Advanced Search
Display options
Filter resources
Text Availability
Article type
Publication date
Species
Language
Sex
Age
Showing 1 to 12 of 236 entries
Sorted by: Best Match Show Resources per page
Retraction: withdrawn: expression of Sapium sebiferum (L.) Roxb stearoyl-acyl carrier protein desaturase in Escherichia coli.

Protein expression and purification

Zhou B, Peng D, Tan X, Yuan D, Liu X, Zhang L.
PMID: 24979737
Protein Expr Purif. 2015 May;109:127. doi: 10.1016/j.pep.2014.05.008. Epub 2014 Jun 27.

This article has been withdrawn at the request of the author(s) and/or editor. The Publisher apologizes for any inconvenience this may cause. The full Elsevier Policy on Article Withdrawal can be found at http://www.elsevier.com/locate/withdrawalpolicy.

Cite
Zhou B, Peng D, Tan X, et al. Retraction: withdrawn: expression of Sapium sebiferum (L.) Roxb stearoyl-acyl carrier protein desaturase in Escherichia coli. Protein Expr Purif. 2014;109:127doi: 10.1016/j.pep.2014.05.008.
Zhou, B., Peng, D., Tan, X., Yuan, D., Liu, X., & Zhang, L. (2015). Retraction: withdrawn: expression of Sapium sebiferum (L.) Roxb stearoyl-acyl carrier protein desaturase in Escherichia coli. Protein expression and purification, 109127. https://doi.org/10.1016/j.pep.2014.05.008
Zhou, Bo, et al. "Retraction: withdrawn: expression of Sapium sebiferum (L.) Roxb stearoyl-acyl carrier protein desaturase in Escherichia coli." Protein expression and purification vol. 109 (2015): 127. doi: https://doi.org/10.1016/j.pep.2014.05.008
Zhou B, Peng D, Tan X, Yuan D, Liu X, Zhang L. Retraction: withdrawn: expression of Sapium sebiferum (L.) Roxb stearoyl-acyl carrier protein desaturase in Escherichia coli. Protein Expr Purif. 2015 May;109:127. doi: 10.1016/j.pep.2014.05.008. Epub 2014 Jun 27. PMID: 24979737.
Copy Download .nbib Format: NLM
Bacterial co-expression of the α and β protomers of human l-asparaginase-3: Achieving essential N-terminal exposure of a catalytically critical threonine located in the β-subunit.

Protein expression and purification

Karamitros CS, Konrad M.
PMID: 24157738
Protein Expr Purif. 2014 Jan;93:1-10. doi: 10.1016/j.pep.2013.10.007. Epub 2013 Oct 22.

l-asparaginases hydrolyze l-asparagine to l-aspartic acid and ammonia. Enzymes of bacterial origin are used as therapeutic agents for the treatment of acute lymphoblastic leukemia. Recently, the structure of a human homolog, hASNase3, which possesses l-asparaginase activity, was solved setting...

Cite
Karamitros CS, Konrad M. Bacterial co-expression of the α and β protomers of human l-asparaginase-3: Achieving essential N-terminal exposure of a catalytically critical threonine located in the β-subunit. Protein Expr Purif. 2013;93:1-10doi: 10.1016/j.pep.2013.10.007.
Karamitros, C. S., & Konrad, M. (2014). Bacterial co-expression of the α and β protomers of human l-asparaginase-3: Achieving essential N-terminal exposure of a catalytically critical threonine located in the β-subunit. Protein expression and purification, 931-10. https://doi.org/10.1016/j.pep.2013.10.007
Karamitros, Christos S, and Konrad, Manfred. "Bacterial co-expression of the α and β protomers of human l-asparaginase-3: Achieving essential N-terminal exposure of a catalytically critical threonine located in the β-subunit." Protein expression and purification vol. 93 (2014): 1-10. doi: https://doi.org/10.1016/j.pep.2013.10.007
Karamitros CS, Konrad M. Bacterial co-expression of the α and β protomers of human l-asparaginase-3: Achieving essential N-terminal exposure of a catalytically critical threonine located in the β-subunit. Protein Expr Purif. 2014 Jan;93:1-10. doi: 10.1016/j.pep.2013.10.007. Epub 2013 Oct 22. PMID: 24157738.
Copy Download .nbib Format: NLM
Reprint of: Tagging for Protein Expression.

Protein expression and purification

Malhotra A.
PMID: 21889988
Protein Expr Purif. 2011 Sep 02; doi: 10.1016/j.pep.2011.08.023. Epub 2011 Sep 02.

