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Description: Mouse TGF beta 1 (Transforming Growth Factor beta 1) is a member of a superfamily of homologous, disulfide-linked, homodimeric proteins that regulate the proliferation and differentiation of normal and transformed cells. Human TGF beta 1 is a 25 kDa protein with each subunit containing 112 aa residues. TGF beta 1 is secreted from the many cell types in a complex with LAP (Latency Associated Peptide) and also with LTBP (latent TGF beta binding protein). Disassociation is thought to happen in the extracellular matrix via proteases and/or integrins. Regulatory T cells are a recently identified source of TGF beta 1 thought to be a key player in their suppressive functions. TGF beta 1 binds through TGF beta receptors (of which there is a large family). The protein is highly conserved across all mammalian species.
Applications Reported: Recombinant mouse TGF- beta 1 is biologically active and can inhibit IL-4 induced proliferation of mouse HT-2 cells.
Applications Tested: The ED50 of this protein, as measured by inhibition of IL-4 induced proliferation in HT-2 cells, is less than or equal to 40 pg/mL. This corresponds to a specific activity of greater than or equal to 2.5 x 10e7 Units/mg.
Bioactivity: The ED50 of this protein, as measured by inhibition of IL-4 induced proliferation in HT-2 cells, is less than or equal to 40 pg/mL. This corresponds to a specific activity of greater than or equal to 2.5 x 10e7 units/mg.
Endotoxin: Less than 0.01 ng/ug cytokine as determined by the LAL assay. Purity: >95% as determined by SDS-PAGE.
Molecular Weight: Mature TGFb1 polypeptide has a predicted molecular mass of 12,794. On reducing SDS-PAGE the protein migrates as a 13 kDa polypeptide and on non-reducing SDS page the cystine-linked homodimer migrates as a 25 kDa protein.
Storage and handling: For best recovery, quick-spin vial prior to opening. Use in a sterile environment.
Purity: Greater than 90%, as determined by SDS-PAGE.
Aggregation: Less than 10%, as determined by HPLC.
Filtration: 0.2 µm post-manufacturing filtered.
TGF beta-1 (TGFB1, Transforming Growth Factor Beta 1) is a polypeptide member of the transforming growth factor beta superfamily of cytokines, found almost ubiquitously in tissues. Transforming growth factor (TGF)-b is stored in the extracellular matrix as a latent complex with its pro-domain. Activation of TGF beta-1 requires the binding of aV integrin to an RGD sequence in the prodomain and exertion of force on this domain, which is held in the extracellular matrix by latent TGF-b binding proteins. Latent forms are complexes of TGF beta-1, an amino-terminal portion of the TGF-beta precursor, designated TGF-LAP (TGF-latency associated peptide), and a specific binding protein, known as LTBP. TGF beta-1 helps regulates proliferation, differentiation, adhesion, migration in many cell types. Many cells have TGF beta receptors, and the protein positively and negatively regulates many other growth factors. TGF beta-1 is cleaved into a latency-associated peptide and a mature TGF beta-1 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 TGF beta-1 homodimer. The mature peptide may also form heterodimers with other TGF beta family members. The gene for TGF beta-1 is frequently upregulated in tumor cells, and mutations in this gene result in Camurati-Engelmann disease and cystic fibrosis.
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