Analytical Data
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Gene name
TGFbR2
- Application
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Alternative Names
MFS2
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P37173
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Expression Region
Thr23~Gln166
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Molecular Weight
22kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
Transforming Growth Factor Beta Receptor II (TGFβR2) is a critical component of the TGF-β signaling pathway, which plays a significant role in various cellular processes, including cell growth, differentiation, and apoptosis. Dysregulation of this pathway has been implicated in numerous diseases, particularly in cancer and fibrotic disorders. TGFβR2 exists as a transmembrane receptor that, upon binding with TGF-β, forms heteromeric complexes with TGFβR1, initiating a cascade of intracellular signaling events. The study of recombinant TGFβR2 proteins is vital for understanding the receptor's structure-function relationship and its role in disease. Researchers produce recombinant TGFβR2 to investigate its signaling mechanisms, explore potential therapeutic targets, and develop novel drugs that may inhibit aberrant TGF-β signaling. Additionally, these proteins are invaluable tools in basic research, allowing scientists to elucidate the biochemical properties of the receptor and its interactions with other proteins. Ongoing research focuses on the structural characterization of TGFβR2, its ligand-binding properties, and the specific pathways that mediate its effects in various pathological contexts. Given its central role in cell signaling, TGFβR2 continues to be a focal point in drug discovery efforts aimed at treating cancer and fibrotic diseases, highlighting the importance of understanding this receptor at a molecular level.
