目录号 | 产品详情 | 靶点 | |
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T7284 | Others | ||
Vasopressin acetate (113-79-1(free base)) 是一种具有血管收缩和抗利尿活性的肽激素,可与血管精氨酸加压素受体 V1 结合,在 A7r5 大鼠主动脉平滑肌细胞和新生大鼠心肌细胞中的 Kd 值分别为 1.31 和 1.44 nM。 | |||
T62893 | Adrenergic Receptor | ||
SM-2470 是一种α1-adrenoceptor拮抗剂,具有降压活性,可减低前神经节肾上腺神经活性和主动脉降压神经活性。SM-2470 具有降胆固醇活性,可抑制胆固醇吸收。 | |||
T11598 | TLR | ||
IAXO-102 是一种 TLR4 拮抗剂,可负向调节 TLR4 信号传导,还可以防止实验性腹主动脉瘤的发展。它抑制 MAPK 和 p65 NF-κB 磷酸化和 TLR4 依赖性促炎蛋白的表达。 | |||
T11076 | Others | ||
Dooku1 是Yoda1 的类似物,是一种内源性Piezo1通道的选择性拮抗剂,能够抑制Yoda1 诱导的主动脉舒张。它在HEK 293 细胞以及HUVEC 中测得对2 μM Yoda1 诱导的钙离子流的IC50值分别为1.3 μM 和1.5 μM。 | |||
T6102 | Antioxidant Reductase | ||
2'-Acetylacteoside 是一种苯乙醇苷类化合物,分离自来江藤中,可抑制自由基诱导的红细胞溶血,具有清除自由基的作用。 | |||
T30140 | 5-HT Receptor Adrenergic Receptor | ||
Arotinolol hydrochloride(Arotinolol HCl) 是一种非选择性的 α/β-肾上腺素受体 (α/β-adrenergic receptor ) 阻滞剂。Arotinolol hydrochloride 对放射性配体 125I-ICYP 与 5HT1B-羟色胺受体能结合有抑制作用。Arotinolol hydrochloride 是一种抗高血压和抗肥胖试剂,可改善大鼠主动脉僵硬,研究肥胖相关疾病。 | |||
T68123 | Calcium Channel | ||
Oxodipine 是一种二氢吡啶型钙拮抗剂 ,抑制了KCl 诱导的兔主动脉收缩,降低了效力较低的大鼠心室试纸收缩的心脏力量。在大鼠培养的新生儿心室肌细胞中,Oxodipine 降低了L 型Ca 电流(I),IC 为0.24μM,对T 型Ca 电流(I)的IC 为0.41μM。Oxodipine 会使小鼠便秘和狗牙龈增生。 | |||
TN1724 | P450 Antioxidant | ||
Harmalol hydrochloride (Harmidol hydrochloride) 是一种可从Peganum harmala L.的种子中提取出来的β-咔啉生物碱。Harmalol hydrochloride 是Harmaline 的主要代谢产物,在转录和翻译后水平上显著抑制二恶英介导的 CYP1A1 诱导。Harmalol hydrochloride 在去氧肾上腺素或KCl 预先收缩的分离大鼠胸主动脉制剂中显示出血管松弛活性。 Harmalol hydrochloride 具有抗氧化活性. | |||
T33440 | |||
MK785 is part of the association between inhibition of aortic histamine formation, aortic albumin permeability, and atherosclerosis. Aortic histamine synthesis was inhibited by partial inhibition of aortic histidine decarboxylase (HD) by application of MK | |||
T32406 | |||
Kmup-4 is an enhancer of cGMP activity and an aortic smooth muscle relaxant. |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPH-00882 | ACTA2 Protein, Human, Recombinant (His) | Human | E. coli | ||
Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
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TMPH-02494 | AEBP1 Protein, Mouse, Recombinant (His & SUMO) | Mouse | E. coli | ||
As a positive regulator of collagen fibrillogenesis, it is probably involved in the organization and remodeling of the extracellular matrix.; May positively regulate MAP-kinase activity in adipocytes, leading to enhanced adipocyte proliferation and reduced adipocyte differentiation. May also positively regulate NF-kappa-B activity in macrophages by promoting the phosphorylation and subsequent degradation of I-kappa-B-alpha (NFKBIA), leading to enhanced macrophage inflammatory responsiveness. Can act as a transcriptional repressor.
