TGF-β3, Human, Recombinant, S. frugiperda

Recombinant, human transforming growth factor-β3 expressed in S. frugiperda insect cells.

Recombinant, human transforming growth factor-β3 expressed in S. frugiperda insect cells. The disulfide-linked homodimeric human recombinant TGF-β3 contains two 112 amino acid peptides and has a predicted molecular weight of ~25 kDa. Useful for growth ihibition assays and other assays designed to study cellular responses and receptor interactions involving TGF. The transforming growth factor (TGF) superfamily contains structurally related secretory peptides, which become activated by proteolytic cleavage. In addition to the TGF-βs, other family members include the activins, inhibins, bone morphogenetic proteins (BMPs), glial cell-line derived neurotrophic factor (GDNF), and Mullerian inhibitory substance (MIS). The three TGF-β isoforms, TGF-β1, TGF-β2, and TGF-β3, are potent regulators of cell growth and differentiation, extracellular matrix formation, and inflammatory events. The TGF-βs bind to three high affinity serine/threonine kinase receptors, designated type I (~55-65 kDa), type II (~70-85 kDa), and type III/betaglycan (~200-400 kDa). Structurally, the TGF-β1, β2, and β3 proteins are homodimers composed of disulfide linked chains 112 amino acids in length. Composition of TGF-β proteins from different species is highly conserved at the DNA level as well as at the protein level showing in general >85% identity within a subtype and 64-82% identity between subtypes. TGF-β1 and β2 were first identified on the basis of their biological activity and subsequently cloned from expression libraries. Human TGF-β3 was identified first at the cDNA level and of the three major isoforms, appears to be the most biologically active. The expression of TGF-β3 at various stages of morphogenesis and at different sites suggests an important role in the developmental process.

EC₅₀ = 0.01-0.03 ng/ml as determined by the ability to inhibit IL-4-dependent ³H-thymidine incorporation in mouse HT-2 cells.

Lyophilized from 30% acetonitrile, 0.1% TFA, 50 µg BSA/µg of cytokine.

Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 3 months at -20°C. Purified human recombinant TGF-β3 is an extremely hydrophobic protein that adheres strongly to surfaces.

Reconstitute in sterile 4 mM HCl containing at least 0.1% human serum albumin or bovine serum albumin to a final concentration of ≥1 µg/ml.

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Toxicity: Standard Handling (A)