TGFBR1/ALK-5 Protein, Human (HEK293, Fc)

TGFBR1/ALK-5 proteins cooperate with TGFBR2 to form dedicated receptors for TGFB1, TGFB2, and TGFB3, transmitting signals and coordinating different physiological and pathological processes. It induces cell cycle arrest, modulates mesenchymal cell dynamics, contributes to wound healing, and affects immunosuppression and carcinogenesis. TGFBR1/ALK-5 Protein, Human (HEK293, Fc) is the recombinant human-derived TGFBR1/ALK-5 protein, expressed by HEK293 , with C-hFc labeled tag.

The transmembrane serine/threonine kinase, TGFBR1 (ALK-5), collaborates with the TGF-beta type II serine/threonine kinase receptor, TGFBR2, to form the dedicated receptor for TGF-beta cytokines, including TGFB1, TGFB2, and TGFB3. Serving as a signal transducer, TGFBR1 mediates the transmission of TGFB1, TGFB2, and TGFB3 signals from the cell surface to the cytoplasm, thereby orchestrating a diverse array of physiological and pathological processes. These include cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression, and carcinogenesis. The receptor complex, composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer, leads to the phosphorylation and activation of TGFBR1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2, causing its dissociation from the receptor and interaction with SMAD4. The resulting SMAD2-SMAD4 complex translocates to the nucleus, where it modulates the transcription of TGF-beta-regulated genes, constituting the canonical SMAD-dependent TGF-beta signaling cascade. Additionally, TGFBR1 is involved in non-canonical, SMAD-independent TGF-beta signaling pathways. For instance, it induces TRAF6 autoubiquitination, leading to MAP3K7 ubiquitination and activation, triggering apoptosis. TGFBR1 also regulates epithelial to mesenchymal transition through a SMAD-independent signaling pathway involving PARD6A phosphorylation and activation.

1.This product does not contain protein kinase domain.
2.Measured by its binding ability in a functional ELISA. When Recombinant Human TGF-beta RII is immobilized at 1 μg/mL (100 μL/well), it binds Recombinant Human TGF-beta RI in the presence of TGF-beta 1. The concentration of rhTGF-beta RI that produces 50% of the optimal binding response is approximately 1.278 μg/mL.

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  Measured by its binding ability in a functional ELISA. When Recombinant Human TGF-beta RII is immobilized at 1 μg/mL (100 μL/well), it binds Recombinant Human TGF-beta RI in the presence of TGF-beta 1. The concentration of rhTGF-beta RI that produces 50% of the optimal binding response is approximately 1.278 μg/mL.

Human

HEK293

C-hFc

P36897-1 (L34-E125)

7046  [NCBI]

Extracellular Domain

LQCFCHLCTKDNFTCVTDGLCFVSVTETTDKVIHNSMCIAEIDLIPRDRPFVCAPSSKTGSVTTTYCCNQDHCNKIELPTTVKSSPGLGPVE

Approximately 38-58 kDa, based on SDS-PAGE under reducing conditions.

≥ 95%, as determined by reducing SDS-PAGE.

Lyophilized powder.

Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.