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Catalog Number: (10748-752)
Supplier: Prosci
Description: ACVR1B Antibody: Activins are dimeric growth and differentiation factors which belong to the transforming growth factor-beta (TGF-beta) superfamily of structurally related signaling proteins. Activins signal through a heteromeric complex of receptor serine kinases which include at least two type I and two type II receptors. ACVR1B, also known as activin receptor-like kinase 4 (ALK4), is a type I receptor for activin and plays major roles in cell differentiation, growth arrest and apoptosis. Like another type I activin receptor ACVR1C, ACVR1B can mediate signaling by ligands such as Nodal, Xnr1, GDF-1/3, activin B and activin AB. In Xenopus embryos, expression of a dominant-negative form of ACVR1B blocked all mesoderm-inducing ligands, while expression of a dominant negative ACVR1C only blocked Nodal and Xnr1 signaling, suggesting that the ACVR1B and ACVR1C possess distinct functions.


Catalog Number: (77439-836)
Supplier: Bioss
Description: ATF6 is a transcription factor that acts during endoplasmic reticulum stress by activating unfolded protein response target genes. It binds DNA on the 5'-CCAC[GA]-3'half of the ER stress response element (ERSE) (5'-CCAAT-N(9)-CCAC[GA]-3') and of ERSE II (5'-ATTGG-N-CCACG-3'). Binding to ERSE requires binding of NF-Y to ERSE. ATF6 could also be involved in activation of transcription by the serum response factor. ATF6 exists as a homodimer and heterodimer with ATF6 beta. The dimer interacts with the nuclear transcription factor Y (NF-Y) trimer through direct binding to NF-Y subunit C (NF-YC). It also interacts with the transcription factors GTF2I, YY1 and SRF. Under ER stress the cleaved N-terminal cytoplasmic domain translocates into the nucleus. The basic domain of ATF6 functions as a nuclear localization signal and the basic leucine zipper domain is sufficient for association with the NF-Y trimer and binding to ERSE. During the unfolded protein response an approximately 50 kDa fragment containing the cytoplasmic transcription factor domain is released by proteolysis. The cleavage seems to be performed sequentially by site 1 and site 2 proteases. ATF6 is N glycosylated, phosphorylated in vitro by MAPK14/P38MAPK and belongs to the bZIP family.


Catalog Number: (89416-720)
Supplier: Prosci
Description: ACVR1B Antibody: Activins are dimeric growth and differentiation factors which belong to the transforming growth factor-beta (TGF-beta) superfamily of structurally related signaling proteins. Activins signal through a heteromeric complex of receptor serine kinases which include at least two type I and two type II receptors. ACVR1B, also known as activin receptor-like kinase 4 (ALK4), is a type I receptor for activin and plays major roles in cell differentiation, growth arrest and apoptosis. Like another type I activin receptor ACVR1C, ACVR1B can mediate signaling by ligands such as Nodal, Xnr1, GDF-1/3, activin B and activin AB. In Xenopus embryos, expression of a dominant-negative form of ACVR1B blocked all mesoderm-inducing ligands, while expression of a dominant negative ACVR1C only blocked Nodal and Xnr1 signaling, suggesting that the ACVR1B and ACVR1C possess distinct functions.


Catalog Number: (10368-944)
Supplier: Bioss
Description: Signal transducer and transcription activator that mediates cellular responses to interferons (IFNs), cytokine KITLG/SCF and other cytokines and other growth factors. Following type I IFN (IFN-alpha and IFN-beta) binding to cell surface receptors, signaling via protein kinases leads to activation of Jak kinases (TYK2 and JAK1) and to tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs dimerize and associate with ISGF3G/IRF-9 to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of IFN-stimulated genes (ISG), which drive the cell in an antiviral state. In response to type II IFN (IFN-gamma), STAT1 is tyrosine- and serine-phosphorylated. It then forms a homodimer termed IFN-gamma-activated factor (GAF), migrates into the nucleus and binds to the IFN gamma activated sequence (GAS) to drive the expression of the target genes, inducing a cellular antiviral state. Becomes activated in response to KITLG/SCF and KIT signaling. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4.


