| Reactivity | MuSpecies Glossary |
| Applications | Bioactivity |
| Format | Carrier-Free |
| Details of Functionality | Measured by its ability to inhibit TGF-beta 1 activity on HT‑2 mouse T cells. Tsang, M. et al. (1995) Cytokine 7:389. The ED50 for this effect is 10-70 ng/mL. |
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| Source | Mouse myeloma cell line, NS0-derived mouse TGF-beta RII protein
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| Accession # | |||||||
| N-terminal Sequence | Ile24 |
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| Structure / Form | Disulfide-linked homodimer |
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| Protein/Peptide Type | Recombinant Proteins |
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| Gene | Tgfbr2 |
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| Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
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| Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
| Dilutions |
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| Theoretical MW | 44.6 kDa (monomer). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
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| SDS-PAGE | 60-65 kDa, reducing conditions |
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| Publications |
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| Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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| Buffer | Lyophilized from a 0.2 μm filtered solution in PBS. |
| Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
| Reconstitution Instructions | Reconstitute at 100 μg/mL in sterile PBS. |
Most cell types express three sizes of receptors for TGF-beta . These are designated Type I (53 kDa), Type II (70 - 85 kDa), and Type III (250 - 350 kDa). The Type III receptor, a proteoglycan that exists in membrane-bound and soluble forms, binds TGF-beta 1, TGF-beta 2, and TGF-beta 3 but does not appear to be involved in signal transduction. The Type II receptor is a membrane-bound serine/threonine kinase that binds TGF-beta 1 and TGF-beta 3 with high affinity and TGF-beta 2 with a much lower affinity. The Type I receptor is also a membrane-bound serine/threonine kinase that apparently requires the presence of the Type II receptor to bind TGF-beta . Current evidence suggests that signal transduction requires the cytoplasmic domains of both the Type I and Type II receptors.
The recombinant soluble TGF-beta Type II receptor is capable of binding TGF-beta 1, TGF-beta 3, and TGF-beta 5 with sufficient affinity to act as an inhibitor of these isoforms at high concentrations. The soluble receptor also binds TGF-beta 2, but with an affinity at least two orders of magnitude lower. Binding of TGF-beta 1, TGF-beta 3, and TGF-beta 5 to the soluble TGF-beta Type II receptor can also be demonstrated by using the soluble receptor as a capture agent on ELISA plates and this observation has been used as the basis for the development of immunoassays for these isoforms of TGF-beta .
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