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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, hematopoietic cells, lung, kidney, gut, liver, eye, ear, skin, and the nervous system.

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, hematopoietic cells, lung, kidney, gut, liver, eye, ear, skin, and the nervous system.

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, hematopoietic cells, lung, kidney, gut, liver, eye, ear, skin, and the nervous system.

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).

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).

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).

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, hematopoietic cells, lung, kidney, gut, liver, eye, ear, skin, and the nervous system.

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, hematopoietic cells, lung, kidney, gut, liver, eye, ear, skin, and the nervous system.

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, hematopoietic cells, lung, kidney, gut, liver, eye, ear, skin, and the nervous system.

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

TGF-β1 (transforming growth factor beta 1) is one of three closely related mammalian members of the large TGF-β1 superfamily that share a characteristic cystine knot structure. TGF-β1, -2 and -3 are highly pleiotropic cytokines that act as cellular switches to regulate processes such as immune function, proliferation and epithelial-mesenchymal transition. Each TGF-β isoform has some non-redundant function; for TGF-β1, mice with targeted deletion show defects in hematopoiesis and endothelial differentiation and died of overwhelming inflammation. TGF-β1 signaling begins with high-affinity binding to a type II ser/thr kinase receptor termed TGF-β RII. This receptor then phosphorylates and activates a second ser/thr kinase receptor, TGF-β RI (also called activin receptor‑like kinase (ALK)-5), or alternatively, ALK-1. This complex phosphorylates and activates Smad proteins that regulate transcription.

TGF-β1 (transforming growth factor beta 1) is one of three closely related mammalian members of the large TGF-β1 superfamily that share a characteristic cystine knot structure. TGF-β1, -2 and -3 are highly pleiotropic cytokines that act as cellular switches to regulate processes such as immune function, proliferation and epithelial-mesenchymal transition. Each TGF-β isoform has some non-redundant function; for TGF-β1, mice with targeted deletion show defects in hematopoiesis and endothelial differentiation and died of overwhelming inflammation. TGF-β1 signaling begins with high-affinity binding to a type II ser/thr kinase receptor termed TGF-β RII. This receptor then phosphorylates and activates a second ser/thr kinase receptor, TGF-β RI (also called activin receptor‑like kinase (ALK)-5), or alternatively, ALK-1. This complex phosphorylates and activates Smad proteins that regulate transcription.

TGF-β1 (transforming growth factor beta 1) is one of three closely related mammalian members of the large TGF-β1 superfamily that share a characteristic cystine knot structure. TGF-β1, -2 and -3 are highly pleiotropic cytokines that act as cellular switches to regulate processes such as immune function, proliferation and epithelial-mesenchymal transition. Each TGF-β isoform has some non-redundant function; for TGF-β1, mice with targeted deletion show defects in hematopoiesis and endothelial differentiation and died of overwhelming inflammation. TGF-β1 signaling begins with high-affinity binding to a type II ser/thr kinase receptor termed TGF-β RII. This receptor then phosphorylates and activates a second ser/thr kinase receptor, TGF-β RI (also called activin receptor‑like kinase (ALK)-5), or alternatively, ALK-1. This complex phosphorylates and activates Smad proteins that regulate transcription.

TGF-β1 (transforming growth factor beta 1) is one of three closely related mammalian members of the large TGF-β1 superfamily that share a characteristic cystine knot structure. TGF-β1, -2 and -3 are highly pleiotropic cytokines that act as cellular switches to regulate processes such as immune function, proliferation and epithelial-mesenchymal transition. Each TGF-β isoform has some non-redundant function; for TGF-β1, mice with targeted deletion show defects in hematopoiesis and endothelial differentiation and died of overwhelming inflammation. TGF-β1 signaling begins with high-affinity binding to a type II ser/thr kinase receptor termed TGF-β RII. This receptor then phosphorylates and activates a second ser/thr kinase receptor, TGF-β RI (also called activin receptor‑like kinase (ALK)-5), or alternatively, ALK-1. This complex phosphorylates and activates Smad proteins that regulate transcription.

TGF-β1 (transforming growth factor beta 1) is one of three closely related mammalian members of the large TGF-β1 superfamily that share a characteristic cystine knot structure. TGF-β1, -2 and -3 are highly pleiotropic cytokines that act as cellular switches to regulate processes such as immune function, proliferation and epithelial-mesenchymal transition. Each TGF-β isoform has some non-redundant function; for TGF-β1, mice with targeted deletion show defects in hematopoiesis and endothelial differentiation and died of overwhelming inflammation. TGF-β1 signaling begins with high-affinity binding to a type II ser/thr kinase receptor termed TGF-β RII. This receptor then phosphorylates and activates a second ser/thr kinase receptor, TGF-β RI (also called activin receptor‑like kinase (ALK)-5), or alternatively, ALK-1. This complex phosphorylates and activates Smad proteins that regulate transcription.

TGF-β1 (transforming growth factor beta 1) is one of three closely related mammalian members of the large TGF-β1 superfamily that share a characteristic cystine knot structure. TGF-β1, -2 and -3 are highly pleiotropic cytokines that act as cellular switches to regulate processes such as immune function, proliferation and epithelial-mesenchymal transition. Each TGF-β isoform has some non-redundant function; for TGF-β1, mice with targeted deletion show defects in hematopoiesis and endothelial differentiation and died of overwhelming inflammation. TGF-β1 signaling begins with high-affinity binding to a type II ser/thr kinase receptor termed TGF-β RII. This receptor then phosphorylates and activates a second ser/thr kinase receptor, TGF-β RI (also called activin receptor‑like kinase (ALK)-5), or alternatively, ALK-1. This complex phosphorylates and activates Smad proteins that regulate transcription.

Molecular Formula : C18H18O4S

Molecular Formula : C18 H18 O4 S

Molecular Formula : C18 H18 O4 S

Molecular Formula : C21H24N4O2

Molecular Formula : C21H24N4O2

Molecular Formula : C21H24N4O2

Molecular Formula : C9 H16 Br2 N5 O4 P

Molecular Formula : C9 H16 Br2 N5 O4 P

Molecular Formula : C9 H16 Br2 N5 O4 P

Thalidomide

Thalidomide

Thalidomide

Molecular Formula : C13 2H4 H6 N2 O4

Molecular Formula : C13 2H4 H6 N2 O4

Thallium (I) Nitrate

Thallium (I) Nitrate

Molecular Formula : C2 H6 O . Tl

Molecular Formula : C2 H6 O . Tl

Molecular Formula : C2 H6 O . Tl

Molecular Formula : O4 S . 2 Tl

Molecular Formula : O4 S . 2 Tl

Molecular Formula : O4 S . 2 Tl

Molecular Formula : C34 H50 O12

Molecular Formula : C34 H50 O12

Molecular Formula : C34 H50 O12

Thaumatin

Thaumatin

Molecular Formula : C29 H24 O12

Molecular Formula : C29 H24 O12

Molecular Formula : C36 H28 O16

Molecular Formula : C19 H21 N O3

Molecular Formula : C19 H21 N O3