Tags are frequently used in the expression of recombinant proteins to improve solubility and for affinity purification. A large number of tags have been developed for protein production and researchers face a profusion of choices when designing expression constructs....

Cite
Malhotra A. Reprint of: Tagging for Protein Expression. Protein Expr Purif. 2011;doi: 10.1016/j.pep.2011.08.023.
Malhotra, A. (2011). Reprint of: Tagging for Protein Expression. Protein expression and purification, . https://doi.org/10.1016/j.pep.2011.08.023
Malhotra, Arun. "Reprint of: Tagging for Protein Expression." Protein expression and purification vol. (2011). doi: https://doi.org/10.1016/j.pep.2011.08.023
Malhotra A. Reprint of: Tagging for Protein Expression. Protein Expr Purif. 2011 Sep 02; doi: 10.1016/j.pep.2011.08.023. Epub 2011 Sep 02. PMID: 21889988.
Copy Download .nbib Format: NLM
Reprint of: Comparison of affinity tags for protein purification.

Protein expression and purification

Lichty JJ, Malecki JL, Agnew HD, Michelson-Horowitz DJ, Tan S.
PMID: 21893203
Protein Expr Purif. 2011 Sep 03; doi: 10.1016/j.pep.2011.08.017. Epub 2011 Sep 03.

Affinity tags are highly efficient tools for purifying proteins from crude extracts. To facilitate the selection of affinity tags for purification projects, we have compared the efficiency of eight elutable affinity tags to purify proteins from Escherichia coli, yeast,...

Cite
Lichty JJ, Malecki JL, Agnew HD, et al. Reprint of: Comparison of affinity tags for protein purification. Protein Expr Purif. 2011;doi: 10.1016/j.pep.2011.08.017.
Lichty, J. J., Malecki, J. L., Agnew, H. D., Michelson-Horowitz, D. J., & Tan, S. (2011). Reprint of: Comparison of affinity tags for protein purification. Protein expression and purification, . https://doi.org/10.1016/j.pep.2011.08.017
Lichty, Jordan J, et al. "Reprint of: Comparison of affinity tags for protein purification." Protein expression and purification vol. (2011). doi: https://doi.org/10.1016/j.pep.2011.08.017
Lichty JJ, Malecki JL, Agnew HD, Michelson-Horowitz DJ, Tan S. Reprint of: Comparison of affinity tags for protein purification. Protein Expr Purif. 2011 Sep 03; doi: 10.1016/j.pep.2011.08.017. Epub 2011 Sep 03. PMID: 21893203.
Copy Download .nbib Format: NLM
Developing a secretory AcGFP1-based IRES expression system for efficient production of mammalian recombinant proteins.

Protein expression and purification

Zou Z, Spencer M, Sun PD.
PMID: 34920134
Protein Expr Purif. 2021 Dec 14;192:106029. doi: 10.1016/j.pep.2021.106029. Epub 2021 Dec 14.

To generate stable cell lines that express high levels of recombinant genes often requires screening of a large number of transfected cells using ELISA. The most widely used alternative to ELISA screening is to use an intracellularly expressed GFP...

Cite
Zou Z, Spencer M, Sun PD. Developing a secretory AcGFP1-based IRES expression system for efficient production of mammalian recombinant proteins. Protein Expr Purif. 2021;192:106029doi: 10.1016/j.pep.2021.106029.
Zou, Z., Spencer, M., & Sun, P. D. (2021). Developing a secretory AcGFP1-based IRES expression system for efficient production of mammalian recombinant proteins. Protein expression and purification, 192106029. https://doi.org/10.1016/j.pep.2021.106029
Zou, Zhongcheng, et al. "Developing a secretory AcGFP1-based IRES expression system for efficient production of mammalian recombinant proteins." Protein expression and purification vol. 192 (2021): 106029. doi: https://doi.org/10.1016/j.pep.2021.106029
Zou Z, Spencer M, Sun PD. Developing a secretory AcGFP1-based IRES expression system for efficient production of mammalian recombinant proteins. Protein Expr Purif. 2021 Dec 14;192:106029. doi: 10.1016/j.pep.2021.106029. Epub 2021 Dec 14. PMID: 34920134.
Copy Download .nbib Format: NLM
Method for efficient soluble expression and purification of recombinant hyperactive Tn5 transposase.

