Efficient production and purification of recombinant human interleukin-12 (IL-12) overexpressed in mammalian cells without affinity tag

Jayanthi, Srinivas; Koppolu, Bhanu prasanth; Smith, Sean G.; Jalah, Rashmi; Bear, Jenifer; Rosati, Margherita; Pavlakis, George N.; Felber, Barbara K.; Zaharoff, David A.; Kumar, Thallapuranam Krishnaswamy Suresh

doi:10.1016/j.pep.2014.07.002

Title: Efficient production and purification of recombinant human interleukin-12 (IL-12) overexpressed in mammalian cells without affinity tag

Full Record
Other Related Research

Authors:

Jayanthi, Srinivas;

; Smith, Sean G.; Jalah, Rashmi; Bear, Jenifer; Rosati, Margherita; Pavlakis, George N.; Felber, Barbara K.; Zaharoff, David A.; Kumar, Thallapuranam Krishnaswamy Suresh

Publication Date:: Wed Oct 01 00:00:00 EDT 2014

Sponsoring Org.:: USDOE

OSTI Identifier:: 1222399

Grant/Contract Number:: FG02-01ER15161

Resource Type:: Journal Article: Publisher's Accepted Manuscript

Journal Name:: Protein Expression and Purification

Additional Journal Information:: Journal Name: Protein Expression and Purification Journal Volume: 102 Journal Issue: C; Journal ID: ISSN 1046-5928

Publisher:: Elsevier

Country of Publication:: United States

Language:: English

Citation Formats


                    Jayanthi, Srinivas, Koppolu, Bhanu prasanth, Smith, Sean G., Jalah, Rashmi, Bear, Jenifer, Rosati, Margherita, Pavlakis, George N., Felber, Barbara K., Zaharoff, David A., and Kumar, Thallapuranam Krishnaswamy Suresh. Efficient production and purification of recombinant human interleukin-12 (IL-12) overexpressed in mammalian cells without affinity tag.  United States: N. p., 2014. 
        Web.  doi:10.1016/j.pep.2014.07.002.

Copy to clipboard


                    Jayanthi, Srinivas, Koppolu, Bhanu prasanth, Smith, Sean G., Jalah, Rashmi, Bear, Jenifer, Rosati, Margherita, Pavlakis, George N., Felber, Barbara K., Zaharoff, David A., & Kumar, Thallapuranam Krishnaswamy Suresh. Efficient production and purification of recombinant human interleukin-12 (IL-12) overexpressed in mammalian cells without affinity tag.  United States.  https://doi.org/10.1016/j.pep.2014.07.002

Copy to clipboard


                    Jayanthi, Srinivas, Koppolu, Bhanu prasanth, Smith, Sean G., Jalah, Rashmi, Bear, Jenifer, Rosati, Margherita, Pavlakis, George N., Felber, Barbara K., Zaharoff, David A., and Kumar, Thallapuranam Krishnaswamy Suresh. 2014.  
        "Efficient production and purification of recombinant human interleukin-12 (IL-12) overexpressed in mammalian cells without affinity tag".  United States.  https://doi.org/10.1016/j.pep.2014.07.002.

Copy to clipboard


                    
@article{osti_1222399,

  title        = {Efficient production and purification of recombinant human interleukin-12 (IL-12) overexpressed in mammalian cells without affinity tag},

  author       = {Jayanthi, Srinivas and Koppolu, Bhanu prasanth and Smith, Sean G. and Jalah, Rashmi and Bear, Jenifer and Rosati, Margherita and Pavlakis, George N. and Felber, Barbara K. and Zaharoff, David A. and Kumar, Thallapuranam Krishnaswamy Suresh},

  abstractNote = {},

  doi          = {10.1016/j.pep.2014.07.002},

  url          = {https://www.osti.gov/biblio/1222399},
  journal      = {Protein Expression and Purification},

  issn         = {1046-5928},

  number       = C,

  volume       = 102,

  place        = {United States},

  year         = {Wed Oct 01 00:00:00 EDT 2014},

  month        = {Wed Oct 01 00:00:00 EDT 2014}

}

Copy to clipboard

Journal Article:

