Recombinant Human TGF-beta receptor type-1 (TGFBR1), partial

Overview

Recombinant Human TGF-beta receptor type-1 (TGFBR1), partial is a recombinant protein reagent derived from Homo sapiens (Human) and produced in E.coli. It is commonly used to support Cancer research by enabling binding assays, assay development and protein–protein interaction studies in controlled in vitro settings.

Key elements and design rationale

• Expressed region: 34-126aa. Region selection can focus on functional domains, improve solubility, or isolate interaction surfaces for targeted studies.
• Expression system: E.coli. Expression host can influence folding and the presence/absence of post-translational modifications.
• Tag / fusion: N-terminal 10xHis-tagged and C-terminal Myc-tagged. Tags can support purification and detection; evaluate potential tag effects when studying sensitive interactions.
• Molecular weight (reported): 17.6 kDa. Apparent size may vary with tags, processing, and gel conditions.

When comparing results across batches or platforms, interpret signals in the context of construct design (region, tags) and expression host, especially for modification-dependent interactions.

Biological background

The gene commonly associated with this target is TGFBR1. TGFBR1 refers to a protein target that is studied across multiple biological contexts; annotations and nomenclature can vary by species and isoform. This product corresponds to the Homo sapiens (Human) sequence context, which can be important when comparing homologs or orthologs across model systems. For curated functional annotations, domains, and sequence features, consult primary databases (e.g., UniProt/NCBI) and the recent literature for the specific organism and isoform.

Research relevance and current trends

• Mapping pathway dependencies and signaling networks that drive tumor growth and drug resistance.
• Developing and benchmarking biomarker assays (e.g., immunoassays or binding reagents) for candidate targets.
• Characterizing protein variants, domains, or interaction partners relevant to targeted therapeutics and precision oncology.

Relevance: Transmembrane serine/threonine kinase forming with the TGF-beta type II serine/threonine kinase receptor, TGFBR2, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and the activation of TGFBR1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non-canonical, SMAD-independent TGF-beta signaling pathways. For instance, TGFBR1 induces TRAF6 autoubiquitination which in turn results in MAP3K7 ubiquitination and activation to trigger apoptosis. Also regulates epithelial to mesenchymal transition through a SMAD-independent signaling pathway through PARD6A phosphorylation and activation.

Common research applications

• Assay and standard development for immunoassays or binding-based detection methods.
• Protein–protein interaction studies (e.g., receptor–ligand or complex assembly) using purified components.
• Structure–function analysis, including domain mapping or evaluation of sequence variants.

In quantitative assay development, changes in binding or activity readouts are typically interpreted relative to appropriate negative/positive controls and, where possible, orthogonal assay formats that support the same conclusion.

Notes for experimental interpretation

• Recombinant constructs may represent a defined region (domain) rather than the full-length protein; interpret results in the context of the expressed region.
• Tag or fusion elements can aid purification and detection but may influence binding surfaces or oligomerization; consider tag controls when relevant.
• Species and isoform differences can affect interaction partners and post-translational modifications; align experimental controls to the intended biological context.
• E. coli expression can limit eukaryotic post-translational modifications; for modification-dependent biology, interpret results accordingly.

• Datasheet (12933533)
• MSDS (12933533)

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