Protein expression and purification

Xu T, Xiao M, Yu L.
PMID: 33716122
Protein Expr Purif. 2021 Jul;183:105866. doi: 10.1016/j.pep.2021.105866. Epub 2021 Mar 11.

Efficient preparation of libraries is the key step of next-generation sequencing (NGS) methods. Tn5 transposase enables simple, robust and highly efficient tagmentation-based library construction. Here, we report a simple and reliable expression and purification strategy based on fusing Tn5...

Cite
Xu T, Xiao M, Yu L. Method for efficient soluble expression and purification of recombinant hyperactive Tn5 transposase. Protein Expr Purif. 2021;183:105866doi: 10.1016/j.pep.2021.105866.
Xu, T., Xiao, M., & Yu, L. (2021). Method for efficient soluble expression and purification of recombinant hyperactive Tn5 transposase. Protein expression and purification, 183105866. https://doi.org/10.1016/j.pep.2021.105866
Xu, Tongtong, et al. "Method for efficient soluble expression and purification of recombinant hyperactive Tn5 transposase." Protein expression and purification vol. 183 (2021): 105866. doi: https://doi.org/10.1016/j.pep.2021.105866
Xu T, Xiao M, Yu L. Method for efficient soluble expression and purification of recombinant hyperactive Tn5 transposase. Protein Expr Purif. 2021 Jul;183:105866. doi: 10.1016/j.pep.2021.105866. Epub 2021 Mar 11. PMID: 33716122.
Copy Download .nbib Format: NLM
Expression in Escherichia coli, purification and kinetic characterization of LAPLm, a Leishmania major M17-aminopeptidase.

Protein expression and purification

Aguado ME, González-Matos M, Izquierdo M, Quintana J, Field MC, González-Bacerio J.
PMID: 33775769
Protein Expr Purif. 2021 Jul;183:105877. doi: 10.1016/j.pep.2021.105877. Epub 2021 Mar 25.

The Leishmania major leucyl-aminopeptidase (LAPLm), a member of the M17 family of proteases, is a potential drug target for treatment of leishmaniasis. To better characterize enzyme properties, recombinant LAPLm (rLAPLm) was expressed in Escherichia coli. A LAPLm gene was...

Cite
Aguado ME, González-Matos M, Izquierdo M, et al. Expression in Escherichia coli, purification and kinetic characterization of LAPLm, a Leishmania major M17-aminopeptidase. Protein Expr Purif. 2021;183:105877doi: 10.1016/j.pep.2021.105877.
Aguado, M. E., González-Matos, M., Izquierdo, M., Quintana, J., Field, M. C., & González-Bacerio, J. (2021). Expression in Escherichia coli, purification and kinetic characterization of LAPLm, a Leishmania major M17-aminopeptidase. Protein expression and purification, 183105877. https://doi.org/10.1016/j.pep.2021.105877
Aguado, Mirtha Elisa, et al. "Expression in Escherichia coli, purification and kinetic characterization of LAPLm, a Leishmania major M17-aminopeptidase." Protein expression and purification vol. 183 (2021): 105877. doi: https://doi.org/10.1016/j.pep.2021.105877
Aguado ME, González-Matos M, Izquierdo M, Quintana J, Field MC, González-Bacerio J. Expression in Escherichia coli, purification and kinetic characterization of LAPLm, a Leishmania major M17-aminopeptidase. Protein Expr Purif. 2021 Jul;183:105877. doi: 10.1016/j.pep.2021.105877. Epub 2021 Mar 25. PMID: 33775769.
Copy Download .nbib Format: NLM
Antibody mimetic drug conjugate manufactured by high-yield Escherichia coli expression and non-covalent binding system.

Protein expression and purification

Yamatsugu K, Katoh H, Yamashita T, Takahashi K, Aki S, Tatsumi T, Kaneko Y, Kawamura T, Miura M, Ishii M, Ohkubo K, Osawa T, Kodama T, Ishikawa S, Kanai M, Sugiyama A.
PMID: 34973460
Protein Expr Purif. 2021 Dec 30;192:106043. doi: 10.1016/j.pep.2021.106043. Epub 2021 Dec 30.

Antibody-drug conjugates (ADCs) are a major therapeutic tool for the treatment of advanced cancer. Malignant cells in advanced cancer often display multiple genetic mutations and become resistant to monotherapy. Therefore, a therapeutic regimen that simultaneously targets multiple molecules with...

