tgf-β 1

TGF beta 1 Protein, Rat Mouse, Recombinant is expressed in HEK293 mammalian cells. The predicted molecular weight is 12.8 kDa.

Transforming growth factor beta-2 (TGF-β2) is a secreted protein which belongs to the TGF-beta family. It is known as a cytokine that performs many cellular functions and has a vital role during embryonic development. The precursor is cleaved into mature TGF-beta-2 and LAP, which remains non-covalently linked to mature TGF-beta-2 rendering it inactive. It is an extracellular glycosylated protein. It is known to suppress the effects of interleukin dependent T-cell tumors. Defects in TGFB2 may be a cause of non-syndromic aortic disease (NSAD).

Growth and differentiation factor 15 (GDF15) is an inflammation-associated hormone with poorly defined biology. Here, we investigated the role of GDF15 in bacterial and viral infections. Inflammation induced GDF15, and that GDF15 was necessary for surviving both bacterial and viral infections, as well as sepsis. The protective effects of GDF15 were largely independent of pathogen control or the magnitude of inflammatory response, suggesting a role in disease tolerance. GDF-15 Protein, Mouse, Recombinant (hFc) is expressed in HEK293 mammalian cells with N-hFc tag. The predicted molecular weight is 37.9 kDa and the accession number is Q9Z0J7.

Latent TGF beta 1 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 42.4 kDa and the accession number is A0A499FJK2.

TGF beta 1 Protein, Human Rhesus Cynomolgus Canine, Recombinant is expressed in CHO mammalian cells. The predicted molecular weight is 12.8 kDa and the accession number is A0A499FJK2.

Latent TGF beta 1 Protein, Rat, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 42.7 kDa and the accession number is P17246.

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 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.

Latent TGF beta 1 Protein, Mouse, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 42.7 kDa and the accession number is P04202.

Bone morphogenetic protein 7 (BMP7), also known as osteogenic protein-1 (OP-1) is a member of Transforming growth factor-β (TGF-β) family of proteins. Bone morphogenetic proteins were discovered in 1965 by Marshal Urist, of which BMP7 is of particular interest in this review being a leptin-independent anorexinogen and having role in energy expenditure in the brown adipose tissue, which makes it a potential target for preventing treating obesity. As it has been established that Obesity displays a state of leptin-resistance, thus a protein-like BMP7 which acts through a leptin-independent pathway could give new therapeutic directions.

Latent TGF-beta 1 Protein, Mouse, Recombinant (His & Avi), Biotinylated is expressed in HEK293 mammalian cells with N-8xHis-Avi tag. The predicted molecular weight is 13 and 35-45 KDa and the accession number is P04202.

Transforming Growth Factor β-1 (TGFβ-1) is a secreted protein which belongs to the TGF-β family. TGFβ-1 is abundantly expressed in bone, articular cartilage and chondrocytes and is increased in osteoarthritis (OA). TGFβ-1 performs many cellular functions, including the control of cell growth, cell proliferation, cell differentiation and apoptosis. The precursor is cleaved into a latency-associated peptide (LAP) and a mature TGFβ-1 peptide. TGFβ-1 may also form heterodimers with other TGFβ family members. It has been found that TGFβ-1 is frequently upregulated in tumor cells. Mutations in this gene results in Camurati-Engelmann disease.

Transforming growth factor beta (TGFβ) family members are secreted in inactive complexes with a latency-associated peptide (LAP), a protein derived from the N-terminal region of the TGFβ gene product. Extracellular activation of these complexes is a critical step in regulation of TGFβ function in vivo. The TGFβ1 LAP is a ligand for the integrin αvβ6 and that αvβ6-expressing cells induce spatially restricted activition of TGFβ1. And LAP identifies a novel CD4+ CD25+ regulatory T cell subset with TGFbeta-mediated function and enhanced suppression of experimental autoimmune encephalomyelitis.

Latent TGF-beta 1 Protein, Cynomolgus, Recombinant (His) is expressed in HEK293 mammalian cells with N-6xHis tag. The predicted molecular weight is 11 and 35-45 KDa and the accession number is F7HCV5.

