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TB-500 Fragment (17-23)

TB-500 Fragment (17-23) is a synthetic research peptide consisting of the key active amino acid sequence from the actin-binding region of thymosin beta-4.

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TB-500 Fragment (17-23) is a synthetic research peptide consisting of the key active amino acid sequence from the actin-binding region of thymosin beta-4. Supplied as a high-purity lyophilized powder, it’s used in laboratory research to study cellular migration, actin dynamics, angiogenic signaling, and tissue remodeling processes.

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All Biotech Peptides products are independently third-party tested at a USA-based HPLC-licensed laboratory prior to distribution. Certificates of Analysis (COA) are published on the Independent Test Results page and available at product level. If any independently conducted HPLC test returns a negative result, Biotech Peptides will refund: (1) the cost of the HPLC test, and (2) the full order amount including shipping.
TB-500 Fragment (17-23)5mg 1vial | 10mg 1vial
Chemical Formula C38H68N10O14
Synonyms TB-500 Fragment (17-23), Thymosin Beta-4 Fragment 17-23, LKKTETQ
Molar Mass 889.02 g/mol
CAS Number 885340-08-9
PubChem CID 62707662
Total Compound Content 10 mg per vial
Shelf Life 36 months

TB-500 Fragment (17-23) is the N-acetylated seven-residue sequence (Ac-Leu-Lys-Lys-Thr-Glu-Thr-Gln) corresponding to the LKKTET actin-binding motif found at position 17–23 of Thymosin Beta-4. Because this short sequence contains the core determinant of Tβ4's interaction with G-actin, it is frequently used in comparative studies examining whether a given cytoskeletal or signaling effect requires the full 43-residue protein or can be reproduced by the isolated binding motif alone.

Experimental work involving this fragment has focused on actin monomer sequestration assays, structure-activity mapping of the Tβ4 actin-binding domain, and mechanistic comparisons between the minimal fragment and full-length Tβ4 in cytoskeletal reorganization models. Because of its small size relative to full-length Tβ4, the fragment is also used in analytical chemistry and mass-spectrometry method development, including doping-control and peptide-identification research.

Every batch is independently lab tested for identity, purity and potency. View our lab testing program →

How does TB-500 Fragment (17-23) differ from full-length TB-500/Thymosin Beta-4?

The Fragment (17-23) contains only the seven-residue LKKTET actin-binding motif that sits within the larger 43-residue Tβ4 sequence, rather than the full protein. It is typically used to test whether an observed effect of full-length Tβ4 depends on the whole protein or can be attributed to this minimal actin-binding region alone.

What is the primary research application of this fragment?

It's used mainly in comparative actin-binding and structure-function studies, where researchers assess G-actin interaction and cytoskeletal effects of the isolated motif relative to full-length Thymosin Beta-4. It also sees use in analytical/mass-spectrometry method development for peptide identification.

Is this compound identical to commercial "TB-500"?

The name "TB-500" has been used inconsistently across the peptide supply industry — some vendors apply it to the full 43-residue Tβ4 analogue, while analytical and anti-doping literature identifies "TB-500" specifically as this Ac-LKKTETQ fragment. This listing is the isolated 7-residue fragment (CAS 885340-08-9); check formula and CAS number against any other "TB-500" product before comparing them directly.

Customer Reviews (8)

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Anonymous

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Patterson

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CoreLab

Highly satisfied with the ordering process and the chemical quality is top notch. A trustworthy supplier. The experimental results were exceptional.

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Michael

Cannot recommend enough the ordering process and the compound is pure and high quality. Reordering next week. My laboratory research results exceeded expectations.

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SciGuy

I'm very happy with the fast turnaround times, quality was great and dispatch was incredibly fast. Highly recommend this vendor. Our research results are completely exceeding expectations.