Cite
Yamatsugu K, Katoh H, Yamashita T, et al. Antibody mimetic drug conjugate manufactured by high-yield Escherichia coli expression and non-covalent binding system. Protein Expr Purif. 2021;192:106043doi: 10.1016/j.pep.2021.106043.
Yamatsugu, K., Katoh, H., Yamashita, T., Takahashi, K., Aki, S., Tatsumi, T., Kaneko, Y., Kawamura, T., Miura, M., Ishii, M., Ohkubo, K., Osawa, T., Kodama, T., Ishikawa, S., Kanai, M., & Sugiyama, A. (2021). Antibody mimetic drug conjugate manufactured by high-yield Escherichia coli expression and non-covalent binding system. Protein expression and purification, 192106043. https://doi.org/10.1016/j.pep.2021.106043
Yamatsugu, Kenzo, et al. "Antibody mimetic drug conjugate manufactured by high-yield Escherichia coli expression and non-covalent binding system." Protein expression and purification vol. 192 (2021): 106043. doi: https://doi.org/10.1016/j.pep.2021.106043
Yamatsugu K, Katoh H, Yamashita T, Takahashi K, Aki S, Tatsumi T, Kaneko Y, Kawamura T, Miura M, Ishii M, Ohkubo K, Osawa T, Kodama T, Ishikawa S, Kanai M, Sugiyama A. Antibody mimetic drug conjugate manufactured by high-yield Escherichia coli expression and non-covalent binding system. Protein Expr Purif. 2021 Dec 30;192:106043. doi: 10.1016/j.pep.2021.106043. Epub 2021 Dec 30. PMID: 34973460.
Copy Download .nbib Format: NLM
Expression and characterization of a recombinant broadly-reactive monoclonal antibody against group 1 and 2 influenza viruses.

Protein expression and purification

Hu Z, Huang Y, Zhao J, Hu J, Hu S, Liu X.
PMID: 35007721
Protein Expr Purif. 2022 Jan 07;106046. doi: 10.1016/j.pep.2022.106046. Epub 2022 Jan 07.

Production of broadly-reactive antibodies is critical for universal immunodiagnosis of rapidly-evolving influenza viruses. Most monoclonal antibodies (mAbs) are generated in mice using the hybridoma technology which involves labor- and time-consuming screening and low yield issues. In this study, a...

Cite
Hu Z, Huang Y, Zhao J, et al. Expression and characterization of a recombinant broadly-reactive monoclonal antibody against group 1 and 2 influenza viruses. Protein Expr Purif. 2022;106046doi: 10.1016/j.pep.2022.106046.
Hu, Z., Huang, Y., Zhao, J., Hu, J., Hu, S., & Liu, X. (2022). Expression and characterization of a recombinant broadly-reactive monoclonal antibody against group 1 and 2 influenza viruses. Protein expression and purification, 106046. https://doi.org/10.1016/j.pep.2022.106046
Hu, Zenglei, et al. "Expression and characterization of a recombinant broadly-reactive monoclonal antibody against group 1 and 2 influenza viruses." Protein expression and purification vol. (2022): 106046. doi: https://doi.org/10.1016/j.pep.2022.106046
Hu Z, Huang Y, Zhao J, Hu J, Hu S, Liu X. Expression and characterization of a recombinant broadly-reactive monoclonal antibody against group 1 and 2 influenza viruses. Protein Expr Purif. 2022 Jan 07;106046. doi: 10.1016/j.pep.2022.106046. Epub 2022 Jan 07. PMID: 35007721.
Copy Download .nbib Format: NLM
Developing a secretory AcGFP1-based IRES expression system for efficient production of mammalian recombinant proteins.

Protein expression and purification

Zou Z, Spencer M, Sun PD.
PMID: 34920134
Protein Expr Purif. 2022 Apr;192:106029. doi: 10.1016/j.pep.2021.106029. Epub 2021 Dec 14.

To generate stable cell lines that express high levels of recombinant genes often requires screening of a large number of transfected cells using ELISA. The most widely used alternative to ELISA screening is to use an intracellularly expressed GFP...