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TMPJ-00258 | TGF beta 2 Protein, Human, Recombinant | Human | Human Cells | ||
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).
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TMPY-02836 | MFGE8 Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
MFG-E8, also known as lactadherin and MFGE8, contains 1 EGF-like domain and 2 F5/8 type C domains. It also contains phosphatidylserine (PS) binding domain, as well as an Arginine-Glycine-Aspartic acid motif, which enables the binding to integrins. It binds PS, which is exposed on the surface of apoptotic cells. MFG-E8 is expressed in mammary epithelial cell surfaces and aortic media. Overexpression of MFG-E8 can be found in several carcinomas. MFG-E8 has opsonization of the apoptotic cells and binding to integrins on the surface of phagocytic cells. It also mediates the engulfment of the dead cell. MFG-E8 plays an important role in the maintenance of intestinal epithelial homeostasis and the promotion of mucosal healing. It promotes VEGF-dependent neovascularization and contributes to the phagocytic removal of apoptotic cells in many tissues. It also binds to phosphatidylserine-enriched cell surfaces in a receptor-independent manner.
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TMPY-05157 | TGFBR2 Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
TGFBR2 is a member of the Ser/Thr protein kinase family and the TGFB receptor subfamily. It is a transmembrane protein. TGFBR2 is comprised of a C-terminal protein kinase domain and an N-terminal ectodomain. The ectodomain consists of a compact fold containing nine beta-strands and a single helix stabilized by a network of six intra strand disulfide bonds. The folding topology includes a central five-stranded antiparallel beta-sheet, eight-residues long at its centre, covered by a second layer consisting of two segments of two-stranded antiparallel beta-sheets. TGFBR2 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 TGFBR2 gene have been associated with Marfan syndrome, Loeys-Deitz Aortic Aneurysm Syndrome, and the development of various types of tumors. TGFBR2 attenuates the biological activities of TGF-beta in colorectal cancer. TGFBR2 expression is increased in oral squamous cell carcinoma cells. Its expression is decreased by IL-1beta while inducing Sp3 via NFkappaB. TGFB2 and TGFBR2 are involved in the antiestrogenic activity.
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TMPY-00510 | FKBP11 Protein, Human, Recombinant (mFc) | Human | HEK293 | ||
FKBP11 serve as biomarker and/or therapeutic target for Acute aortic dissection (AAD). FKBP11 during the development of HCC and FKBP11 has the potential to be an early marker for HCC.
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TMPY-03052 | MFAP5 Protein, Human, Recombinant (His) | Human | HEK293 | ||
MFAP5 (Microfibril Associated Protein 5, also known as MAGP2) is a Protein Coding gene. MFAP5 is a component of the elastin-associated microfibrils. It belongs to the MFAP family. As a 25-kD microfibril-associated glycoprotein, MFAP5 is rich in serine and threonine residues. It stimulates the assembly of elastic fibers, a complex structure composed of a tropoelastin inner core and microfibril outer mantle comprising proteins such as fibrillins and microfibril-associated glycoproteins that guide tropoelastin deposition. MFAP5 also stabilizes type 1 procollagen and thus plays an important role in extracellular matrix homeostasis. It has multiple binding regions on fibrillins and has a covalent periodic association with fibrillin-containing microfibrils. Diseases associated with MFAP5 include Aortic Aneurysm, Familial Thoracic 9, and Familial Thoracic Aortic Aneurysm And Aortic Dissection.
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TMPH-02863 | LOX Protein, Mouse, Recombinant (His & Myc) | Mouse | Baculovirus | ||
Responsible for the post-translational oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. Regulator of Ras expression. May play a role in tumor suppression. Plays a role in the aortic wall architecture.