Catalog Number: (10368-946)
Supplier: Bioss
Description: Signal transducer and transcription activator that mediates cellular responses to interferons (IFNs), cytokine KITLG/SCF and other cytokines and other growth factors. Following type I IFN (IFN-alpha and IFN-beta) binding to cell surface receptors, signaling via protein kinases leads to activation of Jak kinases (TYK2 and JAK1) and to tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs dimerize and associate with ISGF3G/IRF-9 to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of IFN-stimulated genes (ISG), which drive the cell in an antiviral state. In response to type II IFN (IFN-gamma), STAT1 is tyrosine- and serine-phosphorylated. It then forms a homodimer termed IFN-gamma-activated factor (GAF), migrates into the nucleus and binds to the IFN gamma activated sequence (GAS) to drive the expression of the target genes, inducing a cellular antiviral state. Becomes activated in response to KITLG/SCF and KIT signaling. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4.


Catalog Number: (10090-586)
Supplier: Proteintech
Description: MTUS1, also named as ATBP, ATIP, GK1, KIAA1288 and MTSG1, Belongs to the MTUS1 family. It cooperates with AGTR2 to inhibit ERK2 activation and cell proliferation. MTUS1 may be required for AGTR2 cell surface expression. Together with PTPN6, induces UBE2V2 expression upon angiotensin-II stimulation. Isoform 1 inhibits breast cancer cell proliferation, delays the progression of mitosis by prolonging metaphase and reduces tumor growth. MTUS1 up-regulation during cellular transition from proliferation to quiescence and differentiation. It is a potential tumor suppressor gene located at chromosome 8p21.3.22, near marker D8S254. According to the functional data and intracellular localization, MTUS1 also named as mitochondrial tumor suppressor gene 1 (MTSG1). One main feature common to all ATIP members is the presence of a large C-terminal coiled-coil domain that allows homo- and hetero-dimerization of these proteins. The antibody can recognize all the isoforms except isoform 5 (85-90kd). The antibody tested HomoDimer isoforms (80kd/110-120/280kd) in Jurkat cell.


Catalog Number: (10748-754)
Supplier: Prosci
Description: ACVR1C Antibody: Activins are dimeric growth and differentiation factors which belong to the transforming growth factor-beta (TGF-beta) superfamily of structurally related signaling proteins. Activins signal through a heteromeric complex of receptor serine kinases which include at least two type I and two type II receptors. ACVR1C, also known as ALK7, is a type I activin receptor and plays a role in cell differentiation, growth arrest and apoptosis. ACVR1C can mediate signaling by ligans such as Nodal, GDF-1/3, activin B and activin AB, all of which can also signal through the ubiquitous activin type I receptor ACVR1B (also known as ALK4). ACVR1C is a novel marker specifically expressed during the late phase of adipocyte differentiation. ACVR1C is dispensable for mouse embryogenesis, which suggests alternative functions for this receptor in postnatal development and tissue homeostasis. ACVR1C plays an important role in regulating the functional plasticity of pancreatic islets, negatively affecting beta-cell function by mediating the effects of activin B on Ca2+ signaling.


