Transforming growth factor-beta 3 (TGF-β3), also known as TGFB3, is a member of the TGF beta family of growth factors along with TGF-β1 and -2. The members of this family can be expressed by most cell types and are proposed to act as cellular switches that regulate immune function, proliferation and epithelial-mesenchymal transition (1). These cytokines are secreted in precursor form consisting of a bioactive C-terminal domain attached to an N-terminal domain known as latency associated protein (LAP). Cleavage of LAP results in the mature protein, which functions as a disulfide-linked homodimer. TGF-β3 and these homodimers of LAP remain non-covalently associated after secretion, forming the latent TGF-β3 complex (2). Activation of this latent complex is accomplished by actions from plasmin, MMPs, thrombospondin 1 and some integrins (3). The receptor for TGF-β3 is TGF-β RII which phosphorylates, and activates another receptor, either ALK-5 or ALK-1. This second complex activates Smad proteins that regulate transcription. TGF-β3 is involved in oxygen-dependent differentiation processes during placental development and pregnancy disorders (4) and it also plays an important role in wound repair and scarring (5). TGF-β3 is believed to regulate molecules involved in cellular adhesion and extracellular matrix (ECM) formation during the process of palate development, without it, mammals develop a deformity known as a cleft palate (6). Similarly, TGF-β3 also plays an essential role in controlling the development of lungs in mammals, also by regulating cell adhesion and ECM formation in this tissue (6). Defects in the TGF-β3 gene are a cause of familial arrhythmogenic right ventricular dysplasia 1 (ARVD1) (7). ARVD1 is an autosomal dominant disease characterized by partial degeneration of the myocardium of the right ventricle, electrical instability and sudden death.
>97% by SDS-PAGE and analyzed by silver stain.
<0.01 EU/µg as determined by the LAL method
The biological activity of Human TGF-β3 was determined by its ability to inhibit the IL-4-dependent proliferation of mouse HT-2 cells. The expected ED50 for this effect is typically 0.03 - 0.08 ng/ml.
Sf 21 Insect Cells
Amino Acid Sequence
aldtnycfrn leenccvrpl yidfrqdlgw kwvhepkgyy anfcsgpcpy lrsadtthst vlglyntlnp easaspccvp qdlepltily yvgrtpkveq lsnmvvksck cs
N-terminal Sequence Analysis
State of Matter
Predicted Molecular Mass
The predicted molecular weight of Recombinant Human TGF-β3 is Mr 12.7 kDa. However, the actual molecular weight as observed by migration on SDS-PAGE is 12 kDa (reducing conditions) and 24 kDa (non-reducing conditions).
This recombinant protein was lyophilized from a 0.2 μm filtered solution in 40% acetonitrile (CH3CN) and 0.1% trifluoroacetic acid (TFA).
Storage and Stability
This lyophilized protein is stable for six to twelve months when stored desiccated at -20°C to -70°C. After aseptic reconstitution, this protein may be stored at 2°C to 8°C for one month or at -20°C to -70°C in a manual defrost freezer. Avoid Repeated Freeze Thaw Cycles. See Product Insert for exact lot specific storage instructions.
Country of Origin
Next Day Ambient
NCBI Gene Bank
References & Citations
1. Sporn, MB. et al. (2006) Cytokine Growth factor Rev. 17:3
2. Derynck, R. et al. (1988) EMBO J. 7:3737
3. Oklu, R. et al. (2000) Biochem. J. 352:601
4. Wenger, RH. et al. (2003) Placenta 24:941
5. Bandyopadhyay, B. et al. (2006) J. Cell. Biol. 172:1093
6. Kaartinen, V. et al. (1995) Nat. Genet. 11:415
7. Nattel, S. et al. (2005) Cardiovasc. Res. 65:302
IMPORTANT Use lot specific datasheet for all technical information pertaining to this recombinant protein.
Products are for research use only. Not for use in diagnostic or therapeutic procedures.