Cite
Zou Z, Spencer M, Sun PD. Developing a secretory AcGFP1-based IRES expression system for efficient production of mammalian recombinant proteins. Protein Expr Purif. 2021;192:106029doi: 10.1016/j.pep.2021.106029.
Zou, Z., Spencer, M., & Sun, P. D. (2022). Developing a secretory AcGFP1-based IRES expression system for efficient production of mammalian recombinant proteins. Protein expression and purification, 192106029. https://doi.org/10.1016/j.pep.2021.106029
Zou, Zhongcheng, et al. "Developing a secretory AcGFP1-based IRES expression system for efficient production of mammalian recombinant proteins." Protein expression and purification vol. 192 (2022): 106029. doi: https://doi.org/10.1016/j.pep.2021.106029
Zou Z, Spencer M, Sun PD. Developing a secretory AcGFP1-based IRES expression system for efficient production of mammalian recombinant proteins. Protein Expr Purif. 2022 Apr;192:106029. doi: 10.1016/j.pep.2021.106029. Epub 2021 Dec 14. PMID: 34920134.
Copy Download .nbib Format: NLM
MmpL3, the trehalose monomycolate transporter, is stable in solution in several detergents and can be reconstituted into peptidiscs.

Protein expression and purification

Ung KL, Alsarraf H, Kremer L, Blaise M.
PMID: 34767949
Protein Expr Purif. 2021 Nov 09;191:106014. doi: 10.1016/j.pep.2021.106014. Epub 2021 Nov 09.

Mycobacteria possess a complex and waxy cell wall comprising a large panel of glycolipids. Among these, trehalose monomycolate (TMM) represents abundant and crucial components for the elaboration of the mycomembrane. TMM is synthesized in the cytoplasmic compartment and translocated...

Cite
Ung KL, Alsarraf H, Kremer L, et al. MmpL3, the trehalose monomycolate transporter, is stable in solution in several detergents and can be reconstituted into peptidiscs. Protein Expr Purif. 2021;191:106014doi: 10.1016/j.pep.2021.106014.
Ung, K. L., Alsarraf, H., Kremer, L., & Blaise, M. (2021). MmpL3, the trehalose monomycolate transporter, is stable in solution in several detergents and can be reconstituted into peptidiscs. Protein expression and purification, 191106014. https://doi.org/10.1016/j.pep.2021.106014
Ung, Kien Lam, et al. "MmpL3, the trehalose monomycolate transporter, is stable in solution in several detergents and can be reconstituted into peptidiscs." Protein expression and purification vol. 191 (2021): 106014. doi: https://doi.org/10.1016/j.pep.2021.106014
Ung KL, Alsarraf H, Kremer L, Blaise M. MmpL3, the trehalose monomycolate transporter, is stable in solution in several detergents and can be reconstituted into peptidiscs. Protein Expr Purif. 2021 Nov 09;191:106014. doi: 10.1016/j.pep.2021.106014. Epub 2021 Nov 09. PMID: 34767949.
Copy Download .nbib Format: NLM
Optimization strategies for expression and purification of soluble N-terminal domain of human centriolar protein SAS-6 in Escherichia coli.

Protein expression and purification

Maddi ER, Natesh R.
PMID: 33640460
Protein Expr Purif. 2021 Jul;183:105856. doi: 10.1016/j.pep.2021.105856. Epub 2021 Feb 25.

Spindle assembly abnormal protein 6 (SAS-6), a highly conserved centriolar protein, constitutes the center of the cartwheel assembly that scaffolds centrioles early in their biogenesis. Abnormalities in cartwheel assembly lead to chromosomal dysfunctions. The molecular structure of human SAS-6...

Cite
Maddi ER, Natesh R. Optimization strategies for expression and purification of soluble N-terminal domain of human centriolar protein SAS-6 in Escherichia coli. Protein Expr Purif. 2021;183:105856doi: 10.1016/j.pep.2021.105856.
Maddi, E. R., & Natesh, R. (2021). Optimization strategies for expression and purification of soluble N-terminal domain of human centriolar protein SAS-6 in Escherichia coli. Protein expression and purification, 183105856. https://doi.org/10.1016/j.pep.2021.105856
Maddi, Eswar Reddy, and Natesh, Ramanathan. "Optimization strategies for expression and purification of soluble N-terminal domain of human centriolar protein SAS-6 in Escherichia coli." Protein expression and purification vol. 183 (2021): 105856. doi: https://doi.org/10.1016/j.pep.2021.105856
Maddi ER, Natesh R. Optimization strategies for expression and purification of soluble N-terminal domain of human centriolar protein SAS-6 in Escherichia coli. Protein Expr Purif. 2021 Jul;183:105856. doi: 10.1016/j.pep.2021.105856. Epub 2021 Feb 25. PMID: 33640460.
Copy Download .nbib Format: NLM
Showing 1 to 12 of 236 entries