TGFβ1 (mutant) (human):Fc (human) (rec.)
|Synonyms||Transforming Growth Factor beta-1; TGFB1; TGFB|
The mutant human TGF-β1 (including aa30-278 (Latency-Associated Peptide, LAP) and aa279-390 (TGF-β1)) is fused to the N-terminus of the Fc region of human IgG4. Site-directed mutagenesis was used to change three cysteine codons into a serine codon that are located in the pro region of the TGF-β precursor at amino acid positions 33, 223, and 225.
Binds human TGFβ. Shown to cross-react with mouse TGFβ (see lit. reference 1).
Shows the biological function of the TGFβ1 moiety and exerts a prolonged circulating half-life caused by the modified Fc domain.
|Endotoxin Content||<0.06EU/μg protein (LAL test; Lonza).|
Reconstitute with 100 µl sterile water.
Add 1X PBS to the desired protein concentration.
|Formulation||Lyophilized from 0.2μm-filtered solution in PBS.|
|Protein Negative Control|
|Declaration||Manufactured by Chimerigen.|
|Shipping and Handling|
|Short Term Storage||+4°C|
|Long Term Storage||-20°C|
Avoid freeze/thaw cycles.
Centrifuge lyophilized vial before opening and reconstitution.
Stable for at least 1 year after receipt when stored at -20°C.
Working aliquots are stable for up to 3 months when stored at -20°C.
|Product Specification Sheet|
TGF-β1 (Transforming growth factor beta 1) is a polypeptide member of the transforming growth factor beta superfamily of cytokines. It is a secreted protein that performs many cellular functions, including the control of cell growth, cell proliferation, cell differentiation and apoptosis. In humans, TGF-β1 is encoded by the TGFB1 gene. TGF-β1 was first identified in human platelets as a protein with a molecular mass of 25 kaD with a potential role in wound healing. It was later characterized as a large protein precursor (containing 390 aa) that was proteolytically processed to produce a mature peptide of 112 aa. TGF-β1 plays an important role in controlling the immune system, and shows different activities on different types of cell, or cells at different developmental stages. Most immune cells (or leukocytes) secrete TGF-β1.
Normally, TGF-β1 is secreted as a complex with Latency-Associated Peptide (LAP) that is inactive. Removal of LAP activates TGF-β1 that is cleared quickly from the circulation. This specific mutant protein containing the LAP+TGF-β1 domains including the indicated three mutated cysteines, allows the protein to be active and to have long lasting biological activity with increased stability and half-life time.
- Combined administration of a mutant TGF-beta1/Fc and rapamycin promotes induction of regulatory T cells and islet allograft tolerance: W. Zhang, et al.; J. Immunol. 185, 4750 (2010)