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Study · In vitro (cells) · mouse · 2015

5 results

Examination of alternate codon bias solutions for expression and purification of recombinant mechano-growth factor in Escherichia coli.

Feng J, Wan R, Yi Q, He L, Yang L, Tang L

Biotechnology and applied biochemistry6 Aug 2015Cited by 5 (Europe PMC)

PMID25345350 (opens in a new tab)DOI10.1002/bab.1312 (opens in a new tab)PepBankPUB-25345350
Publisher pagePubMedAsk about this study
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Summary

The text of this summary is not shown here, because the article license does not allow reuse. Read it at the source (opens in a new tab)

Text rights: Publisher copyright. Results still quote short attributed sentences.

Results from this study5

1 result from studies that gave the peptide. No result from this study comes from people.

  1. 01LabIn vitro (cells)Activity measurement

    In mouse C2C12 cells, purified recombinant human MGF promoted cell proliferation significantly.

    In plain wordsIn mouse muscle cells in the lab, purified recombinant MGF made the cells multiply significantly.

    Peptide
    MGF / PEG-MGF
    Outcome
    IncreaseC2C12 cell proliferation with purified rhMGF
    Study

    mousen: not reported in source

    C2C12 cell line
    Outcome group
    Muscle injury and repair · Musculoskeletal
    Studied dose
    Dose not stated

    Source sentences

    Summary
    We test the biological activity of MGF protein purified by affinity chromatography in C2C12 cell line and find that rhMGF promotes cell proliferation significantly.

Studies that did not test the peptide alone4

In this study, MGF / PEG-MGF was a lab tool or a carrier, part of a mix, or the subject of a lab method. These results are not evidence about taking MGF / PEG-MGF.

  1. 02LabNot a test of MGF / PEG-MGF aloneOther designOther

    The native human MGF gene gave recombinant human MGF protein in Rosetta (DE3) E. coli but not in BL21 (DE3).

    In plain wordsIn lab bacteria, the natural MGF gene made MGF protein in one E. coli strain but not in another.

    Peptide
    MGF / PEG-MGF
    Outcome
    Not applicablerhMGF expression with native gene in Rosetta (DE3) versus BL21 (DE3)
    Study

    n: not reported in source

    Outcome group
    Synthesis and manufacturing · Pharmacology

    Source sentences

    Summary
    In this study, the human MGF gene is cloned into pGEX-4T-1 and the recombinant human MGF (rhMGF) protein could be expressed in Rosetta (DE3) by isopropyl β-D-1-thiogalactopyranoside induction but not in BL21 (DE3).

    In this study, MGF / PEG-MGF was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking MGF / PEG-MGF.

  2. 03LabNot a test of MGF / PEG-MGF aloneOther designOther

    BL21 (DE3) cells with the MGF(Mut54-56) or MGF(Mut-total) construct could be induced to express recombinant human MGF protein.

    In plain wordsIn lab bacteria, changing rare codons let the E. coli strain BL21 make MGF protein.

    Peptide
    MGF / PEG-MGF
    Outcome
    Not applicablerhMGF expression from codon-mutated genes in BL21 (DE3)
    Study

    n: not reported in source

    Outcome group
    Synthesis and manufacturing · Pharmacology

    Source sentences

    Summary
    Both pGEX-4T-1/MGF(Mut54-56)- and pGEX-4T-1/MGF(Mut-total)-transformed BL21 (DE3) can be induced to express rhMGF protein.

    In this study, MGF / PEG-MGF was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking MGF / PEG-MGF.

  3. 04LabNot a test of MGF / PEG-MGF aloneOther designOther

    Recombinant human MGF expression in BL21 (DE3) was significantly higher than in Rosetta (DE3).

    In plain wordsIn lab bacteria, the BL21 strain made significantly more MGF protein than the Rosetta strain.

    Peptide
    MGF / PEG-MGF
    Outcome
    IncreaserhMGF expression in BL21 (DE3) versus Rosetta (DE3)
    Study

    n: not reported in source

    Comparator
    Rosetta (DE3)
    Outcome group
    Synthesis and manufacturing · Pharmacology

    Source sentences

    Summary
    Results indicate that rhMGF expression in BL21 (DE3) is significantly higher than that in Rosetta (DE3).

    In this study, MGF / PEG-MGF was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking MGF / PEG-MGF.

  4. 05LabNot a test of MGF / PEG-MGF aloneOther designOther

    The protein yield of pGEX-4T-1/MGF(Mut-total) in BL21 (DE3) was higher than that of pGEX-4T-1/MGF(Mut54-56).

    In plain wordsIn lab bacteria, the fully mutated MGF construct gave a higher protein yield than the partly mutated one.

    Peptide
    MGF / PEG-MGF
    Outcome
    IncreaseProtein yield of Mut-total versus Mut54-56 construct in BL21 (DE3)
    Study

    n: not reported in source

    Comparator
    pGEX-4T-1/MGF(Mut54-56)
    Outcome group
    Synthesis and manufacturing · Pharmacology

    Source sentences

    Summary
    The protein yield of pGEX-4T-1/MGF(Mut-total) in BL21 (DE3) is higher than that of pGEX-4T-1/MGF(Mut54-56).

    In this study, MGF / PEG-MGF was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking MGF / PEG-MGF.

AI wrote and checked these results. AI can make mistakes, so check important results against the source.

Version history

PepBank keeps every version of the data on this study. Status changes from Retraction Watch, Europe PMC and Crossref are listed with their source.

  1. Version 2Current

    13 Oct 2026, 21:44 UTC

    Study results updated

  2. Version 1

    13 Oct 2026, 16:31 UTC

    First added · source update from Europe PMC

Subjects

Terms as the source lists them.

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