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Research Peptide
TB-500 research peptide kit.
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99%+ purity
HPLC verified
43AA
SEQUENCE LENGTH
Active region of Thymosin Beta-4
80+
PUBLICATIONS
In wound healing & tissue repair
4.9kDa
MOL. WEIGHT
Small actin-binding protein
G-actin
MECHANISM
Sequesters monomeric actin
7-14days
STUDY DURATION
Typical research timeframe
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on orders over $150
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Research
This listing supplies TB-500, the acetate salt of Thymosin Beta-4, as a lyophilized research peptide for in-vitro and preclinical laboratory work only. Thymosin Beta-4 (often abbreviated Tβ4) is a 43-residue, water-soluble peptide belonging to the beta-thymosin family and is one of the most abundant members of that family in the research literature. In laboratory shorthand the material is frequently referred to by the code TB-500, a designation historically used for synthetic beta-thymosin preparations studied in animal and cell-culture models. The compound carries CAS number 77591-33-4 and the molecular formula C212H350N56O78S, corresponding to a single sulfur-bearing methionine within an otherwise acidic, unstructured chain.
The defining structural motif of this peptide in the research literature is its actin-binding sequence. Beta-thymosins contain a short conserved segment (commonly written as the LKKTET-type motif) that mediates interaction with monomeric G-actin. Much of the mechanistic interest in TB-500 as a reference material stems from this actin-sequestering behavior, which places it among the tool compounds used to study cytoskeletal dynamics at the bench. The material is offered strictly as a characterized reference substance for that kind of controlled investigation and has no established consumer application.
Published work on Thymosin Beta-4 is predominantly in-vitro and rodent-model in nature and is best understood as mechanistic and hypothesis-generating rather than settled. The summaries below describe observations reported in laboratory systems only; they are not evidence of outcomes in humans or animals, and the research remains preliminary and ongoing.
These references describe experimental laboratory work only. They are not medical claims, are not evidence of safety or efficacy in humans or animals, and should not be interpreted as guidance for any use outside a controlled research environment. Nothing here is medical advice.
For a 43-residue peptide, reproducible research depends on confirming both sequence fidelity and purity before the material enters an experiment. Each research lot is supplied as a lyophilized powder and characterized using orthogonal methods so that identity (confirmation the molecule is the correct sequence) is separated from purity (how much of the sample is the target peptide). Reversed-phase HPLC (RP-HPLC) quantifies chromatographic purity by peak-area integration, with lot purity reported on the Certificate of Analysis (COA) at ≥98%. The chromatogram resolves the main peak from process-related impurities and truncated sequences that can arise during synthesis of a chain this length.
Identity is confirmed by mass spectrometry (commonly ESI-MS or MALDI-TOF), which verifies that the observed mass matches the theoretical value for the C212H350N56O78S composition rather than a deletion or oxidation variant; the single methionine residue means oxidation state is one attribute worth confirming on the analytical record. Because TB-500 is supplied as an acetate salt, a lyophilized vial also contains counter-ion and residual water, so net peptide content can differ from gross fill weight. Researchers evaluating the material typically review the lot-matched COA for reported HPLC purity, the mass-spec identity confirmation, and net peptide content, and retain it alongside experimental records to support traceability and accurate stock-concentration calculations.
The following describes conventional handling of lyophilized research peptides and is not instruction for human or animal use. As a freeze-dried peptide, TB-500 is hygroscopic and sensitive to repeated temperature cycling. Standard laboratory practice is to allow sealed vials to equilibrate to room temperature before opening to minimize condensation on the powder, and to reconstitute with an appropriate research-grade solvent under aseptic technique. Aliquoting reconstituted stock into single-use portions limits freeze-thaw cycles that can degrade a long, unstructured peptide. Detailed temperature and stability windows for lyophilized, reconstituted, and working solutions appear in the storage table on this page, and handling should follow institutional chemical-safety procedures with appropriate PPE.
It supplies TB-500 (Thymosin Beta-4 acetate) as a lyophilized, freeze-dried white powder in a sealed research vial, sized by peptide mass (for example 5 mg or 10 mg). Lyophilization improves shelf stability for a peptide of this length and lets the researcher reconstitute with a chosen research-grade solvent under aseptic conditions when preparing in-vitro experiments. It is a research chemical for laboratory use only, not a therapeutic product.
TB-500 is the laboratory designation commonly applied to synthetic Thymosin Beta-4 preparations, supplied here as the acetate salt (CAS 77591-33-4, formula C212H350N56O78S). Thymosin Beta-4 is a 43-residue beta-thymosin peptide, and its conserved actin-binding motif is the structural feature most frequently referenced when the compound is used as a research probe.
Published work is predominantly in-vitro and rodent-model, spanning actin-sequestration biochemistry, cell-migration and scratch-wound assays, and angiogenesis-associated endpoints in preclinical model systems. These are mechanistic, model-based observations that remain preliminary and ongoing; they do not establish any human or animal outcome and are not medical claims.
Purity is measured by reversed-phase HPLC and reported as a percentage of total peak area (≥98% for this material), while identity is confirmed by mass spectrometry (ESI-MS or MALDI-TOF) against the theoretical mass for the C212H350N56O78S composition. Review the lot-specific COA for the HPLC purity value, the mass-spec identity confirmation, and net peptide content, since it is the authoritative analytical record for the exact vial you receive.
This product is sold strictly for in-vitro research and laboratory use only. It is not intended for human or animal consumption, diagnostic purposes, or therapeutic application.
By purchasing this product, you confirm that you are a qualified researcher operating within an appropriate laboratory environment and will use this compound in accordance with all applicable local, state, and federal regulations.
Amino Science Labs assumes no liability for misuse of this product outside of its intended research application.
A lyophilized acetate-salt vial contains counter-ion and residual water in addition to the peptide, so the net peptide mass can be lower than the gross fill weight. Using the lot-matched COA's reported net peptide content and purity lets researchers calculate accurate stock concentrations, which is essential for reproducible in-vitro work. The single methionine residue also makes oxidation state worth confirming on the analytical record.
Allow the sealed vial to reach room temperature before opening to prevent condensation on the hygroscopic powder, reconstitute using aseptic technique with a research-grade solvent, and aliquot stock to avoid repeated freeze-thaw cycles that can degrade a long peptide. Follow the temperature and time windows in the storage table on this page and your institution's chemical-safety practices. This material is for in-vitro and preclinical research only, not for human or animal use.