TB 500 (Timosina Beta 4)

Research peptides

TB 500 (Timosina Beta 4)

Available documentary data and items still to verify are detailed below.

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SKUTB 500

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02 — Information to verify

Product details

Overview

TB-500 is a name associated with a fragment of thymosin β4. The peptide fragment must be distinguished from the full protein: its name, sequence, and terminal modifications define different molecular species.

Structure and technical data

Technical data

Catalog format: 10 mg. The listed structural record describes Ac-LKKTETQ, a seven-residue fragment with N-terminal acetylation. Its formula and mass include the acetyl group.

TB 500 (Timosina Beta 4): 2D molecular structure
2D molecular structure — PubChem. PubChem CID 62707662
Sequence
Ac-LKKTETQ
Molecular formula
C38H68N10O14
Reported molecular mass
889.0 g/mol
CAS number
885340-08-9
PubChem CID
62707662
Reported synonyms
QHK6Z47GTG

Reference molecular data.

View the PubChem record — PubChem CID 62707662

The record describes the N-acetylated fragment Ac-LKKTETQ, not full-length thymosin β4. Formula and mass include the acetylation, which is absent from the abbreviated sequence LKKTETQ.

Research context

Research considers cell migration, actin, and extracellular-matrix remodelling. The cited analytical paper examines identification of TB-500 and its metabolites by chromatography and mass spectrometry. Studies of full-length thymosin β4 do not automatically establish the same properties for the fragment.

Fragment, acetylation, and thymosin β4

The seven-residue fragment and full-length thymosin β4 are different experimental entities. N-terminal acetylation changes formula and mass without changing the seven sequence letters. Comparing studies requires material identity, termini, and analytical methods rather than the TB-500 name alone.

10.1016/j.chroma.2012.09.043

Actin, migration, and cellular organisation

Actin dynamics connect the cytoskeleton with adhesion and cell movement. In thymosin-β4-family research, migration, proliferation, and differentiation describe different processes. Fragment research must determine which full-protein interactions are retained rather than assuming they all transfer.

10.1016/j.chroma.2012.09.043

Extracellular matrix, collagen, and MMP/TIMP

Tissue remodelling depends on both matrix deposition and degradation. Metalloproteinases (MMPs) and their inhibitors (TIMPs) are studied within this balance. The liver-fibrosis review describes these general mechanisms; it is not an experiment establishing the same effects for the TB-500 fragment.

10.1016/j.biopha.2023.114472

Biomaterials, immunomodulation, and muscle

Biomaterials research includes supporting matrices, controlled signal release, macrophage polarisation, and stem-cell interactions. Some papers evaluate muscle repair and transcriptomes after volumetric muscle loss. These are studies of complex platforms, not evidence that peptide alone reproduces every result.

10.1002/jbm.a.37239 10.1016/j.bioactmat.2021.04.017 10.1186/s12891-023-06401-1

LC-MS identification and metabolites

The 2012 analytical paper studies TB-500 in equine urine and plasma using liquid chromatography and mass spectrometry. Separation, fragmentation, and metabolite recognition distinguish it from related peptides. A detection method does not establish biological efficacy or safety.

10.1016/j.chroma.2012.09.043

References

Catalog of products presented for research activities. Not for human or veterinary use. This notice does not replace verification of applicable rules.