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TMPY-04471 | APEG1 Protein, Human, Recombinant (His) | Human | E. coli | ||
Striated muscle preferentially expressed protein kinase, also known as aortic preferentially expressed protein 1, APEG-1, SPEG and KIAA1297, is a protein that belongs to the protein kinase superfamily and CAMK Ser/Thr protein kinase family. SPEG / APEG-1 contains two fibronectin type-III domains, nine Ig-like (immunoglobulin-like) domains, two protein kinase domains. Isoform 1 of SPEG is preferentially expressed in striated muscle. Non-kinase form such as isoform 3 of SPEG is predominantly expressed in the aorta. Isoform 3 of SPEG appears to be expressed only in highly differentiated ASMC in normal vessel walls and down-regulated in dedifferentiated ASMC. Isoform 3 of SPEG may have a role in regulating the growth and differentiation of arterial smooth muscle cells. Isoform 3 of SPEG is quickly down-regulated in response to vascular injury, when ASMC cells change from a quiescent to a proliferative phenotype.
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TMPY-04066 | LOX-1 Protein, Rat, Recombinant (His) | Rat | HEK293 | ||
Oxidized low-density lipoprotein receptor 1 (Ox-LDL receptor 1 or OLR1), also known as lectin-type oxidized LDL receptor 1 (LOX1), is a receptor protein that belongs to the C-type lectin superfamily. LOX1 is a multi-ligand receptor originally identified as the endothelial oxidized LDL receptor. OLR1 / LOX1 was isolated from an aortic endothelial cell, and recently it has been discovered in macrophages and vascular smooth muscle cells in artery vessels. The expression of LOX1 is induced by inflammatory stimuli and oxidative stimuli. This protein binds, internalizes, and degrades oxidized low-density lipoprotein. LOX1 may play an important role in the progression of vulnerable carotid plaque and might regulate vulnerable plaque formation in cooperation with MMPs and TIMP-2. In clinical, LOX1 is thought to be involved in the development of atherosclerotic lesions.
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TMPY-03371 | LOX-1 Protein, Rat, Recombinant (hFc) | Rat | HEK293 | ||
Oxidized low-density lipoprotein receptor 1 (Ox-LDL receptor 1 or OLR1), also known as lectin-type oxidized LDL receptor 1 (LOX1), is a receptor protein that belongs to the C-type lectin superfamily. LOX1 is a multi-ligand receptor originally identified as the endothelial oxidized LDL receptor. OLR1 / LOX1 was isolated from an aortic endothelial cell, and recently it has been discovered in macrophages and vascular smooth muscle cells in artery vessels. The expression of LOX1 is induced by inflammatory stimuli and oxidative stimuli. This protein binds, internalizes, and degrades oxidized low-density lipoprotein. LOX1 may play an important role in the progression of vulnerable carotid plaque and might regulate vulnerable plaque formation in cooperation with MMPs and TIMP-2. In clinical, LOX1 is thought to be involved in the development of atherosclerotic lesions.
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TMPY-02490 | LOX-1 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Oxidized low-density lipoprotein receptor 1 (Ox-LDL receptor 1 or OLR1), also known as lectin-type oxidized LDL receptor 1 (LOX1), is a receptor protein that belongs to the C-type lectin superfamily. LOX1 is a multi-ligand receptor originally identified as the endothelial oxidized LDL receptor. OLR1 / LOX1 was isolated from an aortic endothelial cell, and recently it has been discovered in macrophages and vascular smooth muscle cells in artery vessels. The expression of LOX1 is induced by inflammatory stimuli and oxidative stimuli. This protein binds, internalizes, and degrades oxidized low-density lipoprotein. LOX1 may play an important role in the progression of vulnerable carotid plaque and might regulate vulnerable plaque formation in cooperation with MMPs and TIMP-2. In clinical, LOX1 is thought to be involved in the development of atherosclerotic lesions.
