Thymosin beta 4

Thymosin beta 4 is a peptide, indexed here under Tissue repair peptides.

Identity

Measured identity values, each with the source that reports it
FieldValue
ClassificationPeptide
Primary classTissue repair peptides
CAS registry numberUnknown No CAS-format synonym was present on the retrieved PubChem record.
PubChem CID45382195[1]
UniProt accessionUnknown No UniProt query was run in v1.
Molecular formulaC212H350N56O78S[1]
Molecular weight4963 g/mol[1]
Amino-acid sequenceUnknown Not reported by the PubChem property set retrieved for this record; no sequence database query was run in v1.
Reported half-lifeUnknown No pharmacokinetics source was retrieved in v1. PubChem does not carry half-life as a property, so this is recorded as not yet sourced rather than estimated.

What the cited literature examines

Thymosin beta 4 is a naturally occurring peptide. Its retrieved literature is primarily cell-biological: a 1991 Journal of Biological Chemistry paper reports that thymosin beta 4 and Fx, an actin-sequestering peptide, are indistinguishable, a 1993 Cell paper examines how profilin promotes actin filament assembly in its presence, and a 1992 Molecular Biology of the Cell paper addresses the control of actin nucleotide exchange by thymosin beta 4 and profilin.

A 1981 Proceedings of the National Academy of Sciences paper reports the complete amino acid sequence of bovine thymosin beta 4, and a 1997 FASEB Journal paper reports directional migration of human umbilical vein endothelial cells. The sequence is published in that 1981 paper but was not transcribed into this dataset, so the sequence field is recorded as not sourced.

[3, 4, 5, 6, 7]

Reported mechanism

Actin sequestration; identified in the retrieved literature as an actin-sequestering peptide that participates in the control of actin filament dynamics.

[3, 5]

Stated in the titles of the cited 1991 Journal of Biological Chemistry and 1992 Molecular Biology of the Cell papers.

Targets named in the cited records: actin.

FDA application register

A query of the FDA Drugs@FDA application register on 2026-10-09 returned no application records for this compound name. This compound is not approved by the FDA for human use.[2]

Scope statement: this records the result of a single automated query against the openFDA drugsfda endpoint on the stated date. It is not legal advice and is not a jurisdiction-by-jurisdiction legality assessment.

Retrieved 2026-10-09.

Amounts reported in the cited literature

Unknown. No retrieved record in this dataset states an amount, so none is shown. Where an amount is recorded it is what a named study reported administering in its own stated model, in the past tense, and is not a protocol.

No study-reported dose was taken from a source read in v1. Literature-reported values are only recorded where the retrieved citation metadata states the figure.

Adverse effects reported in the cited literature

Unknown. No retrieved record in this dataset reports an adverse effect for this compound, so no row is shown. Absence of a row records the absence of a retrieved report, nothing more.

No adverse-effect row was taken from a source read in v1. Rows are only recorded with the study model named and the reporting citation attached.

Other names

Thymosin beta 4 appears under these other names in the cited records or in common usage. Each one resolves to this page rather than to a separate page of its own.

Where this page sits

Research records

Cited research records for Thymosin beta 4, each with its identifier, the publication type it is indexed as, and the study model stated by its assigned subject headings.

Side-by-side pages that include Thymosin beta 4

Compounds indexed next to it

Named targets in the cited records

Class page: Tissue repair peptides. Full index: all indexed compounds.

Questions this page answers

What does the cited literature examine for Thymosin beta 4?

Thymosin beta 4 is a naturally occurring peptide. Its retrieved literature is primarily cell-biological: a 1991 Journal of Biological Chemistry paper reports that thymosin beta 4 and Fx, an actin-sequestering peptide, are indistinguishable, a 1993 Cell paper examines how profilin promotes actin filament assembly in its presence, and a 1992 Molecular Biology of the Cell paper addresses the control of actin nucleotide exchange by thymosin beta 4 and profilin.

Which class is Thymosin beta 4 indexed under?

Thymosin beta 4 is indexed under Tissue repair peptides. This grouping covers peptides whose retrieved research literature is predominantly concerned with tissue repair endpoints in laboratory and animal models, rather than a single shared receptor.

What does the FDA application register show for Thymosin beta 4?

A query of the FDA Drugs@FDA application register on 2026-10-09 returned no application records for this compound name. This compound is not approved by the FDA for human use.

Sources

  1. PubChem Compound Summary for CID 45382195, Thymosin Beta 4. PubChem, National Library of Medicine (2026). pubchem:45382195
  2. Drugs@FDA application register query for this compound, no application records returned. U.S. Food and Drug Administration, openFDA drugsfda endpoint (2026). fda:thymosin-beta-4
  3. Thymosin beta 4 and Fx, an actin-sequestering peptide, are indistinguishable. J Biol Chem (1991). pmid:1999398
  4. How profilin promotes actin filament assembly in the presence of thymosin beta 4. Cell (1993). pmid:8252614
  5. The control of actin nucleotide exchange by thymosin beta 4 and profilin. A potential regulatory mechanism for actin polymerization in cells. Mol Biol Cell (1992). pmid:1330091
  6. Complete amino acid sequence of bovine thymosin beta 4: a thymic hormone that induces terminal deoxynucleotidyl transferase activity in thymocyte populations. Proc Natl Acad Sci U S A (1981). pmid:6940133
  7. Thymosin beta 4 stimulates directional migration of human umbilical vein endothelial cells. FASEB J (1997). pmid:9194528

On each stated value was matched to the record cited for it. That is record matching, not an appraisal of the research. Compiled and checked by: Peptide Monographs editorial desk. No qualified clinical reviewer.

Further reading