Transforming growth factor betas (TGF-betas) are signaling molecules that play a crucial role in regulating cell growth and differentiation during embryonic development. Three main types of TGF-betas (TGF-beta1, TGF-beta2, and TGF-beta3) have been identified in mammals. These proteins are initially produced in a precursor form and undergo enzymatic cleavage to release a smaller active protein of 112 amino acids. The active TGF-beta remains associated with the remaining portion of the precursor molecule, forming a complex.
Recombinant Mouse TGFB1, produced in E. coli, is a single polypeptide chain without any glycosylation modifications. It consists of 135 amino acids (corresponding to amino acid positions 279-390 of the native protein) and has a molecular weight of 15.2 kDa. For purification and detection purposes, a 23 amino acid Histidine tag is attached to the N-terminus of the TGFB1 protein. Purification is carried out using proprietary chromatographic methods.
The product is a clear, colorless solution that has been sterilized by filtration.
The TGFB1 protein is supplied in a solution at a concentration of 0.25 mg/ml. The solution contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
For short-term storage (up to 2-4 weeks), keep the product refrigerated at 4°C. For extended storage, freeze the product at -20°C. To ensure long-term stability during frozen storage, it is recommended to add a carrier protein such as albumin (0.1% HSA or BSA). Repeated freezing and thawing of the product should be avoided to maintain its integrity and activity.
The purity of the TGFB1 protein is determined to be greater than 85.0% using SDS-PAGE analysis.
TGF-β1 is a homodimeric protein, meaning it consists of two identical subunits linked by disulfide bonds. The precursor form of TGF-β1 contains 390 amino acids, including an N-terminal signal peptide, a latency-associated peptide (LAP), and a C-terminal region that becomes the active TGF-β1 upon activation . The mature form of TGF-β1 is produced through proteolytic cleavage, which removes the LAP and releases the active cytokine.
TGF-β1 is involved in a wide range of biological processes:
Cell Proliferation and Differentiation: TGF-β1 can either promote or inhibit cell proliferation depending on the cell type and context. It plays a critical role in the differentiation of various cell types, including immune cells, fibroblasts, and epithelial cells .
Angiogenesis: TGF-β1 promotes the formation of new blood vessels, which is essential for tissue repair and regeneration .
Immune Regulation: TGF-β1 has both immunosuppressive and immunostimulatory effects. It can inhibit the proliferation of T cells and the production of pro-inflammatory cytokines, while also promoting the differentiation of regulatory T cells (Tregs) and Th17 cells .
TGF-β1 exerts its effects by binding to specific cell surface receptors, known as TGF-β receptors. The binding of TGF-β1 to the type II receptor (TβRII) leads to the recruitment and phosphorylation of the type I receptor (TβRI). This receptor complex then activates intracellular signaling pathways, including the Smad pathway, which regulates the expression of target genes involved in various cellular processes .
Recombinant mouse TGF-β1 is extensively used in research to study its role in various biological processes and diseases. Some key applications include:
Cancer Research: TGF-β1 is known to play a dual role in cancer, acting as a tumor suppressor in early stages and as a promoter of tumor progression in later stages. Researchers use recombinant TGF-β1 to investigate its effects on cancer cell proliferation, invasion, and metastasis .
Immunology: TGF-β1 is a critical regulator of immune responses. It is used to study its effects on T cell differentiation, immune tolerance, and autoimmune diseases .
Tissue Engineering and Regenerative Medicine: Due to its role in cell proliferation and differentiation, TGF-β1 is used in tissue engineering to promote the regeneration of damaged tissues and organs .