Reactivity | HuSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Details of Functionality | When
Recombinant Human TGF-beta 1
(Catalog #
7754-BH) is
immobilized at 0.2 µg/mL (100 µL/well), Biotinylated Recombinant Human TGF-beta RII Fc Chimera Avi-tag (Catalog # AVI341) binds with an ED50
of 0.2-1.6 ng/mL. |
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Source | Human embryonic kidney cell, HEK293-derived human TGF-beta RII protein
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Accession # | |||||||||
N-terminal Sequence | Thr23 |
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Structure / Form | Biotinylated via Avi-tag. |
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Protein/Peptide Type | Recombinant Proteins |
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Purity | >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
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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 kDa. 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. |
SDS-PAGE | 56-72 kDa, under reducing conditions. |
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 with Trehalose. |
Purity | >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions | Reconstitute at 250 μg/mL in 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 . Our Avi-tag Biotinylated TGF-beta RII Fc Chimera features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.
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Uniprot |
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