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Study · Not a test of the peptide alone · 2005

2 results

Overexpression of soluble human thymosin alpha 1 in Escherichia coli.

Chen PF, Zhang HY, Fu GF, Xu GX, Hou YY

Acta biochimica et biophysica Sinica1 Feb 2005Cited by 11 (Europe PMC)

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 study2

No result from this study comes from a test of the peptide.

Studies that did not test the peptide alone2

In this study, Thymosin alpha-1 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 Thymosin alpha-1.

  1. 01LabNot a test of Thymosin alpha-1 aloneOther designOther

    In the E. coli BL21/pET-28a system, soluble fusion protein with thymosin alpha‑1 reached up to 70% of total expressed bacterial proteins.

    In plain wordsIn lab tests, bacteria made thymosin alpha‑1 fusion protein in soluble form at up to 70% of their expressed protein.

    Outcome
    Not applicableSoluble fusion protein expression level
    Study

    n: not reported in source

    E. coli expression system
    Outcome group
    Analytical methods and detection · Pharmacology

    Measurements

    Expression level
    ≤ 70 % of total expressed protein
    BL21/pET-28a

    Source sentences

    Summary
    Among the five expression systems, the BL21/pET-28a system provides the highest expression level of fusion protein in a soluble form, which is up to 70% of total expressed bacterial proteins as visualized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE).

    In this study, Thymosin alpha-1 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 Thymosin alpha-1.

  2. 02LabNot a test of Thymosin alpha-1 aloneOther designOther

    The purified fusion protein reached 94.5% purity by SDS-PAGE and made up 2.53% of the wet bacterial pellet weight.

    In plain wordsIn lab tests, the purified thymosin alpha‑1 fusion protein was 94.5% pure.

    Outcome
    Not applicablePurity and yield of purified fusion protein
    Study

    n: not reported in source

    E. coli expression system
    Outcome group
    Analytical methods and detection · Pharmacology

    Measurements

    Purity
    94.5%
    SDS-PAGE
    Yield
    2.53 % of wet pellet weight
    nickel affinity chromatography

    Source sentences

    Summary
    The resulting fusion protein purified through nickel affinity chromatography accounts for 2.53% of the wet bacterial pellet weight and reaches 94.5% purity by SDS-PAGE.

    In this study, Thymosin alpha-1 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 Thymosin alpha-1.

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 3Current

    10 Oct 2026, 08:55 UTC

    Study results updated

  2. Version 2

    9 Oct 2026, 03:03 UTC

    Study data updated · source update from Europe PMC

  3. Version 1

    9 Oct 2026, 03:02 UTC

    First added · source update from Europe PMC

Subjects

Terms as the source lists them.

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