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TMPY-03351 | LOX-1 Protein, Cynomolgus, Recombinant (His) | Cynomolgus | HEK293 | ||
Oxidized low-density lipoprotein receptor 1 (Ox-LDL receptor 1 or OLR1), also known as lectin-type oxidized LDL receptor 1 (LOX1), is a receptor protein that belongs to the C-type lectin superfamily. LOX1 is a multi-ligand receptor originally identified as the endothelial oxidized LDL receptor. OLR1 / LOX1 was isolated from an aortic endothelial cell, and recently it has been discovered in macrophages and vascular smooth muscle cells in artery vessels. The expression of LOX1 is induced by inflammatory stimuli and oxidative stimuli. This protein binds, internalizes, and degrades oxidized low-density lipoprotein. LOX1 may play an important role in the progression of vulnerable carotid plaque and might regulate vulnerable plaque formation in cooperation with MMPs and TIMP-2. In clinical, LOX1 is thought to be involved in the development of atherosclerotic lesions.
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TMPY-05235 | MFGE8 Protein, Human, Recombinant (His & Avi), Biotinylated | Human | Baculovirus-Insect Cells | ||
MFG-E8, also known as lactadherin and MFGE8, contains 1 EGF-like domain and 2 F5/8 type C domains. It also contains phosphatidylserine (PS) binding domain, as well as an Arginine-Glycine-Aspartic acid motif, which enables the binding to integrins. It binds PS, which is exposed on the surface of apoptotic cells. MFG-E8 is expressed in mammary epithelial cell surfaces and aortic media. Overexpression of MFG-E8 can be found in several carcinomas. MFG-E8 has opsonization of the apoptotic cells and binding to integrins on the surface of phagocytic cells. It also mediates the engulfment of the dead cell. MFG-E8 plays an important role in the maintenance of intestinal epithelial homeostasis and the promotion of mucosal healing. It promotes VEGF-dependent neovascularization and contributes to the phagocytic removal of apoptotic cells in many tissues. It also binds to phosphatidylserine-enriched cell surfaces in a receptor-independent manner.
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TMPY-01910 | TIE1 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Tyrosine kinase with immunoglobulin-like and EGF-like domains 1 also known as Tie1 is an angiopoietin receptor and is an orphan receptor tyrosine kinase that is expressed almost exclusively in endothelial cells and that is required for normal embryonic vascular development. The receptor tyrosine kinase Tie1 is expressed primarily in vascular endothelial cells. The receptor has also been detected in epithelial tumours in breast, thyroid and gastric cancers and in tumour cell lines where it appears as a 45 kDa truncated receptor fragment. Tie1 promotes endothelial cell survival, but other studies have suggested that the Tie1 kinase has little to no activity. Embryos deficient in Tie1 failed to establish structural integrity of vascular endothelial cells, resulting in oedema and subsequently localized haemorrhage. Tie1 is significantly higher in human aortic endothelial cells than in human umbilical vein endothelial cells. Additionally, attachment of cells of monocytic lineage to endothelial cells is also enhanced by Tie1 expression. Collectively Tie1 has a proinflammatory property and may play a role in endothelial inflammatory diseases such as atherosclerosis.
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TMPY-01577 | ORP150 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Hypoxia up-regulated protein 1, also known as 15 kDa oxygen-regulated protein, 17 kDa glucose-regulated protein, ORP-15, GRP-17, and HYOU1, is a member of the heat shock protein 7 family. Seven members from four different heat shock protein (HSP) families were identified including HYOU1 (ORP15), HSPC1 (HSP86), HSPA5 (Bip), HSPD1 (HSP6), and several isoforms of the two testis-specific HSP7 chaperones HSPA2 and HSPA1L. HYOU1 is highly expressed in tissues that contain well-developed endoplasmic reticulum and synthesize large amounts of secretory proteins. It is highly expressed in the liver and pancreas. HYOU1 is also expressed in macrophages within aortic atherosclerotic plaques and in breast cancers. HYOU1 has a pivotal role in cytoprotective cellular mechanisms triggered by oxygen deprivation. It may play a role as a molecular chaperone and participate in protein folding. Suppression of HYOU1 is associated with accelerated apoptosis. It is suggested to have an important cytoprotective role in hypoxia-induced cellular perturbation. This protein is up-regulated in tumors, especially in breast tumors, and thus it is associated with tumor invasiveness.
