Skip to content

Study · Animal study (in vivo) · mouse · 1982

7 results

Chemical characterization of thymosin beta 4.

Low TL, Goldstein AL

The Journal of biological chemistry1 Jan 1982Cited by 90 (Europe PMC)

Summary

As part of our ongoing investigations on the endocrine thymus, we have isolated and purified to homogeneity a hormone-like peptide which we have termed thymosin beta 4. Thymosin beta 4 has Mr = 4982 and an isoelectric point of 5.1. The complete amino acid sequence of this polypeptide has been established by automated Edman degradation as well as by manual sequence analysis. Thymosin beta 4 is composed of 43 amino acid residues with acetylserine at the NH2 terminus. This molecule induces expression of terminal deoxynucleotidyl transferase in transferase-negative murine thymocytes in vivo and in vitro. It also exhibits ability to inhibit the migration of macrophages. Comparison of the sequence of thymosin beta 4 to other thymic hormones or other published protein sequences does not reveal any statistically significant relationship. Two helical regions were identified in the structure using data for prediction of protein conformation. It is proposed that thymosin beta 4 is one of the biologically active peptides present in thymosin fractions 5 and 5A which participate in the regulation, differentiation, and function of thymus-derived lymphocytes and may also act directly or indirectly on macrophages and perhaps other cells involved in cell-mediated immunity.
CC BYText from Europe PMC. Highlighted sentences are the source of results.

Results from this study7

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

  1. 01AnimalAnimal study (in vivo)Activity measurement

    Thymosin beta‑4 induced expression of terminal deoxynucleotidyl transferase in transferase-negative murine thymocytes in vivo.

    In plain wordsIn mice, thymosin beta‑4 switched on terminal deoxynucleotidyl transferase in thymus immune cells that had none.

    Outcome
    IncreaseTerminal deoxynucleotidyl transferase expression in thymocytes in vivo
    Study

    mousen: not reported in source

    transferase-negative murine thymocytes
    Outcome group
    Immune response · Immune and inflammation
    Studied dose
    Dose not stated

    Source sentences

    Summary
    induces expression of terminal deoxynucleotidyl transferase in transferase-negative murine thymocytes in vivo
  2. 02LabIn vitro (cells)Activity measurement

    Thymosin beta‑4 induced expression of terminal deoxynucleotidyl transferase in transferase-negative murine thymocytes in vitro.

    In plain wordsIn mouse cells, thymosin beta‑4 switched on terminal deoxynucleotidyl transferase in thymus immune cells that had none.

    Outcome
    IncreaseTerminal deoxynucleotidyl transferase expression in thymocytes in vitro
    Study

    mousen: not reported in source

    transferase-negative murine thymocytes
    Outcome group
    Immune response · Immune and inflammation
    Studied dose
    Dose not stated

    Source sentences

    Summary
    induces expression of terminal deoxynucleotidyl transferase in transferase-negative murine thymocytes in vivo and in vitro.
  3. 03LabOther designActivity measurement

    Thymosin beta‑4 exhibits the ability to inhibit the migration of macrophages.

    In plain wordsIn lab tests, thymosin beta‑4 reduced the movement of macrophages.

    Outcome
    DecreaseInhibition of macrophage migration
    Study

    n: not reported in source

    Outcome group
    Immune response · Immune and inflammation
    Studied dose
    Dose not stated

    Source sentences

    Summary
    It also exhibits ability to inhibit the migration of macrophages.

Studies that did not test the peptide alone4

In this study, Thymosin beta-4 (human) 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 beta-4 (human).

  1. 04LabNot a test of Thymosin beta-4 (human) aloneIn vitro (cell-free)Other

    Thymosin beta‑4 has a molecular mass (Mr) of 4982 and an isoelectric point of 5.1.

    In plain wordsIn lab analysis, thymosin beta‑4 had a mass of 4982 and an isoelectric point of 5.1.

    Outcome
    Not applicableMolecular mass and isoelectric point of thymosin beta 4
    Study

    n: not reported in source

    Outcome group
    Peptide structure and chemistry · Pharmacology

    Measurements

    Mr
    4982
    thymosin beta 4
    isoelectric point
    5.1
    thymosin beta 4

    Source sentences

    Summary
    Thymosin beta 4 has Mr = 4982 and an isoelectric point of 5.1.

    In this study, Thymosin beta-4 (human) 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 beta-4 (human).

  2. 05LabNot a test of Thymosin beta-4 (human) aloneIn vitro (cell-free)Other

    Thymosin beta‑4 is composed of 43 amino acid residues with acetylserine at the NH2 terminus.

    In plain wordsIn lab analysis, thymosin beta‑4 had 43 amino acids and started with acetylserine.

    Outcome
    Not applicableAmino acid composition and NH2 terminus of thymosin beta 4
    Study

    n: not reported in source

    Outcome group
    Peptide structure and chemistry · Pharmacology

    Measurements

    amino acid residues
    43
    thymosin beta 4

    Source sentences

    Summary
    Thymosin beta 4 is composed of 43 amino acid residues with acetylserine at the NH2 terminus.

    In this study, Thymosin beta-4 (human) 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 beta-4 (human).

  3. 06Computer modelNot a test of Thymosin beta-4 (human) aloneIn silicoOther

    Two helical regions were identified in the structure of thymosin beta‑4 using data for prediction of protein conformation.

    In plain wordsIn computer prediction, thymosin beta‑4 had two helical regions.

    Outcome
    Not applicablePredicted helical regions in thymosin beta 4
    Study

    n: not reported in source

    Outcome group
    Peptide structure and chemistry · Pharmacology

    Source sentences

    Summary
    Two helical regions were identified in the structure using data for prediction of protein conformation.

    In this study, Thymosin beta-4 (human) 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 beta-4 (human).

  4. 07Computer modelNot a test of Thymosin beta-4 (human) aloneIn silicoOther

    Comparison of the thymosin beta‑4 sequence to other thymic hormones or other published protein sequences revealed no statistically significant relationship.

    In plain wordsIn computer comparison, the thymosin beta‑4 sequence did not match other thymic hormones or published protein sequences in a meaningful way.

    Outcome
    No significant changeSequence relationship of thymosin beta 4 to other thymic hormones
    Study

    n: not reported in source

    Outcome group
    Peptide structure and chemistry · Pharmacology

    Source sentences

    Summary
    Comparison of the sequence of thymosin beta 4 to other thymic hormones or other published protein sequences does not reveal any statistically significant relationship.

    In this study, Thymosin beta-4 (human) 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 beta-4 (human).

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, 01:52 UTC

    Study results updated

  2. Version 1

    12 Oct 2026, 18:17 UTC

    First added · source update from Europe PMC

Subjects

Terms as the source lists them.

PepBank is a research reference. Talk to a doctor before you use any peptide.