In cross-linking experiments with pure proteins in vitro, Tβ4 interacted with PDGF-BB, shown by EDC cross-linking and biotin label transfer.
In plain wordsIn lab tests with pure proteins, Tβ4 was found to bind PDGF-BB.
- Peptide
- Thymosin beta-4 (human)
- Outcome
- Not applicableBinding of Tβ4 to PDGF-BB
- Study
n: not reported in source
purified Tβ4 and PDGF-BB proteins- Outcome group
- Receptor activity and mechanism · Pharmacology
- Studied dose
- Dose not stated
Source sentences
We identified an interaction between Tβ4 and PDGF-BB by 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC) cross-linking as well as through biotin label transfer using a bifunctional photoactivatable derivative of Tβ4.
2 context sentences(design, population, supporting numbers)
In an in vitro system, PDGF-BB was identified as the first extracellular partner interacting with Tβ4.
To prove our suggestion of a direct interaction between Tβ4 and PDGF-BB, we carried out chemical as well as photochemical cross-linking experiments between the two pure proteins in vitro.