Host: HEK293 cells • AA: 301-412 • Tag: N-terminal IgG1 Fc • MW: 41.2 kDa
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TGF-β3 Receptor-Binding Domain (human, recombinant)

Item No. 42759

Product Insert (PDF)
Technical Information
Synonyms
  • Transforming Growth Factor β3
Purity
≥90% estimated by SDS-PAGE
Endotoxin Testing
<1.0 EU/µg determined by the LAL endotoxin assay
Source
Recombinant N-terminal human IgG1 Fc-tagged TGF-β3 receptor-binding domain expressed in HEK293 cells
Amino Acids
301-412
MW
41.2 kDa
Lyophilized from sterile 20 mM HEPES pH 7.0, with 150 mM sodium chloride and 0.2% CHAPS
Host
HEK293 cells
UniProt Accession №
P10600
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    Product Description

    TGF-β3 is a multifunctional cytokine and member of the TGF-β superfamily.1 TGF-β3 is expressed as a proprotein that is cleaved in the Golgi to form TGF-β3 latency-associated peptide (LAP) and mature TGF-β3.2 TGF-β3 and TGF-β3 LAP remain non-covalently bound until mature TGF-β3 is released from latency by various proteins, including matrix metalloproteinases and plasmin.2,1 Secreted TGF-β3 homodimers induce signaling through activin receptor-like kinase 5 (ALK5), also known as TGF-β receptor type 1 (TGF-βRI), and TGF-β receptor type 2 (TGFBR2) and is involved in embryonic development, epidermal homeostasis, wound healing, bone formation, and involution of excess mammary gland epithelial cells during lactation.1 It increases collagen levels in primary human foreskin fibroblasts.3 High levels of TGF-β3 are associated with disease progression in patients with osteosarcoma.4 Cayman's TGF-β3 Receptor-Binding Domain (human, recombinant) protein is a disulfide-linked homodimer. The reduced monomer, composed of TGF-β3 (amino acids 301-412) fused to human IgG1 Fc at its N-terminus, consists of 373 amino acids and has a calculated molecular weight of 41.2 kDa.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Laverty, H.G., Wakefield, L.M., Occleston, N.L., et alTGF-β3 and cancer: A review. Cytokine Growth Factor Rev. 20(4), 305-317 (2009).

    2. Khalil, N. TGF-β: From latent to active. Microbes Infect. 1(15), 1255-1263 (1999).

    3. Murata, H., Zhou, L., Ochoa, S., et alTGF-β3 stimulates and regulates collagen synthesis through TGF-β1-dependent and independent mechanisms. J. Invest. Dermatol. 108(3), 258-262 (1997).

    4. Kloen, P., Gebhardt, M.C., Perez-Atayde, A., et alExpression of transforming growth factor-β (TGF-β) isoforms in osteosarcomas: TGF-beta3 is related to disease progression. Cancer 80(12), 2230-2309 (1997).