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Construction, expression and functional characterization of an engineered antibody against tumor antigen MUC-1C

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Construction, expression and functional characterization of an engineered antibody against tumor antigen MUC-1C. / Pourjafar, Mona; Miehe, Michaela; Najafi, Rezvan et al.

In: Protein Expression and Purification, Vol. 199, 106148, 11.2022.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

Harvard

Pourjafar, M, Miehe, M, Najafi, R, Soleimani, M & Spillner, E 2022, 'Construction, expression and functional characterization of an engineered antibody against tumor antigen MUC-1C', Protein Expression and Purification, vol. 199, 106148. https://doi.org/10.1016/j.pep.2022.106148

APA

Pourjafar, M., Miehe, M., Najafi, R., Soleimani, M., & Spillner, E. (2022). Construction, expression and functional characterization of an engineered antibody against tumor antigen MUC-1C. Protein Expression and Purification, 199, [106148]. https://doi.org/10.1016/j.pep.2022.106148

CBE

Pourjafar M, Miehe M, Najafi R, Soleimani M, Spillner E. 2022. Construction, expression and functional characterization of an engineered antibody against tumor antigen MUC-1C. Protein Expression and Purification. 199:Article 106148. https://doi.org/10.1016/j.pep.2022.106148

MLA

Pourjafar, Mona et al. "Construction, expression and functional characterization of an engineered antibody against tumor antigen MUC-1C". Protein Expression and Purification. 2022. 199. https://doi.org/10.1016/j.pep.2022.106148

Vancouver

Pourjafar M, Miehe M, Najafi R, Soleimani M, Spillner E. Construction, expression and functional characterization of an engineered antibody against tumor antigen MUC-1C. Protein Expression and Purification. 2022 Nov;199:106148. doi: 10.1016/j.pep.2022.106148

Author

Pourjafar, Mona ; Miehe, Michaela ; Najafi, Rezvan et al. / Construction, expression and functional characterization of an engineered antibody against tumor antigen MUC-1C. In: Protein Expression and Purification. 2022 ; Vol. 199.

Bibtex

@article{07ca2c690c0c4a71a14fd9bd71ca5cd6,
title = "Construction, expression and functional characterization of an engineered antibody against tumor antigen MUC-1C",
abstract = "Minibodies (single-chain Fv-CH3) are fusion proteins of a single-chain variable fragment (scFv) to the human IgG1 CH3 domain. They exhibit superior properties as compared to whole antibodies due to their smaller size and less complex composition, and also as compared to scFvs due to the two antigen-binding domains, for immunotherapy and imaging of various carcinomas including breast cancer. In the current study, efficient production of the recombinant anti-MUC-1 minibody for its dominant format (VH-VL) was obtained in the periplasmic space of the Escherichia coli BL21 (DE3) expression system. The active recombinant protein was successfully purified from soluble fraction. Functional assays presented the in vitro targeting properties and specificity of the expressed anti-MUC-1 HL minibody in the MUC-1 positive cell lines compared to normal cell.",
keywords = "Breast cancer, Engineered antibody, Mammalian expression, Minibody, Mucin-1, Periplasmic expression",
author = "Mona Pourjafar and Michaela Miehe and Rezvan Najafi and Meysam Soleimani and Edzard Spillner",
note = "Publisher Copyright: {\textcopyright} 2022",
year = "2022",
month = nov,
doi = "10.1016/j.pep.2022.106148",
language = "English",
volume = "199",
journal = "Protein Expression and Purification",
issn = "1046-5928",
publisher = "Academic Press",

}

RIS

TY - JOUR

T1 - Construction, expression and functional characterization of an engineered antibody against tumor antigen MUC-1C

AU - Pourjafar, Mona

AU - Miehe, Michaela

AU - Najafi, Rezvan

AU - Soleimani, Meysam

AU - Spillner, Edzard

N1 - Publisher Copyright: © 2022

PY - 2022/11

Y1 - 2022/11

N2 - Minibodies (single-chain Fv-CH3) are fusion proteins of a single-chain variable fragment (scFv) to the human IgG1 CH3 domain. They exhibit superior properties as compared to whole antibodies due to their smaller size and less complex composition, and also as compared to scFvs due to the two antigen-binding domains, for immunotherapy and imaging of various carcinomas including breast cancer. In the current study, efficient production of the recombinant anti-MUC-1 minibody for its dominant format (VH-VL) was obtained in the periplasmic space of the Escherichia coli BL21 (DE3) expression system. The active recombinant protein was successfully purified from soluble fraction. Functional assays presented the in vitro targeting properties and specificity of the expressed anti-MUC-1 HL minibody in the MUC-1 positive cell lines compared to normal cell.

AB - Minibodies (single-chain Fv-CH3) are fusion proteins of a single-chain variable fragment (scFv) to the human IgG1 CH3 domain. They exhibit superior properties as compared to whole antibodies due to their smaller size and less complex composition, and also as compared to scFvs due to the two antigen-binding domains, for immunotherapy and imaging of various carcinomas including breast cancer. In the current study, efficient production of the recombinant anti-MUC-1 minibody for its dominant format (VH-VL) was obtained in the periplasmic space of the Escherichia coli BL21 (DE3) expression system. The active recombinant protein was successfully purified from soluble fraction. Functional assays presented the in vitro targeting properties and specificity of the expressed anti-MUC-1 HL minibody in the MUC-1 positive cell lines compared to normal cell.

KW - Breast cancer

KW - Engineered antibody

KW - Mammalian expression

KW - Minibody

KW - Mucin-1

KW - Periplasmic expression

U2 - 10.1016/j.pep.2022.106148

DO - 10.1016/j.pep.2022.106148

M3 - Journal article

C2 - 35940518

AN - SCOPUS:85135701459

VL - 199

JO - Protein Expression and Purification

JF - Protein Expression and Purification

SN - 1046-5928

M1 - 106148

ER -