Generation and Characterization of Human Interferon-beta Neutralizing Humanized Antibody

2020 ◽  
Vol 46 (5) ◽  
pp. 778-786
Author(s):  
V. S. Rybchenko ◽  
A. A. Panina ◽  
N. V. Novoseletsky ◽  
D. S. Balabashin ◽  
S. A. Yakimov ◽  
...  
Keyword(s):  
Interferon Beta ◽  
Human Interferon ◽  
Humanized Antibody

Human interferon beta, nimustine hydrochloride, and radiation therapy in the treatment of newly diagnosed malignant astrocytomas

2005 ◽  
Vol 72 (1) ◽  
pp. 57-62 ◽  
Author(s):  
Takao Watanabe ◽  
Yoichi Katayama ◽  
Atsuo Yoshino ◽  
Chikashi Fukaya ◽  
Takamitsu Yamamoto
Keyword(s):  
Radiation Therapy ◽  
Interferon Beta ◽  
Human Interferon ◽  
Newly Diagnosed ◽  
Malignant Astrocytomas ◽  
Nimustine Hydrochloride

scholarly journals Antibiotic-free expression system for the production of human interferon-beta protein

3 Biotech ◽  
2017 ◽  
Vol 8 (1) ◽  
Author(s):  
Dharam Pal ◽  
Rajan K. Tripathy ◽  
Madaka Surya Teja ◽  
Mukesh Kumar ◽  
Uttam Chand Banerjee ◽  
...  
Keyword(s):  
Interferon Beta ◽  
Expression System ◽  
Free Expression ◽  
Human Interferon

Inducible expression of the human interferon beta 1 gene linked to a bovine papilloma virus DNA vector and maintained extrachromosomally in mouse cells

1983 ◽  
Vol 3 (2) ◽  
pp. 233-240
Author(s):  
S Mitrani-Rosenbaum ◽  
L Maroteaux ◽  
Y Mory ◽  
M Revel ◽  
P M Howley
Keyword(s):  
Dna Sequences ◽  
Interferon Beta ◽  
Inducible Expression ◽  
Human Interferon ◽  
Regulatory Sequences ◽  
Hindiii Site ◽  
Papilloma Virus ◽  
Mouse Cells ◽  
Hybrid Dna ◽  
Bovine Papilloma Virus

A 1.6-kilobase DNA segment of the genomic human interferon beta 1 (IF-beta 1) gene was inserted into each of two possible orientations at the single HindIII site of a recombinant plasmid pBPV69T, consisting of the 69% transforming region of the bovine papilloma virus type 1 (BPV-1) and a modified SalI-SalI fragment of plasmid pBR322. After cleavage of the pBR322 sequences from this recombinant, BPV69T-IF-beta 1 hybrid DNAs were transfected onto C127 mouse cells by the standard calcium precipitation technique. Mouse cells transformed by this hybrid DNA produced low levels of human IF-beta 1 constitutively and responded to induction with either inactivated Newcastle disease virus or polyriboinosinic acid-polyribocytidylic acid. The BPV69T-IF-beta 1 hybrid DNA was nonintegrated in the transformed mouse cells but had acquired DNA sequences as a result of the transfection. Accurate transcripts of the IF-beta 1 mRNA were detected in cells only after induction. When the IF-beta 1 gene was oriented in the plasmid in the same direction of transcription as the BPV-1 genome, transcription was promoted from within the BPV-1 sequences. These results indicate that the regulatory sequences responsible for the inducible expression of the human IF-beta 1 gene are present in the 1.6-kilobase genomic segment and that these sequences can function in a free extrachromosomal state linked to BPV-1 sequences.

scholarly journals Constitutive long-term production and characterization of recombinant human interferon-gammas from two different mammalian cells.

1988 ◽  
Vol 13 (2) ◽  
pp. 143-159 ◽  
Author(s):  
Emiko Sano ◽  
Kiyoshi Okano ◽  
Ritsuko Sawada ◽  
Masanobu Naruto ◽  
Tetsuo Sudo ◽  
...  
Keyword(s):  
Mammalian Cells ◽  
Human Interferon

scholarly journals Optimization of Expression Condition, Two Dimensional And Melting Point-Based Characterization of Recombinant Human Interferon Alpha-2a Fusion and Non Fusion Forms

2018 ◽  
Vol 22 (2) ◽  
pp. 57
Author(s):  
Ratih Asmana Ningrum ◽  
Widdya Kusuma Wardhani ◽  
Ike Wahyuni ◽  
Apon Zaenal Mustopa
Keyword(s):  
Interferon Alpha ◽  
Protein Characterization ◽  
Protein Yield ◽  
Size Exclusion ◽  
Human Interferon ◽  
Two Dimensional ◽  
Cancer Treatments ◽  
Sds Page ◽  
Bca Assay

     Recombinant Human Interferon Alpha-2a (rhIFNα-2a) is a therapeutic protein that used in hepatitis and cancer treatments. In our previous research, we developed higher molecular weight of the protein through human serum albumin fusion. The fusion and non fusion form of rhIFNα-2a were produced in Pichia pastoriswith 86 kDa and 19 kDa in size respectively. In previous research, protein yield was not reproducible due to unoptimized expression conditions. This reseach was aimed to optimize expression condition process and to characterize the fusion and non fusion forms of rhIFNα-2a. The parameters to observe in overproduction include nutrient (media and methanol concentration) and non nutrient (temperature andincubation period). Affinity and size exclusion cromatographicwere compared in protein purification. BCA assay was used to determine quantity of protein. Protein characterization was conducted using two-dimensional SDS PAGE and denaturation analyses. The optimal condition of expression was achieved using complex media with 1% of methanol for 3 day incubation period at 25°C. The protein yield was reproducible and higher comparing to previous research. Affinity chromatography resulted in higher purity of the proteins comparing to size exclusions. Characterization using two dimensional gel analysis revealed that isoelectric point of rhIFNα-2a is 6.5 for fusion form and 6.0 for non fusion form. The melting points of fusion protein were 56°C and 62°C whilst that of non fusion was 56°C.

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