Host: HEK293 cells • AA: 1-278 (full length) • Tag: C-terminal His • MW: 29.9 kDa
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TGF-β1 LAP (human, recombinant)

Item No. 42003

Technical Information
Synonyms
  • TGF-β1 Latency-associated Peptide
  • Transforming Growth Factor β1 LAP
  • Transforming Growth Factor β1 Latency-associated Peptide
Purity
≥95% as estimated by SDS-PAGE
Endotoxin Testing
<1.0 EU/µg determined by the LAL endotoxin assay
Source
Recombinant human C-terminal His-tagged TGF-β1 LAP expressed in HEK293 cells
Amino Acids
1-278 (full length)
MW
29.9 kDa
Lyophilized from sterile PBS, pH 7.4
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    Product Description

    Transforming growth factor β1 (TGF-β1) is a multifunctional cytokine and member of the TGF-β superfamily.1,2 It is an extracellular dimeric protein that is produced by multiple cell types, including macrophages, platelets, neutrophils, regulatory T cells, and renal tubular cells, and is the most abundantly expressed isoform of TGF-β. TGF-β1 is expressed as a proprotein that is cleaved in the Golgi to form TGF-β1 latency-associated peptide (LAP) and mature TGF-β1.2 TGF-β1 LAP and TGF-β1 remain non-covalently bound until mature TGF-β1 is released from latency by various proteins, including matrix metalloproteinases and plasmin, to regulate immune function, epithelial-mesenchymal transition, and cell proliferation. TGF-β1 LAP inhibits TGF-β1-induced inflammation and fibrosis in HSC-T6 rat hepatic cells and H9c2 rat cardiomyocytes, as well as in a mouse model of carbon tetrachloride-induced liver fibrosis.3,4 Cayman’s TGF-β1 LAP (human, recombinant) protein consists of 260 amino acids, has a calculated molecular weight of 29.9 kDa, and a predicted N-terminus of Leu30 after signal peptide cleavage. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is ~38-45 kDa due to glycosylation.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Martelossi Cebinelli, G.C., Paiva Trugilo, K., Badaró Garcia, S., et alTGF-β1 functional polymorphisms: A review. Eur. Cytokine Netw. 27(4), 81-89 (2016).

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

    3. Song, X., Shi, J., Liu, J., et alRecombinant truncated latency-associated peptide alleviates liver fibrosis in vitro and in vivo via inhibition of TGF-β/Smad pathway. Mol. Med. 28(1), 80 (2022).

    4. Song, X., Qiu, Y., Shi, J., et alProkaryotic expression, purification and evaluation of anti-cardiac fibrosis activity of recombinant TGF-β latency associated peptide. PeerJ 10, e12797 (2022).