Description
Product Characteristics: Protein. The extracellular domain of a mutant human TGFbeta1 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-beta precursor at amino acid positions 33, 223, and 225. Source: CHO cells. Endotoxin content: <0.06EU/µg protein (LAL test, Lonza). Lyophilized from 0.2µm-filtered solution in PBS. Binds human TGFbeta. Shown to cross-react with mouse TGFbeta (see lit. reference 1). Purity: >98 % (SDS-PAGE). TGF-beta1 (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-beta1 is encoded by the TGFB1 gene. TGF-beta1 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-beta1 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-beta1.
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Target Information: This gene encodes a member of the transforming growth factor beta (TGFB) family of cytokines, which are multifunctional peptides that regulate proliferation, differentiation, adhesion, migration, and other functions in many cell types. Many cells have TGFB receptors, and the protein positively and negatively regulates many other growth factors. The secreted protein is cleaved into a latency-associated peptide (LAP) and a mature TGFB1 peptide, and is found in either a latent form composed of a TGFB1 homodimer, a LAP homodimer, and a latent TGFB1-binding protein, or in an active form composed of a TGFB1 homodimer. The mature peptide may also form heterodimers with other TGFB family members. This gene is frequently upregulated in tumor cells, and mutations in this gene result in Camurati-Engelmann disease.[provided by RefSeq, Oct 2009]