Anti-TGF beta Receptor II/TGFBR2 Antibody Picoband® Fluoro488 Conjugated

TGFBR2 (transforming growth factor, beta receptor II (70/80kDa) ), also known as TGF-beta receptor type-2, TGFR-2, TGF-beta type II receptor, Transforming growth factor-beta receptor type II (TGF-beta receptor type II, TbetaR-II), is a member of the Ser/Thr protein kinase family and the TGFB receptor subfamily. A TGFBR2 cDNA encodes a deduced 565-amino acid protein with a calculated molecular mass of approximately 60 kD in length. The encoded protein is a transmembrane protein that has a protein kinase domain, forms a heterodimeric complex with another receptor protein, and binds TGF-beta. This receptor/ligand complex phosphorylates proteins, which then enter the nucleus and regulate the transcription of a subset of genes related to cell proliferation. Mutations in this gene have been associated with Marfan syndrome, Loeys-Deitz aortic aneurysm syndrome, Osler-Weber-Rendu syndrome, and the development of various types of tumors. Alternatively spliced transcript variants encoding different informs have been characterized.

TGF-beta receptor type-2; TGFR-2;2.7.11.30; TGF-beta type II receptor; Transforming growth factor-beta receptor type II; TGF-beta receptor type II; TbetaR-II; TGFBR2

A synthetic peptide corresponding to a sequence at the N-terminus of human TGFBR2, different from the related mouse sequence by five amino acids, and from the related rat sequence by eight amino acids.

Transmembrane serine/threonine kinase forming with the TGF-beta type I serine/threonine kinase receptor, TGFBR1, 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 TGFRB1 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. .

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