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Study · In vitro (cells) · 2023

2 results

Recombinant expression of IGF-1 and LR3 IGF-1 fused with xylanase in Pichia pastoris.

Lu Z, Liu N, Huang H, Wang Y, Tu T, Qin X, Wang X, Zhang J, Su X, Tian J, Bai Y, Luo H, Yao B, Zhang H

Applied microbiology and biotechnology1 Jun 2023Cited by 3 (Europe PMC)

PMID37261455 (opens in a new tab)DOI10.1007/s00253-023-12606-0 (opens in a new tab)PepBankPUB-37261455
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 study2

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

  1. 01LabIn vitro (cells)Activity measurement

    In cell proliferation tests, purified LR3 IGF-1 made in Pichia pastoris showed bioactivity comparable to standard IGF-1.

    In plain wordsIn lab tests, LR3 IGF-1 made in yeast stimulated cell growth about as well as standard IGF-1.

    Peptide
    IGF-1 LR3
    Outcome
    No significant changeCell proliferation bioactivity of purified LR3 IGF-1
    Study

    n: not reported in source

    Pichia pastoris expression system
    Comparator
    Standard IGF-1
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    purified IGF-1 and LR3 IGF-1 display excellent bioactivity of cell proliferation compared to the standard IGF-1.
    2 context sentences
    Summary · context
    Purified IGF-1 and LR3 IGF-1 show bioactivity comparable to the standard IGF-1. • High heterologous expression of IGF-1 and LR3 IGF-1 is achieved by fermentation in a bioreactor.
    Summary · context
    Here, we report that human IGF-1 and its analog Long R3 IGF-1 (LR3 IGF-1) are recombinant expressed and produced in the Pichia pastoris (P. pastoris) expression system through being fused with highly expressed xylanase XynCDBFV.

Studies that did not test the peptide alone1

In this study, IGF-1 LR3 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 IGF-1 LR3.

  1. 02LabNot a test of IGF-1 LR3 aloneIn vitro (cells)Other

    In a 15-L bioreactor, fermentation of Pichia pastoris reached about 1 g/L of the XynCDBFV-TEV-LR3 IGF-1 fusion protein.

    In plain wordsIn a 15-L bioreactor, yeast produced about 1 g/L of a fusion protein that contains LR3 IGF-1.

    Peptide
    IGF-1 LR3
    Outcome
    Not applicableExpression level of XynCDBFV-TEV-LR3 IGF-1 fusion protein
    Study

    n: not reported in source

    Pichia pastoris expression system
    Outcome group
    Synthesis and manufacturing · Pharmacology

    Measurements

    Expression level
    ≈ 1 g/L
    XynCDBFV-TEV-LR3 IGF-1, 15-L bioreactor

    Source sentences

    Summary
    reaching up to about 0.5 g/L XynCDBFV-IGF-1 and 1 g/L XynCDBFV-TEV-LR3 IGF-1.
    1 context sentence
    Summary · context
    Here, we report that human IGF-1 and its analog Long R3 IGF-1 (LR3 IGF-1) are recombinant expressed and produced in the Pichia pastoris (P. pastoris) expression system through being fused with highly expressed xylanase XynCDBFV.

    In this study, IGF-1 LR3 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 IGF-1 LR3.

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.

Publication types

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