tgf-β receptor

TGFBR2 Protein, Mouse, Recombinant (aa 24-159, hFc) is expressed in HEK293 mammalian cells with C-Fc tag. The predicted molecular weight is 55-65 KDa and the accession number is Q62312-2.

TGFBR2 Protein, Mouse, Recombinant (aa 24-184, hFc) is expressed in HEK293 mammalian cells with C-Fc tag. The predicted molecular weight is 60-75 KDa and the accession number is Q62312.

GDNF family receptor alpha-2 is a glycosylphosphatidylinosito l (GPI)-linked cell surface receptor. It is part of the GDNF receptor family. Glial cell line-derived neurotrophic factor (GDNF) and neurturin (NTN) are two structurally related, potent neurotrophic factors that play key roles in the control of neuron survival and differentiation. GFRA2 mediates the NRTN-induced autophosphorylation and activation of the RET receptor. It also able to mediate GDNF signaling through the RET tyrosine kinase receptor. It acts preferentially as a receptor for NTN compared to its other family member, GDNF family receptor alpha 1.

TGFBR2 Protein, Mouse, Recombinant (His) is expressed in HEK293 mammalian cells with C-6xHis tag. The predicted molecular weight is 25-38 KDa and the accession number is Q62312-2.

TGF-beta RI, also called ALK-5, is an approximately 55 kDa type I transmembrane serine/threonine receptor kinase. In the presence of TGF-beta, TGF-beta RI forms a complex with, and is phosphorylated by, TGF-beta RII. Phosphorylated TGF-beta RI can then transiently bind and phosphorylate Smad2 and Smad3. TGF-beta functions as a tumor suppressor by inhibiting the cell cycle in the G1 phase. Administration of TGF-beta is able to protect against mammary tumor development in transgenic mouse models in vivo. Disruption of the TGF-beta/SMAD pathway has been implicated in a variety of human cancers, with the majority of colon and gastric cancers being caused by an inactivating mutation of TGF-beta RII. TGF-beta RI is likely important during development, since mice deficient for TGF-beta RI die at midgestation with severe defects in vascular development of the yolk sac and placenta, and an absence of circulating red blood cells. Furthermore, TGF-beta RI appears to be involved in proper lymphatic network development.

The TGFBR2 gene provides instructions for making a protein called transforming growth factor-beta (TGF-β) receptor type 2. This receptor transmits signals from the cell surface into the cell through a process called signal transduction. Through this type of signaling, the environment outside the cell affects activities inside the cell such as stimulation of cell growth and division. TGFBR2 Protein, Human, Recombinant (mFc & Avi), Biotinylated is expressed in HEK293 mammalian cells with C-mFc-Avi tag. The predicted molecular weight is 44 kDa and the accession number is P37173-1.

Left-right determination factor 2(LEFTY2) is a secreted protein which belongs to the TGF-beta family. Lefty was first identified in a screen for undifferentiated cell-specific cDNAs from the P19 mouse embryonal carcinoma cells. Its mRNA expression on the left side of the developing embryo earned the name “Lefty”. The human orthologue was initially identified as Ebaf, Endometrial bleeding associated factor. Lefty contains the six cysteine residues that are conserved among TGF-β related proteins and that are necessary to form the cysteineknot structure. Its function in patterning left-right asymmetry of the developing organ systems such as the heart and lung is consistent in all vertebrate species examined. Lefty acts as an antagonist to Nodal signaling, potentially by competing for binding to a common receptor. It may play a role in endometrial bleeding.

Platelet-derived growth factor receptor (PDGFR) signaling is involved in proliferation and survival in a wide array of cell types.PDGFR-β signalling, via TGF-β signalling, may be crucial for restoration of BBB integrity after cerebral ischemia and therefore represents a novel potential therapeutic target.

Activin Receptor-Like Kinase 1 (ALK-1) is a type I cell-surface receptor for the TGF-β superfamily of ligands, which mediates signaling of BMP9 (bone morphogenetic protein) and BMP10. ALK1 signaling is necessary for angiogenesis during embryogenesis, wound healing, and tumor growth. ALK-1 has a high degree of similarity in serine-threonine kinase subdomains, a glycine and serine rich region preceding the kinase-domain, and a C-terminal tail with other activin receptor-like kinase proteins. ALK-1 is mainly expressed in endothelial cells regulating proliferation and migration in vitro and angiogenesis in vivo. Mutations in ALK-1 as well as in endoglin are associated with hereditary hemorrhagic telangiectasia (HHT), suggesting ALK-1 plays a critical role for in the control of blood vessel development or repair.

Activin proteins that belong to the transforming growth factor-beta (TGF-β) superfamily, exert their biological actions by binding to heteromeric receptor complexes of type I and type II serine/threonine kinase receptors. On ligand binding, type I and II receptors form a stable complex, resulting in phosphorylation of type I receptors by type II receptors with constitutive kinase activity, and subsequently initiates the activation of downstream molecules including the endogenous Smads. ActRIIB, also known as ActRIIB, is a type II receptor containing an extracellular domain (ECD), a transmembrane segment, and a cytoplasmic region that includes the kinase domain. ActRIIB is a receptor for activin A, activin B and inhibin A. Multiple ActRIIB isoforms can also be generated, which bind activin isoforms with different affinities.

Dickkopf-related protein 1 (DKK-1), a ligand for the WNT coreceptors low-density lipoprotein receptor-related proteins 5 and 6 (LRP-5 and LRP-6) and an inhibitor of WNT/β-catenin signaling, effectively inhibits pericyte activation, detachment, and transition to myofibroblasts in vivo in response to kidney injury, resulting in attenuated fibrogenesis, capillary rarefaction, and inflammation.LRP-6 interacts closely with PDGF receptor β and TGF-β receptor 1 at the cell membrane, suggesting that it may have roles in pathways other than WNT/β-catenin.