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TMPY-03171 | TGFBR2 Protein, Rhesus, Recombinant (hFc) | Rhesus | HEK293 | ||
TGFBR2 is a member of the Ser/Thr protein kinase family and the TGFB receptor subfamily. It is a transmembrane protein. TGFBR2 is comprised of a C-terminal protein kinase domain and an N-terminal ectodomain. The ectodomain consists of a compact fold containing nine beta-strands and a single helix stabilized by a network of six intra strand disulfide bonds. The folding topology includes a central five-stranded antiparallel beta-sheet, eight-residues long at its centre, covered by a second layer consisting of two segments of two-stranded antiparallel beta-sheets. TGFBR2 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 TGFBR2 gene have been associated with Marfan syndrome, Loeys-Deitz Aortic Aneurysm Syndrome, and the development of various types of tumors. TGFBR2 attenuates the biological activities of TGF-beta in colorectal cancer. TGFBR2 expression is increased in oral squamous cell carcinoma cells. Its expression is decreased by IL-1beta while inducing Sp3 via NFkappaB. TGFB2 and TGFBR2 are involved in the antiestrogenic activity.
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TMPY-05810 | TGFBR2 Protein, Human, Recombinant (His & hFc), Biotinylated | Human | HEK293 | ||
TGFBR2 is a member of the Ser/Thr protein kinase family and the TGFB receptor subfamily. It is a transmembrane protein. TGFBR2 is comprised of a C-terminal protein kinase domain and an N-terminal ectodomain. The ectodomain consists of a compact fold containing nine beta-strands and a single helix stabilized by a network of six intra strand disulfide bonds. The folding topology includes a central five-stranded antiparallel beta-sheet, eight-residues long at its centre, covered by a second layer consisting of two segments of two-stranded antiparallel beta-sheets. TGFBR2 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 TGFBR2 gene have been associated with Marfan syndrome, Loeys-Deitz Aortic Aneurysm Syndrome, and the development of various types of tumors. TGFBR2 attenuates the biological activities of TGF-beta in colorectal cancer. TGFBR2 expression is increased in oral squamous cell carcinoma cells. Its expression is decreased by IL-1beta while inducing Sp3 via NFkappaB. TGFB2 and TGFBR2 are involved in the antiestrogenic activity.
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TMPY-05508 | TGFBR2 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
TGFBR2 is a member of the Ser/Thr protein kinase family and the TGFB receptor subfamily. It is a transmembrane protein. TGFBR2 is comprised of a C-terminal protein kinase domain and an N-terminal ectodomain. The ectodomain consists of a compact fold containing nine beta-strands and a single helix stabilized by a network of six intra strand disulfide bonds. The folding topology includes a central five-stranded antiparallel beta-sheet, eight-residues long at its centre, covered by a second layer consisting of two segments of two-stranded antiparallel beta-sheets. TGFBR2 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 TGFBR2 gene have been associated with Marfan syndrome, Loeys-Deitz Aortic Aneurysm Syndrome, and the development of various types of tumors. TGFBR2 attenuates the biological activities of TGF-beta in colorectal cancer. TGFBR2 expression is increased in oral squamous cell carcinoma cells. Its expression is decreased by IL-1beta while inducing Sp3 via NFkappaB. TGFB2 and TGFBR2 are involved in the antiestrogenic activity.
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TMPY-03082 | TGFBR2 Protein, Rat, Recombinant (hFc) | Rat | HEK293 | ||
TGFBR2 is a member of the Ser/Thr protein kinase family and the TGFB receptor subfamily. It is a transmembrane protein. TGFBR2 is comprised of a C-terminal protein kinase domain and an N-terminal ectodomain. The ectodomain consists of a compact fold containing nine beta-strands and a single helix stabilized by a network of six intra strand disulfide bonds. The folding topology includes a central five-stranded antiparallel beta-sheet, eight-residues long at its centre, covered by a second layer consisting of two segments of two-stranded antiparallel beta-sheets. TGFBR2 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 TGFBR2 gene have been associated with Marfan syndrome, Loeys-Deitz Aortic Aneurysm Syndrome, and the development of various types of tumors. TGFBR2 attenuates the biological activities of TGF-beta in colorectal cancer. TGFBR2 expression is increased in oral squamous cell carcinoma cells. Its expression is decreased by IL-1beta while inducing Sp3 via NFkappaB. TGFB2 and TGFBR2 are involved in the antiestrogenic activity.
