPK mRNA/protein expression is specific to human bladder cancer and might be used as a novel target for development of cancer immunotherapy and diagnostic biomarker. PMID: 24629784
  28. TOPK protein upregulates iNOS gene expression in T cell leukemia Jurkat cells or macrophage leukemic Raw 264.7 cells via NF-kappaB activation in response to LPS, and might act as a critical effector in LPS/TLR4-mediated signaling cascade. PMID: 24440499
  29. PBK/TOPK expression is positively correlated with Ki67 and p53 expression, and can be used as an independent prognostic factor in non-small-cell lung cancer. PMID: 24025073
  30. These results suggest that the malignant transformation of plexiform neurofibroma is associated with distinct changes in the expression of BUB1B, PBK and NEK2 PMID: 23370767
  31. The 3D structure of TOPK protein has been constructed by using multiple templates. PMID: 22940854
  32. that the serine-threonine kinase PBK/TOPK is frequently overexpressed in high-grade lymphomas and its expression is positively correlated to that of c-Myc and E2F1 PMID: 23237560
  33. TOPK directly interacted with and phosphorylated IkappaBalpha at Ser-32, leading to p65 nuclear translocation and NF-kappaB activation. PMID: 23250755
  34. Our results indicate that overexpression of TOPK could predetermine the metastatic capability of tumors and could serve as a significant prognostic predictor of shortened overall survival and time to recurrence. PMID: 22192142
  35. T-LAK cell-originated protein kinase (TOPK) phosphorylation of MKP1 protein prevents solar ultraviolet light-induced inflammation through inhibition of the p38 protein signaling pathway. PMID: 21715333
  36. Upregulation of TOPK is associated with breast cancer. PMID: 20589935
  37. increased levels of PBK/TOPK may contribute to tumor cell development and progression through suppression of p53 function and consequent reductions in the cell-cycle regulatory proteins such as p21. PMID: 20622899
  38. Phosphorylation of Prx1 (Ser-32) by TOPK prevents UVB-induced apoptosis in RPMI7951 melanoma cells through regulation of Prx1 peroxidase activity and blockade of intracellular H(2)O(2) accumulation. PMID: 20647304
  39. TOPK is indispensable for cancer cell cytokinesis throughout phosphorylation on p97. PMID: 19900192
  40. PBK/TOPK protein could serve as a useful indicator for histopathologic differentiation between cholangiocarcinoma and hepatocellular carcinomas and the low expression of PBK/TOPK is predicative of poor survival in cholangiocarcinoma patients. PMID: 19954816
  41. PBK/TOPK is upregulated in Burkitt's lymphoma and other highly proliferative malignant cells and during normal fetal development. PMID: 11783945
  42. TOPK protein is up-regulated in a variety of hematologic malignancies and may be involved in leukemic cell growth; 4 of 5 clinical that strongly expressed TOPK also strongly expressed phosphorylated c-Myc PMID: 14757441
  43. PBK/TOPK plays an important role in transiently amplifying neural progenitors in the adult subependymal zone of transgenically targeted mice. PMID: 16291951
  44. PBK augments tumor cell growth following transient appearance in different types of progenitor cells in vivo as reported. PMID: 17482142
  45. Findings showed that TOPK positively modulated UVB-induced JNK1 activity and played a pivotal role in JNK1-mediated cell transformation induced by H-Ras. PMID: 17545598
  46. The positive feedback loop between TOPK and ERK2 increases tumorigenesis properties of HCT116 colorectal cancer cells, and TOPK-regulated signaling may serve as a potential therapeutic target in colorectal cancer PMID: 17631144

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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