The development of human recombinant protein, GAPtin, for diabetes

Abstract Background: Oral squamous cell carcinoma (OSCC) is a common malignant tumor of the head and neck, accounting for more than 90% of oral and maxillofacial malignancies. Therefore, it is of great importance to explore the key factors regulating OSCC. Notum belongs to the α/β hydrolase family and is a deacylated extracellular protein that regulates Wnt and other signaling pathways. Studies have found that Notum participates in the progression of colorectal cancer and hepatocellular carcinoma and targeting Notum can regulate the occurrence of cancer. However, the relationship between Notum and OSCC is currently unclear. This study aims to explore the role of Notum in regulating OSCC and its specific mechanism. Methods: Nine OSCC tissue sections were selected for hematoxylin and eosin staining and immunohistochemistry for PCNA and Notum. Bioinformatics analysis was used to explore the correlation between OSCC and Notum expression. CCK8, Western blot, RT-PCR, scratch experiment, transwell, clone formation, flow cytometry, cellular immunofluorescence and in vivo nude mouse tumor formation methods were applied to OSCC cells treated with Notum human recombinant protein, a Notum overexpression plasmid, and a Notum small interfering RNA to explore the mechanism of Notum in regulating OSCC. Results: The results of immunohistochemistry and bioinformatics analysis showed that Notum was highly expressed in OSCC tissues. Notum human recombinant protein promoted the proliferation and migration of Cal-27 and SCC-15 cells; overexpression of Notum promoted the proliferation and migration of Cal-27 and SCC-15 cells; si-Notum can significantly inhibit proliferation and migration of Cal-27 and SCC-15 cells and promote their apoptosis. Western blot and RT-PCR results showed that si-Notum can inhibit the Hedgehog signaling pathway. In addition, Notum human recombinant protein can increase the phosphorylation level of GSK3β and promote the expression of β-catenin, thereby further regulating the biological behavior of OSCC.Conclusions: Notum regulates the proliferation and migration of OSCC through Shh/p-GSK3β/β-catenin signaling pathway. Notum maybe an effective targets for the treatment of OSCC.

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Human recombinant protein C for severe sepsis and septic shock in adult and paediatric patients

Cochrane Database of Systematic Reviews ◽

10.1002/14651858.cd004388.pub6 ◽

2012 ◽

Cited By ~ 12

Author(s):

Arturo J Martí-Carvajal ◽

Ivan Solà ◽

Christian Gluud ◽

Dimitrios Lathyris ◽

Vidhu Anand

Keyword(s):

Septic Shock ◽

Severe Sepsis ◽

Recombinant Protein ◽

Protein C ◽

Paediatric Patients ◽

Sepsis And Septic Shock ◽

Human Recombinant Protein

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Recombinant human PRAME immunization reducesPRAME-expressing tumor growth in mice

Russian Journal of Biotherapy ◽

10.17650/1726-9784-2018-17-3-36-42 ◽

2018 ◽

Vol 17 (3) ◽

pp. 36-42

Author(s):

Yu. P. Finashutina ◽

N. A. Lyzhko ◽

N. N. Kasatkina ◽

L. A. Kesaeva ◽

V. V. Tikhonova ◽

...

Keyword(s):

Recombinant Protein ◽

Tumor Volume ◽

High Titer ◽

Mouse Melanoma ◽

B16f10 Cells ◽

Gene Coding ◽

Melanoma B16f10 ◽

Tumor Types ◽

Human Recombinant Protein ◽

Immunization Series

Intrоduction.Human antigen PRAME is preferentially expressed in a number of different tumor types and may be a potent target for anti-tumor immunotherapy.Purpose.To study anti-tumor action of immunogenic mix recombinant PRAME protein and adjuvant in mice with innate immunity.Materials and methods.C57BL/6 female mice were used for immunization with purified human recombinant protein PRAME. Human PRAME gene coding sequence was cloned in mammalian expressing vector pCEP4 and resulting plasmid was introduced in mouse melanoma B16F10 cells by transfection followed by RQ-PCR, Western blot and flow-cytometry analysis. Then stably PRAME-transfected melanoma cells were injected in mice.Results.The mouse melanoma B16F10 cells stably expressing human PRAME protein were obtained. We demonstrate the 10-fold decreased tumor volume in mice with melanoma B16F10 expressing human PRAME after preventive immunization series with recombinant PRAME protein. The tumor volume reducing was correlated with high titer (6.14 × 10 5) of anti-PRAME antibodies in mice sera.Conclusion.These data indicate that recombinant protein PRAME is immunogenic and may be a potent antigen for immunotherapuetics studies.

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Faculty Opinions recommendation of Human recombinant protein C for severe sepsis and septic shock in adult and paediatric patients.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.717969391.793470375 ◽

2013 ◽

Author(s):

Jonathan Sevransky

Keyword(s):

Septic Shock ◽

Severe Sepsis ◽

Recombinant Protein ◽

Protein C ◽

Paediatric Patients ◽

Sepsis And Septic Shock ◽

Human Recombinant Protein

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Purification and functional analysis of the recombinant protein isolated from E. coli by employing three different methods of bacterial lysis

Journal of the Serbian Chemical Society ◽

10.2298/jsc0507943m ◽

2005 ◽

Vol 70 (7) ◽

pp. 943-950

Author(s):

Marija Mojsin ◽

Gordana Nikcevic ◽

Natasa Kovacevic-Grujicic ◽

Tijana Savic ◽

Isidora Petrovic ◽

...

Keyword(s):

Functional Analysis ◽

Recombinant Protein ◽

Protein Purification ◽

Binding Affinity ◽

Fusion System ◽

E Coli ◽

Freeze Thaw ◽

Bacterial Lysis ◽

Dna Binding Affinity ◽

Human Recombinant Protein

In this paper, the purification of the human recombinant protein expressed in E. coli using the GSTGene Fusion System, by applying various methods of bacterial lysis: sonication, freeze/thaw and beadbeating, is presented. The study was an attempt to compare the properties of the proteins obtained by the sonication method, recommended by manufacturers but inaccessible for many researchers, with those obtained using two other readily available lysis methods. The data show that all purified proteins were soluble and intact with the highest protein yield being obtained via the freeze/thaw method. The results of functional analysis indicate that the proteins purified using the sonication and freeze/thaw methods of lysis exhibited similar DNA binding affinity, while the protein purified by beadbeating was also functional but with a lower binding affinity. The conclusion of this study is that all three lysis methods could be successfully employed for protein purification.

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