Rat TGFBR2 Protein (Cytokine)

Transforming growth factor, beta receptor II Protein Datasheet

TGFBR2 / TGFβR2 / TGFR2 Protein Product Information

• Synonym: TGFBR2
• Protein Construction: A DNA sequence encoding the rat TGFBR2 (P38438) (Met1-Gln166) was expressed, fused with the Fc region of human IgG1 at the C-terminus.
• Source: Rat
• Expression Host: Human Cells

TGFBR2 / TGFβR2 / TGFR2 Protein QC Testing

• Purity: > 95% as determined by SDS-PAGE
• Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method
• Stability: Samples are stable for up to twelve months from date of receipt at -70℃
• Predicted N terminal: Ile 24
• Molecular Mass: The recombinant rat TGFBR2/Fc is a disulfide-linked homodimer. The reduced monomer comprises 384 amino acids and has a predicted molecular mass of 43 kDa. The apparent molecular mass of the protein is approximately 54 kDa in SDS-PAGE under reducing conditions.
• Formulation: Lyophilized from sterile PBS, pH7.4.
  1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
  2. Please contact us for any concerns or special requirements.
• SDS-PAGE: TGFBR2 / TGFβR2 / TGFR2 protein

TGFBR2 / TGFβR2 / TGFR2 Protein Usage Guide

• Storage: Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
• Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

TGFBR2 / TGFβR2 / TGFR2 Protein Description

The type I I receptor for transforming growth factor-beta (TGFβ R2) is a member of the serine/threonine protein kinase family and the TGF-β receptor subfamily. This membrane-bound glyvoprotein contains a cysteine-rich extracellular domain, a single hydrophobic transmembrane domain, and a cytoplasmic serine/threonine kinase domain. TGFR2 binds TGF-β1 and TGF-β3 with high affinity and TGF-β2 with a much lower affinity. This type I I receptor forms a heterodimeric complex with type I  receptor and is essential for signal transduction. Upon ligand binding, the TGFR2 autophosphorylates its cytoplasmic domain and subsequently phosphorylates the downstream molecules which then enter the nucleus and regulate the transcription of a subset of genes related to cell proliferation. It has been shown that TGFR2 kinase is regulated intricately by autophosphorylation on different serine residues and affects signal transduction both positively and negatively. Aberrant expression or mutation of this gene is associated with tumorogenesis and progression, as well as the Marfan Syndrome and Loeys-Deitz Aortic Aneurysm Syndrome.

References

1. G Lin, H.Y. et al., 1992, Cell. 68: 775-785.
2. Lawler, S. et al., 1997, J. Biol. Chem. 272: 14850-14859.
3. Luo, K. et al., 1997, EMBO. J. 16: 1970-1981.
4. Moustakas, A. et al., 2001, J. Cell. Sci. 114: 4359-4369.
5. Law, C. et al., 2006, J. Med. Genet. 43: 908-916.