- Recombinant Proteins
- Cytokines and Growth Factors
- TGF-beta Superfamily Neurotrophic Factors
- TGF-β
- TGF-β3
TGF-β3
TGF-β3 (transforming growth factor-β3) is a member of a TGFbeta superfamily subgroup that performs many cellular functions. TGF-β3 has a role in embryogenesis and cell differentiation. TGF-β3 also plays a critical role in palatogenesis, the wound healing process. TGF-β3 is capable of binding directly to the type II receptor (TβRII). Three TGF-β isoforms have been found in mammals: TGF-β1, 2, and 3, which are structurally and functionally similar. TGF-β3 is important in embryonic development, scarless repair of injury in the embryo, adult wound healing and tissue homeostasis. It has an important role in regulating cell migration, angiogenesis, epithelial-mesenchymal transition, apoptosis, modulation of immune function, extracellular matrix (ECM) production and the regulation of ECM remodelling; biological processes that are often required for tumour growth and maintenance[1][2].
As with all members of the family, TGF-β3 is highly conserved across species, with mouse, rat and human TGF-β3 demonstrating >97% sequence homology.
TGF-β3 is released from LAP by integrins: integrin-binding results in distortion of the LAP chain and subsequent release of the active TGF-β3. TGF-β3 expression increases in fetal wound healing and reduces fibronectin and collagen I and III deposition, and also improves the architecture of the neodermis. Fibroblasts are key cells in the wound healing process. In addition, TGF-β3 may actually play a protective role against tumourigenesis in a range of tissues including the skin, breast, oral and gastric mucosa. TGF-β3 is a more potent inhibitor of DNA synthesis in human keratinocytes compared to TGF-β1 and TGF-β2. TGF-β3 mRNA is expressed in lymphocytes such as CD4+ T cells, CD8+ T cells, γδT cells, and B cells. TGF-β3 has the potential to regulate systemic autoimmune diseases by inhibiting B cells. Moreover, during palatogenesis, TGF-β3 is supposed to transduce signals via both canonical Smad-dependent and non-canonical Smad-independent signaling. In human B cells, TGF-β3 induces phosphorylation of Smad1/5 along with Smad2 and Smad3[1][2][3].
- [1]. Mahmoudi Rad M, et al. Expression of TGF-β3 in isolated fibroblasts from foreskin. Rep Biochem Mol Biol. 2015 Apr;3(2):76-81. [Content Brief]
- [2]. Laverty HG, et al. TGF-beta3 and cancer: a review. Cytokine Growth Factor Rev. 2009 Aug;20(4):305-17. [Content Brief]
- [3]. Toshihiko Komai, et al. Reevaluation of Pluripotent Cytokine TGF-β3 in Immunity. Int J Mol Sci. 2018 Aug 1;19(8):2261. [Content Brief]
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TGF-β3 Recombinant Proteins (6)
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Inhibitors & Agonists (280)
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Recombinant Protein Expression Service
- Codon Optimization
- Gene Synthesis
- Construction of Expression Vector
- Strain Screening
- Protein Expression
- Purification & QC
- Protein Delivery
- Formula: Human
- Molecular Weight: Sf9 insect cells
The EpCAM/TROP1 protein serves as an important homogeneous interacting molecule that promotes direct contact between intestinal epithelial cells (IEC) and intraepithelial lymphocytes (IEL) in the mucosal epithelium. This feature helps establish an immune barrier against mucosal infections. EpCAM/TROP1 Protein, Human (His-SUMO) is the recombinant human-derived EpCAM/TROP1 protein, expressed by E. coli , with N-6*His, N-SUMO labeled tag.
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