Free Publicly Available Full Text

Accepted Manuscript (Publisher)

Publisher's Version of Record at https://doi.org/10.1016/j.pep.2014.07.002

Other availability

Search WorldCat to find libraries that may hold this journal

Citation Metrics:

Cited by: 12 works

Citation information provided by
Web of Science

Save / Share:

Export Metadata

Save to My Library

Similar records in OSTI.GOV collections:

Heparin-binding peptide as a novel affinity tag for purification of recombinant proteins

Journal Article Morris, Jacqueline; Jayanthi, Srinivas; Langston, Rebekah; ... - Protein Expression and Purification

Not provided.
https://doi.org/10.1016/j.pep.2016.05.013
Heparin-binding peptide as a novel affinity tag for purification of recombinant proteins

Journal Article Morris, Jacqueline; Jayanthi, Srinivas; Langston, Rebekah; ... - Protein Expression and Purification
Cited by 14
https://doi.org/10.1016/j.pep.2016.05.013
Characterization of a high affinity interleukin-1 (IL-1) specific binding site in a human synovial sarcoma (Hs431) cell line

Journal Article End, D; Garrabrant, T

A subpopulation of cells was derived from the Hs431 connective tissue sarcoma cell line which possessed high affinity (estimated Kd = 0.38-0.55 nM) binding sites for human recombinant ({sup 125}I)-IL-1 alpha. Binding at 4{degrees}C was slow approaching equilibrium by 4 hrs. Dissociation of ({sup 125}I)-IL-1 alpha was also slow and unaffected by high concentrations of cold ligand. The binding site also underwent ligand-induced internalization at 37{degrees}C. An Mr = 83,000 protein was identified in affinity crosslinking studies. Despite these similarities to previously reported IL-1 receptors, Hs431 cells did not exhibit biological responses to IL-1 which have been observed in othermore »« less
Efficient and versatile one-step affinity purification of in vivo biotinylated proteins: Expression, characterization and structure analysis of recombinant human glutamate carboxypeptidase II

Journal Article Tykvart, J; Sacha, P; Barinka, C; ... - Protein Expression and Purification

Affinity purification is a useful approach for purification of recombinant proteins. Eukaryotic expression systems have become more frequently used at the expense of prokaryotic systems since they afford recombinant eukaryotic proteins with post-translational modifications similar or identical to the native ones. Here, we present a one-step affinity purification set-up suitable for the purification of secreted proteins. The set-up is based on the interaction between biotin and mutated streptavidin. Drosophila Schneider 2 cells are chosen as the expression host, and a biotin acceptor peptide is used as an affinity tag. This tag is biotinylated by Escherichia coli biotin-protein ligase in vivo.more »« less
https://doi.org/10.1016/j.pep.2011.11.016
IL-1 binds to high affinity receptors on human osteosarcoma cells and potentiates prostaglandin E2 stimulation of cAMP production

Journal Article Rodan, S; Wesolowski, G; Chin, J; ... - Journal of Immunology; (USA)

IL-1 is a potent bone resorbing agent. Its mechanism of action is unknown, but the presence of osteoblasts was shown to be necessary for IL-1 stimulation of bone resorption by isolated osteoclasts. This study examines the presence of IL-1R and IL-1 effects in osteoblastic cells from a clonal human osteosarcoma cell line, Saos-2/B-10. We found that the binding affinity and the number of binding sites increases substantially during the postconfluent stage. Scatchard and curve-fitting analysis revealed one class of high affinity binding sites, with Kd/Ki's of 40 +/- 17 pM (mean +/- SD) for IL-1 alpha (n = 5) andmore »« less

Similar Records