Latent TGF beta 1 Protein, Cynomolgus, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 42.7 kDa.

Latent TGF beta 1 Protein, Human, Recombinant (His), Biotinylated is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 42.4 kDa and the accession number is A0A499FJK2.

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.

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.

Growth and differentiation factor 15 (GDF15) is an inflammation-associated hormone with poorly defined biology. Here, we investigated the role of GDF15 in bacterial and viral infections. Inflammation induced GDF15, and that GDF15 was necessary for surviving both bacterial and viral infections, as well as sepsis. The protective effects of GDF15 were largely independent of pathogen control or the magnitude of inflammatory response, suggesting a role in disease tolerance. GDF-15 Protein (Primary Amine Labeling), Human, Recombinant (H202D, hFc), Biotinylated is expressed in HEK293 mammalian cells with N-hFc tag. The predicted molecular weight is 37.88 kDa and the accession number is Q99988.

Growth and differentiation factor 15 (GDF15) is an inflammation-associated hormone with poorly defined biology. Here, we investigated the role of GDF15 in bacterial and viral infections. Inflammation induced GDF15, and that GDF15 was necessary for surviving both bacterial and viral infections, as well as sepsis. The protective effects of GDF15 were largely independent of pathogen control or the magnitude of inflammatory response, suggesting a role in disease tolerance. GDF-15 Protein, Cynomolgus, Recombinant (hFc) is expressed in HEK293 mammalian cells with N-hFc tag. The predicted molecular weight is 37.9 kDa and the accession number is G7PWZ3.

Growth and differentiation factor 15 (GDF15) is an inflammation-associated hormone with poorly defined biology. Here, we investigated the role of GDF15 in bacterial and viral infections. Inflammation induced GDF15, and that GDF15 was necessary for surviving both bacterial and viral infections, as well as sepsis. The protective effects of GDF15 were largely independent of pathogen control or the magnitude of inflammatory response, suggesting a role in disease tolerance. GDF-15 Protein, Cynomolgus, Recombinant (His) is expressed in E. coli expression system with N-His tag. The predicted molecular weight is 14.15 kDa and the accession number is G7PWZ3.

Growth and differentiation factor 15 (GDF15) is an inflammation-associated hormone with poorly defined biology. Here, we investigated the role of GDF15 in bacterial and viral infections. Inflammation induced GDF15, and that GDF15 was necessary for surviving both bacterial and viral infections, as well as sepsis. The protective effects of GDF15 were largely independent of pathogen control or the magnitude of inflammatory response, suggesting a role in disease tolerance. GDF-15 Protein (Primary Amine Labeling), Mouse, Recombinant (hFc), Biotinylated is expressed in HEK293 mammalian cells with N-hFc tag. The predicted molecular weight is 37.9 kDa and the accession number is Q9Z0J7.

Latent TGF beta 1 Protein, Canine, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 43.4 kDa.

Growth Differentiation Factor 15 (GDF15), also known as NSAID activated gene-1 (NAG-1), is associated with a large number of biological processes and diseases, including cancer and obesity. GDF15 is synthesized as pro-GDF15, is dimerized, and is cleaved and secreted into the circulation as a mature dimer GDF15. GDF-15 Protein, Rat, Recombinant (His) is expressed in E. coli expression system with N-His tag. The predicted molecular weight is 13.68 kDa and the accession number is Q9Z0J6.

Growth and differentiation factor 15 (GDF15) is an inflammation-associated hormone with poorly defined biology. Here, we investigated the role of GDF15 in bacterial and viral infections. Inflammation induced GDF15, and that GDF15 was necessary for surviving both bacterial and viral infections, as well as sepsis. The protective effects of GDF15 were largely independent of pathogen control or the magnitude of inflammatory response, suggesting a role in disease tolerance. GDF-15 Protein, Mouse, Recombinant (His) is expressed in E. coli expression system with N-His tag. The predicted molecular weight is 13.78 kDa and the accession number is Q9Z0J7.

