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Study · Not a test of the peptide alone · 2000

2 results

Purification of recombinant thymosin alpha 1 in Escherichia coli and its activity

Shi Jihong, Zhang Yingqi, Zhao Ning, Zhao Yongtong, Yan Zhen, Han Wei

Sheng wu gong cheng xue bao = Chinese journal of biotechnology1 Jan 2000

PepBankPUB-98930133
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Summary

The text of this summary is not shown here, because the article license does not allow reuse.

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 E. coli TOP10, a thymosin alpha1 fusion protein of about 38 kD made up 40% of the total bacterial proteins after IPTG induction.

    In plain wordsIn lab-grown bacteria, a thymosin alpha1 fusion protein made up 40% of the bacterial protein.

    Outcome
    Not applicableFusion protein share of bacterial protein
    Study

    n: not reported in source

    E. coli TOP10 expression system
    Outcome group
    Synthesis and manufacturing · Pharmacology

    Measurements

    Fusion protein share
    40 % of total bacterial proteins
    E. coli TOP10

    Source sentences

    Summary
    SDS-PAGE analysis showed an induced expression products band which consititued 40% of the total bacterial proteins.
    1 context sentence
    Summary · context
    After transforming into TOP10, Higher levels of expression of fusion protein, with a molecular weight of about 38kD, was induced at 37deg C by 1 mmol/L IPTG of 4 hours.

    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

    After CNBr cleavage and ion exchange purification, HPLC showed that the purity of thymosin alpha1 was 98%.

    In plain wordsIn the lab, purified recombinant thymosin alpha1 reached 98% purity.

    Outcome
    Not applicablePurity of thymosin alpha1 after cleavage and purification
    Study

    n: not reported in source

    E. coli TOP10 expression system
    Outcome group
    Synthesis and manufacturing · Pharmacology

    Measurements

    Purity
    98%
    HPLC

    Source sentences

    Summary
    HPLC showed the purity of thymosin alpha1 was 98%.
    1 context sentence
    Summary · context
    After CNBr cleavage of the fusion protein in 70% formic acid, thymosin alpha1 was obtained by the ion exchange methods of SP-Sepharose Fast Flow and Q-Sepharose Fast Flow and proved by 2L-Tricine-SDS-PAGE analysis.

    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

    12 Oct 2026, 17:28 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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