Supplier: Peprotech
Description: Myostatin is a TGF-β family member that acts as an inhibitor of skeletal muscle growth. This muscle-specific cytokine interacts with Activin type I and type II receptors, and suppresses myoblast proliferation by arresting cell-cycle in the G1 phase. Suppression of myostatin activity facilitates muscle formation, and may be useful in reducing and/or preventing adiposity and type-2 diabetes. Myostatin activity can be blocked by the activin-binding protein follistatin, and by the propeptide of myostatin. The amino acid sequence of mature myostatin is extremely conserved across species, and is the same in murine, rat, chicken, turkey, porcine, and human. Myostatin is expressed as the C-terminal part of a precursor polypeptide, which also contains a short N-terminal signal sequence for secretion, and a propeptide of 243 amino acids. After dimerization of this precursor, the covalent bonds between the propeptide and the mature ligand are cleaved by furin-type proteases. However, the resulting two proteins remain associated through non-covalent interactions, and are secreted as a latent complex. Recombinant Human/Murine/Rat Myostatin is a 25.0 kDa protein consisting of two identical 109 amino acid polypeptides linked by a single disulfide bond.
Catalog Number: (10097-818)
Supplier: Prosci
Description: IFN gamma receptor beta is part of the receptor for interferon gamma. This class II cytokine receptor pairs with CDw119 to form the IFN gamma receptor and is an integral part of the IFN gamma signal transduction pathway. CDw119 serves as the IFN gamma binding chain and associates with the IFN gamma beta chain which is required for receptor signaling. The extracellular portion of both the IFN gamma receptor alpha and beta chains must be species matched. The IFN gamma receptor beta chain is expressed on T and B cells, NK cells, monocytes/ macrophages, and fibroblasts. Binding of IFN gamma induces receptor dimerization, internalization, Jak1 and Jak2 protein kinase activation and, ultimately, STAT1 activation. It is also likely to interact with GAF. IFN gamma initiates and regulates a variety of immune responses and is required for signal transduction. Contains 2 fibronectin type III domains. Defects in IFN gamma Receptor beta are a cause of mendelian susceptibility to mycobacterial disease (MSMD), a rare condition that confers predisposition to illness caused by several mycobacteria strains


Catalog Number: (10072-560)
Supplier: Prosci
Description: EGF Receptor (EGFR, ErbB1) is a transmembrane protein that exerts tyrosine kinase activity upon ligand induced activation. EGFR can be activated by binding EGF or at least six other structurally related protein ligands, including TGF, HB-EGF, Betacellulin (BTC), Amphiregulin, Epiregulin, and Epigen. Upon activation, EGFR initiates a signaling cascade which includes dimerization and internalization, tyrosine phosphorylation, DNA synthesis of target genes, and, ultimately, cell proliferation. EGFR signaling plays a role in the growth and differentiation of normal cells, but elevated EGFR activity is correlated with the development and pathogenesis of certain cancers. Recombinant soluble human EGFR is a 621 amino acid glycoprotein comprising the extracellular domain of EGFR, and migrates at an apparent MW of 97.5 kDa by SDS-PAGE analysis under reducing conditions.


Catalog Number: (10097-826)
Supplier: Prosci
Description: IFN gamma receptor beta is part of the receptor for interferon gamma. This class II cytokine receptor pairs with CDw119 to form the IFN gamma receptor and is an integral part of the IFN gamma signal transduction pathway. CDw119 serves as the IFN gamma binding chain and associates with the IFN gamma beta chain which is required for receptor signaling. The extracellular portion of both the IFN gamma receptor alpha and beta chains must be species matched. The IFN gamma receptor beta chain is expressed on T and B cells, NK cells, monocytes/ macrophages, and fibroblasts. Binding of IFN gamma induces receptor dimerization, internalization, Jak1 and Jak2 protein kinase activation and, ultimately, STAT1 activation. It is also likely to interact with GAF. IFN gamma initiates and regulates a variety of immune responses and is required for signal transduction. Contains 2 fibronectin type III domains. Defects in IFN gamma Receptor beta are a cause of mendelian susceptibility to mycobacterial disease (MSMD), a rare condition that confers predisposition to illness caused by several mycobacteria strains


Catalog Number: (10097-836)
Supplier: Prosci
Description: IFN gamma receptor beta is part of the receptor for interferon gamma. This class II cytokine receptor pairs with CDw119 to form the IFN gamma receptor and is an integral part of the IFN gamma signal transduction pathway. CDw119 serves as the IFN gamma binding chain and associates with the IFN gamma beta chain which is required for receptor signaling. The extracellular portion of both the IFN gamma receptor alpha and beta chains must be species matched. The IFN gamma receptor beta chain is expressed on T and B cells, NK cells, monocytes/ macrophages, and fibroblasts. Binding of IFN gamma induces receptor dimerization, internalization, Jak1 and Jak2 protein kinase activation and, ultimately, STAT1 activation. It is also likely to interact with GAF. IFN gamma initiates and regulates a variety of immune responses and is required for signal transduction. Contains 2 fibronectin type III domains. Defects in IFN gamma Receptor beta are a cause of mendelian susceptibility to mycobacterial disease (MSMD), a rare condition that confers predisposition to illness caused by several mycobacteria strains