Growth and differentiation factor 15 (GDF15) is an inflammation-associated hormone with poorly defined biology. Here, we investigated the role of GDF15 in bacterial and viral infections. Inflammation induced GDF15, and that GDF15 was necessary for surviving both bacterial and viral infections, as well as sepsis. The protective effects of GDF15 were largely independent of pathogen control or the magnitude of inflammatory response, suggesting a role in disease tolerance. GDF-15 Protein (Primary Amine Labeling), Human, Recombinant (hFc), Biotinylated is expressed in HEK293 mammalian cells with N-hFc tag. The predicted molecular weight is 37.9 kDa and the accession number is Q99988.

Growth and differentiation factor 15 (GDF15) is an inflammation-associated hormone with poorly defined biology. Here, we investigated the role of GDF15 in bacterial and viral infections. Inflammation induced GDF15, and that GDF15 was necessary for surviving both bacterial and viral infections, as well as sepsis. The protective effects of GDF15 were largely independent of pathogen control or the magnitude of inflammatory response, suggesting a role in disease tolerance. GDF-15 Protein (Primary Amine Labeling), Cynomolgus, Recombinant (hFc), Biotinylated is expressed in HEK293 mammalian cells with N-hFc tag. The predicted molecular weight is 37.9 kDa and the accession number is G7PWZ3.

Latent TGF beta 1 Protein, Mouse, Recombinant (His), Biotinylated is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 42.7 kDa and the accession number is P04202.

Growth Differentiation Factor 15 (GDF15), also known as NSAID activated gene-1 (NAG-1), is associated with a large number of biological processes and diseases, including cancer and obesity. GDF15 is synthesized as pro-GDF15, is dimerized, and is cleaved and secreted into the circulation as a mature dimer GDF15. GDF-15 Protein, Human, Recombinant (His & Avi), Biotinylated is expressed in E. coli expression system with N-His-Avi tag. The predicted molecular weight is 15.19 kDa and the accession number is Q99988-1.

Growth Differentiation Factor 15 (GDF15), also known as NSAID activated gene-1 (NAG-1), is associated with a large number of biological processes and diseases, including cancer and obesity. GDF15 is synthesized as pro-GDF15, is dimerized, and is cleaved and secreted into the circulation as a mature dimer GDF15. GDF-15 Protein, Canine, Recombinant (His) is expressed in E. coli expression system with N-His tag. The predicted molecular weight is 13.12 kDa and the accession number is A0A8C0TNP6.

transforming growth factor beta receptor 1 (TGFBR1), a key stimulator of tumor proliferation and metastasis, was a direct target of miR‑98‑5p. miR‑98‑5p overexpression resulted in the downregulation of TGFBR1 and the suppression of the viability, proliferation, migration and invasion of A549 and H1299 cells. TGFBR1 Protein, Human, Recombinant (mFc & Avi) is expressed in HEK293 mammalian cells with C-mFc-Avi tag. The predicted molecular weight is 38.2 kDa and the accession number is P36897-1.

transforming growth factor beta receptor 1 (TGFBR1), a key stimulator of tumor proliferation and metastasis, was a direct target of miR‑98‑5p. miR‑98‑5p overexpression resulted in the downregulation of TGFBR1 and the suppression of the viability, proliferation, migration and invasion of A549 and H1299 cells. TGFBR1 Protein, Human, Recombinant (mFc & Avi), Biotinylated is expressed in HEK293 mammalian cells with C-mFc-Avi tag. The predicted molecular weight is 38.2 kDa and the accession number is P36897-1.

TGF-beta 1 Protein, Bovine, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 16.8 kDa and the accession number is P18341.

Latent TGF beta 1 & GARP Heterotrimer Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 108.72 kDa and the accession number is P01137.

TGF-beta 1 Protein, Chicken, Recombinant (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 29.0 kDa and the accession number is P09531.

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.

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.

