THYMOSIN BETA 4 FRAGMENT AC-SDKP
Thymosin beta 4 is a natural human protein. It is made up of 43 amino acids and has a molecular weight of 4,291 g/mol. It is capable of binding to actin proteins and is considered to be the principal actin-sequestering protein in most cells. It therefore plays a very important role in the polymerization of actin filaments, which are important for cell structure, cell mobility, and extracellular matrix function. There is speculation, though currently no concrete evidence, to suggest that thymosin beta 4 binds to extracellular receptors in the fluids surrounding cells to mediate some of its effects.
Like many naturally occurring proteins, Thymosin Beta 4 is a very long peptide sequence therefore has to be administered Sub-Q only. It is not orally or intranasally bioavailable. Researchers found that the active domain of thymosin beta 3, a region that contains just 7 amino acids (LKKTETQ), retains most of the larger protein’s effects when it comes to cell migration, actin polymerization, and wound healing. This fragmented section is referred to as TB500 Fragment.
Because TB500 Fragment is substantially smaller than its parent molecule, its more readily absorbed by the GI tract and then by cells. This enhanced oral bioavailability makes TB500 Fragment simpler to administer than the 43 amino acid Thymosin Beta 4 and contributes to the fragment’s efficacy.
TB500 Fragment can be broken down from 7 amino acids to just four (Ac-Ser-Asp-Lys-Pro) to produce a peptide that maintains many of the larger peptide’s properties. Ac-SDKP has been found to occur naturally and is broken down by ACE (angiotensin converting enzyme) activity. This may be the reason that ACE inhibitors help to prevent scarring and cardiac remodeling because Ac-SDKP is an anti-fibrotic and anti-inflammatory peptide known to promote blood vessel growth, reduce inflammation, and reduce scarring following injury.
Molecular Formula: C20H33N5O9
Molecular Weight: 487.5 g/mol
PubChem CID: 65938
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