Human Artemin is a GDNF family ligand that is distantly related to the TGF-β superfamily of molecules. It is synthesized as a preproprotein, and contains a variable length pre-, or signal sequence, plus a 68 amino acid (aa) proregion and a 113 aa mature segment. Following synthesis and proteolytic processing, mature ARTN is secreted as a presumably glycosylated, 28 kDa disulfide-linked homodimer that contains three intrachain disulfide bonds and the typical TGF-β signature cysteine-knot motif. In the mature region, human ARTN is 89% and 88% aa identical to rat and mouse ARTN, respectively. Human ARTN is active on rodent cells. The receptor for ARTN has been identified as the ligand binding subunit GFRα-3 plus the signal transducing subunit, RET. The GFRα-1/RET receptor complex has also been suggested to be a ligand binding unit for ARTN. ARTN is known to be a chemoattractant for sympathetic neuron axons innervating the developing cardiovascular system. It also promotes sensory neuron survival and likely plays a role in the development of the peripheral nervous system. Finally, it has been reported to reverse neuropathic pain due to nerve injury, and to help resolve morphological changes associated with nerve damage.

Transforming growth factor beta 1 (TGFβ1) is the prototype of a growing superfamily of peptide growth factors and plays a prominent role in a variety of cellular processes, including cell-cycle progression, cell differentiation, reproductive function, development, motility, adhesion, neuronal growth, bone morphogenesis, wound healing, and immune surveillance. TGF-β1, TGF-β2 and TGF-β3 signal via the same heteromeric receptor complex, consisting of a ligand binding TGF-β receptor type II (TβR-II), and a TGF-β receptor type I (TβR-I). Signal transduction from the receptor to the nucleus is mediated via SMADs. TGF-β expression is found in cartilage, bone, teeth, muscle, heart, blood vessels, haematopoitic cells, lung, kidney, gut, liver, eye, ear, skin, and the nervous system.

Persephin is a secreted protein, belongs to the glial cell linederived neurotrophic factor (GDNF) family of the TGF-β superfamily. It shares 38-46% amino acid (aa) identity with family members GDNF, neurturin and artemin. It is expressed at very low levels in most tissues. Mature protein contains a signal sequence, a pro-domain and a 96 aa mature sequence with several cysteines that are conserved among family members. It circulates as an unglycosylated disulfide-linked homodimer. Like other GDNF family members, Persephin acts through engagement of GRFα4, a glycosylphosphatidylinositol (GPI)-linked GDNF receptor family Persephin is reported to promote both the survival and growth of central dopaminergic and motor neurons, and kidney development. These effects are correlated with the expression patterns of GFRα4, and RET.

Neurturin is a member of the GDNF family of ligands, which include glial cell-derived neurotrophic factor (GDNF), Neurturin, Persephin, and Artemin. Neurturin is expressed in both neuronal and nonneuronal tissues. Similarly to other TGFβ family proteins, Neurturin is synthesized as a precursor protein that is cleaved at the dibasic cleavage site (RXXR) to release the carboxyterminal domain. The carboxy terminal domain of Neurturin contains the characteristic seven conserved cysteine residues necessary for the formation of the cysteine-knot and the single interchain disulfide bond. Biologically active human Neurturin is a disulfide-linked homodimer of the carboxy-terminal 102 amino acid residues. Unlike other members of TGF-β family, bioactivities of all GDNF family ligands are mediated through a unique multicomponent receptor complex composed of high affinity ligand binding component (GFRα-1-GFRα-4) and a common signaling component (cRET receptor tyrosine kinase). Each member of the GDNF family ligands has its preferred binding protein. Neurturin preferentially binds to GFRα-2 but can also bind GFRα-1 at higher concentrations. It may play a role in regulating the development and maintenance of the central and peripheral nervous systems and as well as non neuronal systems.

The TGFBR2 gene provides instructions for making a protein called transforming growth factor-beta (TGF-β) receptor type 2. This receptor transmits signals from the cell surface into the cell through a process called signal transduction. Through this type of signaling, the environment outside the cell affects activities inside the cell such as stimulation of cell growth and division. TGFBR2 Protein, Human, Recombinant (mFc & Avi) is expressed in HEK293 mammalian cells with C-mFc-Avi tag. The predicted molecular weight is 44 kDa and the accession number is P37173-1.

Transforming growth factor beta 3(TGFB3) is a member of a TGF -β superfamily which is defined by theirstructural and functional similarities. TGFB3 is secreted as a complex with LAP. This latent form of TGFB3becomes active upon cleavage by plasmin, matrix metalloproteases, thrombospondin -1, and a subset ofintegrins. It binds with high affinity to TGF- β RII, a type II serine/threonine kinase receptor. TGFB3 is involved incell differentiation, embryogenesis and development.It is believed to regulate molecules involved in cellularadhesion and extracellular matrix (ECM) formation during the process of palate development. Without TGF-β3,mammals develop a deformity known as a cleft palate.

Transforming growth factor beta 2 (TGF-β2) is a member of TGF-beta superfamily that shares a characteristic cysteine knot structure. Mice with TGF-β2 gene deletion show defects in development of cardiac, lung, craniofacial, limb, spinal column, eye, inner ear and urogenital systems. All TGF-β isoforms signal via the same heteromeric receptor complex, consisting of a ligand binding TGF-β receptor type II (TβR-II), and a TGF-β receptor type I (TβR-I). Signal transduction from the receptor to the nucleus is mediated via SMADs. TGF-β expression is found in cartilage, bone, teeth, muscle, heart, blood vessels, haematopoitic cells, lung, kidney, gut, liver, eye, ear, skin, and the nervous system.