Bone Morphogenetic Protein 5 (BMP-5) is a member of the structurally and functionally related bone morphogenetic proteins (BMPs) which constitute a novel subfamily of the transforming growth factor β (TGF-β) superfamily. In agreement with a possible role in the control of cell death, BMP-5 exhibited a regulated pattern of expression in the interdigital tissue. Transcripts of BMP-5 and BMP-5 protein were abundant within the cytoplasm of the fragmenting apoptotic interdigital cells in a way suggesting that delivery of BMPs into the tissue is potentiated during apoptosis. Gain-of-function experiments demonstrated that BMP-5 has the same effect as other interdigital BMPs inducing apoptosis in the undifferentiated mesoderm and growth in the prechondrogenic mesenchyme. BMP-5 is a member of the 60A subgroup of BMPs, other members of which have been shown to stimulate dendritic growth in central and peripheral neurons. The signaling pathway that mediates the dendrite-promoting activity of BMP-5 may involve binding to BMPR-IA and activation of Smad-1, and relative levels of BMP antagonists such as noggin and follistatin may modulate BMP-5 signaling. Since BMP-5 is expressed at relatively high levels not only in the developing but also the adult nervous system, these findings suggest the possibility that BMP-5 regulates dendritic morphology not only in the developing but also the adult nervous system. BMP-5 may play important roles not only in myocardial differentiation but also in the formation and maintenance of endocardial cushion tissue. Additionally, a high expression level of BMP-5 has been detected in certain tumors of mesenchymal origin.

Mast Cell Protease 1 (MMCP-1), also known as MCP-1, MCPT-1 and β-chymase, is a member of the Chymase family of chymotrypsin-like serine proteases. MCPT-1 is a 26 kDa β-chymase that is a component of mast cell granules. It is a 226 amino acid (aa) protein that has a conserved pattern of six cysteines and one potential glycosylation site. The granule-derived mouse mast cell proteases-1 and -2 (mMCP-1 and -2) colocalize in similar quantities in mucosal mast cells but micrograms of mMCP-1 compared with nanograms of mMCP-2 are detected in peripheral blood during intestinal nematode infection. mMCP-1 isolated from serum is complexed with serpins and both the accumulation and the longevity of mMCP-1 in the blood is due to complex formation, protecting it from a pathway that rapidly clears mMCP-2, which is unable to form complexes with serpins. The mucosal mast cell (MMC) granule-specific beta-chymase, mouse mast cell protease-1 (mMCP-1), is released systemically into the bloodstream early in nematode infection before parasite-specific IgE responses develop and TGF-beta1 induces the constitutive release of mMCP-1 by homologs of MMC in vitro. Expression of mMCP-1 is largely restricted to intraepithelial MMC and is thought to play a role in the regulation of epithelial permeability. Its activation is completed by the removal of a two residue N-terminal propeptide by a dipeptidyl peptidase (Cathepsin C). MCPT-1 is upregulated in the intestine in response to nematode infection, or systemic mucosa in response to anaphylaxis. Like human α-chymase, MCPT-1 is capable of the conversion of angiotensin I to angiotensin II, which plays a key role in the regulation of arterial pressure. The intestinal inflammation associated with gastrointestinal helminths is partly mediated by mMCP-1.

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.

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.

Vasorin is a typical type I membrane protein. It contains 1 EGF-like domain, 1 fibronectin type-III domain, 10 LRR (leucine-rich) repeats, 1 LRRCT domain and 1 LRRNT domain. Vasorin is predominantly expressed in vascular smooth muscle cells, and that its expression is developmentally regulated. vasorin It directly binds to transforming growth factor (TGF)-β and attenuates TGF-β signaling in vitro. This suggests that down-regulation of vasorin expression contributes to neointimal formation after vascular injury and that vasorin modulates cellular responses to pathological stimuli in the vessel wall.

TGF beta 3 Protein, Human, Recombinant (hFc) is expressed in HEK293 mammalian cells with hFc tag. The predicted molecular weight is 41.2 kDa and the accession number is P10600-1.

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.