Catalog Number: (10097-828)
Supplier: Prosci
Description: IFN gamma receptor beta is part of the receptor for interferon gamma. This class II cytokine receptor pairs with CDw119 to form the IFN gamma receptor and is an integral part of the IFN gamma signal transduction pathway. CDw119 serves as the IFN gamma binding chain and associates with the IFN gamma beta chain which is required for receptor signaling. The extracellular portion of both the IFN gamma receptor alpha and beta chains must be species matched. The IFN gamma receptor beta chain is expressed on T and B cells, NK cells, monocytes/ macrophages, and fibroblasts. Binding of IFN gamma induces receptor dimerization, internalization, Jak1 and Jak2 protein kinase activation and, ultimately, STAT1 activation. It is also likely to interact with GAF. IFN gamma initiates and regulates a variety of immune responses and is required for signal transduction. Contains 2 fibronectin type III domains. Defects in IFN gamma Receptor beta are a cause of mendelian susceptibility to mycobacterial disease (MSMD), a rare condition that confers predisposition to illness caused by several mycobacteria strains


Catalog Number: (76084-106)
Supplier: Bioss
Description: Signal transducer and transcription activator that mediates cellular responses to interferons (IFNs), cytokine KITLG/SCF and other cytokines and other growth factors. Following type I IFN (IFN-alpha and IFN-beta) binding to cell surface receptors, signaling via protein kinases leads to activation of Jak kinases (TYK2 and JAK1) and to tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs dimerize and associate with ISGF3G/IRF-9 to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of IFN-stimulated genes (ISG), which drive the cell in an antiviral state. In response to type II IFN (IFN-gamma), STAT1 is tyrosine- and serine-phosphorylated. It then forms a homodimer termed IFN-gamma-activated factor (GAF), migrates into the nucleus and binds to the IFN gamma activated sequence (GAS) to drive the expression of the target genes, inducing a cellular antiviral state. Becomes activated in response to KITLG/SCF and KIT signaling. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4.


Supplier: Peprotech
Description: Myostatin is a TGF-β family member that acts as an inhibitor of skeletal muscle growth. This muscle-specific cytokine interacts with Activin type I and type II receptors, and suppresses myoblast proliferation by arresting cell-cycle in the G1 phase. Suppression of myostatin activity facilitates muscle formation, and may be useful in reducing and/or preventing adiposity and type-2 diabetes. Myostatin activity can be blocked by the activin-binding protein follistatin, and by the propeptide of myostatin. The amino acid sequence of mature myostatin is extremely conserved across species, and is the same in murine, rat, chicken, turkey, porcine, and human. Myostatin is expressed as the C-terminal part of a precursor polypeptide, which also contains a short N-terminal signal sequence for secretion, and a propeptide of 243 amino acids. After dimerization of this precursor, the covalent bonds between the propeptide and the mature ligand are cleaved by furin-type proteases. However, the resulting two proteins remain associated through non-covalent interactions, and are secreted as a latent complex. Recombinant Human/Murine/Rat Myostatin is a 25.0 kDa protein consisting of two identical 109 amino acid polypeptides linked by a single disulfide bond.
Catalog Number: (89416-722)
Supplier: Prosci
Description: ACVR1C Antibody: Activins are dimeric growth and differentiation factors which belong to the transforming growth factor-beta (TGF-beta) superfamily of structurally related signaling proteins. Activins signal through a heteromeric complex of receptor serine kinases which include at least two type I and two type II receptors. ACVR1C, also known as ALK7, is a type I activin receptor and plays a role in cell differentiation, growth arrest and apoptosis. ACVR1C can mediate signaling by ligans such as Nodal, GDF-1/3, activin B and activin AB, all of which can also signal through the ubiquitous activin type I receptor ACVR1B (also known as ALK4). ACVR1C is a novel marker specifically expressed during the late phase of adipocyte differentiation. ACVR1C is dispensable for mouse embryogenesis, which suggests alternative functions for this receptor in postnatal development and tissue homeostasis. ACVR1C plays an important role in regulating the functional plasticity of pancreatic islets, negatively affecting beta-cell function by mediating the effects of activin B on Ca2+ signaling.


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