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TMPY-01358 | ALK-5 Protein, Human, Recombinant (His & hFc) | Human | HEK293 | ||
Transforming growth factor, beta receptor I, also known as Transforming growth factor-beta receptor type I , Serine / threonine-protein kinase receptor R4, Activin receptor-like kinase 5, SKR4, ALK-5, and TGFBR1, is a single-pass type I membrane protein that belongs to the protein kinase superfamily and TGFB receptor subfamily. TGFBR1 / ALK-5 is found in all tissues examined. It is most abundant in placenta and least abundant in brain and heart. 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. On ligand binding, TGFBR1 / ALK-5 forms a receptor complex consisting of two type I I and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which auto-phosphorylate, then bind and activate SMAD transcriptional regulators. TGF-beta signaling via TGFBR1 / ALK-5 is not required in myocardial cells during mammalian cardiac development, but plays an irreplaceable cell-autonomous role regulating cellular communication, differentiation and proliferation in endocardial and epicardial cells. Defects in TGFBR1 / ALK-5 are the cause of Loeys-Dietz syndrome type 1A (LDS1A), Loeys-Dietz syndrome type 2A (LDS2A), and aortic aneurysm familial thoracic type 5 (AAT5).
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TMPY-05771 | ALK-5 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
Transforming growth factor, beta receptor I, also known as Transforming growth factor-beta receptor type I , Serine / threonine-protein kinase receptor R4, Activin receptor-like kinase 5, SKR4, ALK-5, and TGFBR1, is a single-pass type I membrane protein that belongs to the protein kinase superfamily and TGFB receptor subfamily. TGFBR1 / ALK-5 is found in all tissues examined. It is most abundant in placenta and least abundant in brain and heart. 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. On ligand binding, TGFBR1 / ALK-5 forms a receptor complex consisting of two type I I and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which auto-phosphorylate, then bind and activate SMAD transcriptional regulators. TGF-beta signaling via TGFBR1 / ALK-5 is not required in myocardial cells during mammalian cardiac development, but plays an irreplaceable cell-autonomous role regulating cellular communication, differentiation and proliferation in endocardial and epicardial cells. Defects in TGFBR1 / ALK-5 are the cause of Loeys-Dietz syndrome type 1A (LDS1A), Loeys-Dietz syndrome type 2A (LDS2A), and aortic aneurysm familial thoracic type 5 (AAT5).
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TMPY-04366 | ALK-5 Protein, Human, Recombinant (aa 200-503, His & GST) | Human | Baculovirus-Insect Cells | ||
Transforming growth factor, beta receptor I, also known as Transforming growth factor-beta receptor type I , Serine / threonine-protein kinase receptor R4, Activin receptor-like kinase 5, SKR4, ALK-5, and TGFBR1, is a single-pass type I membrane protein that belongs to the protein kinase superfamily and TGFB receptor subfamily. TGFBR1 / ALK-5 is found in all tissues examined. It is most abundant in placenta and least abundant in brain and heart. 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. On ligand binding, TGFBR1 / ALK-5 forms a receptor complex consisting of two type I I and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which auto-phosphorylate, then bind and activate SMAD transcriptional regulators. TGF-beta signaling via TGFBR1 / ALK-5 is not required in myocardial cells during mammalian cardiac development, but plays an irreplaceable cell-autonomous role regulating cellular communication, differentiation and proliferation in endocardial and epicardial cells. Defects in TGFBR1 / ALK-5 are the cause of Loeys-Dietz syndrome type 1A (LDS1A), Loeys-Dietz syndrome type 2A (LDS2A), and aortic aneurysm familial thoracic type 5 (AAT5).
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