TGFB1 Human Recombinant
CHO cells.
Description
TGFB1 Human Recombinant produced in CHO cells is a glycosylated homodimeric polypeptide chain containing 2 x 112 amino acids and having a total molecular mass of 25.6kDa. The TGFB1 is purified by proprietary chromatographic techniques.
Product Specs
Transforming growth factor betas (TGF-betas) are involved in cell-to-cell communication during embryonic development in mammals. There are three known types of TGF-betas: TGF-beta1, TGF-beta2, and TGF-beta3. All three TGF-betas are initially synthesized as larger precursor proteins. These precursor proteins undergo cleavage, resulting in a 112-amino acid polypeptide that remains connected to the inactive part of the molecule.
Recombinant human TGFB1, produced in CHO cells, is a glycosylated homodimeric polypeptide chain consisting of 2 chains of 112 amino acids each. The total molecular weight of the protein is 25.6kDa. TGFB1 is purified using proprietary chromatographic methods.
The product appears as a sterile, filtered, white, lyophilized (freeze-dried) powder.
The product is lyophilized from a sterile, filtered solution containing 0.1% trifluoroacetic acid (TFA) and trehalose at a protein-to-trehalose ratio of 1:20.
To reconstitute the lyophilized TGFB1, it is recommended to dissolve it in sterile 10mM HCl at a concentration of 0.1 mg/ml. This solution can then be further diluted in other aqueous solutions as needed.
Lyophilized TGFB1, while stable at room temperature for up to 3 weeks, should be stored in a dry environment below -18°C. Once reconstituted, the human TGFB1 should be stored at 4°C for 2-7 days. For long-term storage, it is recommended to store it below -18°C. The addition of a carrier protein (0.1% HSA or BSA) is advised for long-term storage. Repeated freezing and thawing cycles should be avoided.
The purity of the product is greater than 95.0% as assessed by SDS-PAGE analysis.
The ED50, determined by the dose-dependent inhibition of IL-4-induced proliferation of HT-2 cells, is 0.0149 ng/ml. This corresponds to a specific activity of 6.7 x 10^7 units/mg.
CHO cells.
Product Science Overview
TGF-β1 was originally identified for its ability to induce phenotypic transformation of fibroblasts . It is the most abundant isoform and is secreted by almost every cell type . TGF-β1 is involved in various physiological processes, including embryogenesis, tissue remodeling, and wound healing . It is secreted predominantly as latent complexes, which are stored at the cell surface and in the extracellular matrix . The release of biologically active TGF-β1 from a latent complex involves proteolytic processing of the complex and/or induction of conformational changes by proteins such as thrombospondin-1 .
Human recombinant TGF-β1 is synthesized using genetic engineering techniques, enabling the production of large quantities of biologically active protein for research purposes . The recombinant form is typically derived from human embryonic kidney (HEK293) cells . The protein is a 25.0 kDa molecule with each subunit containing 112 amino acid residues, linked by a single disulfide bond . The recombinant TGF-β1 is purified to a high degree, with a purity of ≥ 98% as determined by SDS-PAGE gel and HPLC analyses .
The biological activity of TGF-β1 is measured by its ability to inhibit the IL-4-dependent proliferation of mouse HT-2 cells . The effective dose (ED50) for this activity is ≤ 0.05 ng/ml, corresponding to a specific activity of ≥ 2 x 10^7 units/mg . TGF-β1 has been implicated in various biological processes, including the formation of skin tumors . It is also involved in angiogenesis, immune regulation, and the promotion or inhibition of various immune events .
Due to its wide range of biological activities, TGF-β1 is a subject of extensive research. It has been studied in the context of cancer, fibrosis, and immune disorders . The recombinant form of TGF-β1 is used in various research applications to study its effects on cell proliferation, differentiation, and immune modulation . It is also used in tissue engineering and regenerative medicine due to its role in tissue remodeling and wound healing .
