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TB-500 5MG research peptide vial - OneLab Peptides

Actin-Binding Fragment

TB-500

  • Ac-LKKTETQ Thymosin beta-4 (17-23)

A synthetic seven-residue, N-terminally acetylated peptide (Ac-LKKTETQ) corresponding to residues 17-23 of human thymosin beta-4, the segment containing that protein's conserved actin-binding motif.

Mass
5mg
Quantity
$45.00

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Compound information

Technical specifications

Description

A synthetic seven-residue, N-terminally acetylated peptide (Ac-LKKTETQ) corresponding to residues 17-23 of human thymosin beta-4, the segment containing that protein’s conserved actin-binding motif.

Molecular profile

Type
Synthetic acetylated heptapeptide
CAS number
885340-08-9
Molecular weight
889.0 g/mol
Molecular formula
C38H68N10O14
Amino acids
7

Storage requirements

Lyophilized (powder) -20°C
Reconstituted 2-8°C
  • Protect from light
  • Avoid repeated freeze-thaw cycles
  • Reconstitute with bacteriostatic water

Frequently researched together

Commonly held alongside this compound in the same catalog category.

Sources & references

Published literature, listed for reference only. Nothing here describes an intended use of this product.

Synthesis and characterization of the N-terminal acetylated 17-23 fragment of thymosin beta 4 identified in TB-500

Drug Test Anal 2012

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Thymosin beta 4 and a synthetic peptide containing its actin-binding domain promote dermal wound repair in db/db diabetic mice and in aged mice

Wound Repair Regen 2003

View source

The actin binding site on thymosin beta4 promotes angiogenesis

FASEB J 2003

View source

Important research notice

Not for human consumption. This product is sold exclusively for laboratory research. It is not intended to diagnose, treat, cure, or prevent any disease, and has not been evaluated by the U.S. Food and Drug Administration.

Any literature referenced on this page is provided for bibliographic reference only. It is not a description of this product, nor a claim about what it does.

By purchasing you confirm you are a qualified researcher and will handle this material in accordance with all applicable laws and institutional requirements.

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