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Catalog Number: (PRSI33-714)
Supplier: ProSci Inc.
Description: Recognises a protein of 78-85 kDa, which is identified as the receptor for Luteinizing hormone/Choriogonadotropin. Luteinizing hormone plays a role in spermatogenesis and ovulation by stimulating the testes and ovaries to produce steroids. Choriogonadotropin production in the placenta maintains estrogen and progesterone levels during the first trimester of pregnancy. Ovaries and testes abundantly express luteinizing hormone/choriogonadotropin receptor (LHCGR) as a seven transmembrane, G protein-coupled receptor glycoprotein. LHCGR influences the protective effect of pregnancy and Gonadotropin against breast cancer. The expression of LHCGR on breast carcinoma correlates in part to the degree of tumor differentiation. LHCGR -positive breast tumors occur more frequently in tumors with greater cell differentiation in premenopausal women.
UOM: 1 * 100 µG


Catalog Number: (PRSI33-442)
Supplier: ProSci Inc.
Description: Recognises 78 kDa moesin protein. Moesin, a member of the talin-4.1 superfamily, is a linking protein of the sub-membranous actin cytoskeleton. It is expressed in variable amounts in cells of different phenotypes such as macrophages, lymphocytes, fibroblastic, endothelial, epithelial, and neuronal cell lines but not in blood cells. The ERM proteins, ezrin, radixin, and moesin are involved in a variety of cellular functions, such as cell adhesion, migration, and the organization of cell surface structures, and are highly homologous, both in protein sequence and in functional activity, with merlin/schwannomin, a neurofibromatosis-2-associated tumor-suppressor protein. Cell lines of epithelial and mesothelial origin contain both moesin and radixin whereas cells of endothelial and lymphoid origin express moesin.
UOM: 1 * 100 µG


Catalog Number: (BOSSBS-8998R)
Supplier: Bioss
Description: The initiation of DNA replication is a multi-step process that depends on the formation of pre-replication complexes, which trigger initiation (1). Among the proteins required for establishing these complexes are the origin recognition complex (ORC) proteins (1). ORC proteins bind specifically to origins of replication where they serve as scaffold for the assembly of additional initiation factors (1). Human ORC subunits 1-6 are expressed in the nucleus of proliferating cells and tissues, such as the testis (2). ORC1 and ORC2 are both expressed at equivalent concentrations throughout the cell cycle; however, only ORC2 remains stably bound to chromatin (3,4). ORC4 and ORC6 are also expressed constantly throughout the cell cycle (5,6). ORC2, ORC3, ORC4 and ORC5 form a core complex upon which ORC6 and ORC1 assemble (7,8). The formation of this core complex suggests that ORC proteins play a crucial role in the G1-S transition in mammalian cells (8).
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-8998R-HRP)
Supplier: Bioss
Description: The initiation of DNA replication is a multi-step process that depends on the formation of pre-replication complexes, which trigger initiation (1). Among the proteins required for establishing these complexes are the origin recognition complex (ORC) proteins (1). ORC proteins bind specifically to origins of replication where they serve as scaffold for the assembly of additional initiation factors (1). Human ORC subunits 1-6 are expressed in the nucleus of proliferating cells and tissues, such as the testis (2). ORC1 and ORC2 are both expressed at equivalent concentrations throughout the cell cycle; however, only ORC2 remains stably bound to chromatin (3,4). ORC4 and ORC6 are also expressed constantly throughout the cell cycle (5,6). ORC2, ORC3, ORC4 and ORC5 form a core complex upon which ORC6 and ORC1 assemble (7,8). The formation of this core complex suggests that ORC proteins play a crucial role in the G1-S transition in mammalian cells (8).
UOM: 1 * 100 µl


Catalog Number: (PRSI34-132)
Supplier: ProSci Inc.
Description: Recognises 78 kDa moesin protein. Moesin, a member of the Talin-4.1 superfamily, is a linking protein of the submembraneous actin cytoskeleton. It is expressed in variable amounts in cells of different phenotypes such as macrophages, lymphocytes, fibroblastic, endothelial, epithelial, and neuronal cell lines but not in blood cells. The ERM proteins, ezrin, radixin, and moesin are involved in a variety of cellular functions, such as cell adhesion, migration, and the organization of cell surface structures, and are highly homologous, both in protein sequence and in functional activity, with merlin/schwannomin, a neurofibromatosis-2-associated tumor-suppressor protein. Cell lines of epithelial and mesothelial origin contain both moesin and radixin whereas cells of endothelial and lymphoid origin express moesin.
UOM: 1 * 100 µG


Catalog Number: (PRSI92-678)
Supplier: ProSci Inc.
Description: Decorin, also known as PG40 and DCN, is a member of the class I family of small leucine-rich proteoglycans (SLRPs) that is expressed in the stroma of various forms of cancer and has been recently proposed to act as a guardian from the matrix. Mature human Decorin contains 12 tandem LRR and shares 80% and 78% aa sequence identity with mouse and rat Decorin, respectively. Decorin embraces numerous functions including: regulation of collagen fibrillogenic, hepatic carcinogenesis, fetal membrane and calcium homeostasis, keratinocyte function, and suppression of angiogenesis. Most recently, soluble decorin has been shown to induce autophagy in endothelial cells and mitophagy in breast carcinoma cells.
UOM: 1 * 50 µG


Catalog Number: (BOSSBS-4250R-A555)
Supplier: Bioss
Description: The three dimensional structure of many extracellular proteins is stabilized by the formation of disulphide bonds. Studies suggest that a microsomal enzyme known as Protein Disulphide Isomerase (PDI) is involved in disulphide-bond formation and isomerization, as well as the reduction of disulphide bonds in proteins. PDI, which catalyses disulphide interchange between thiols and protein dilsulphides, has also been referred to as thiol:protein-disulphide oxidoreductase and as glutathione:insulin transhydrogenase because of its role in reduction of disulphide bonds. The highly conserved sequence Lys-Asp-Glu-Leu (KDEL) is present at the carboxy-terminus of PDI and other soluble endoplasmic reticulum (ER) resident proteins including the 78 and 94 kDa glucose regulated proteins (GRP78 and GRP94 respectively). The presence of carboxy-terminal KDEL appears to be necessary for ER retention and appears to be sufficient to reduce the secretion of proteins from the ER. This retention is reported to be mediated by a KDEL receptor.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11898R-CY5)
Supplier: Bioss
Description: NF-1, also designated CTF, consists of a family of CCAAT box binding proteins that stimulate DNA replication and activate transcription. Analysis of human NF-1 messenger RNA has revealed two forms of the NF-1 protein arising from an alternate splicing of a single NF-1 gene. NF-1 binds its consensus DNA element as a homodimer via an amino-terminal DNA binding domain, and activates transcription through a putatively novel, proline-rich, carboxy terminal transactivation domain. The NF-1 protein has been shown to recognize and bind the adenovirus type 2 promoter and activate transcription of herpes simplex virus thymidine kinase genes. The NF-1 consensus element has been found in the upstream promoter region of myriad eukaryotic genes, including that of Ha-Ras, alpha-globin, HSP 70, GRP 78, Histone H1, myelin basic protein and in the Xenopus laevis vitellogenin gene promoter.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11898R-A680)
Supplier: Bioss
Description: NF-1, also designated CTF, consists of a family of CCAAT box binding proteins that stimulate DNA replication and activate transcription. Analysis of human NF-1 messenger RNA has revealed two forms of the NF-1 protein arising from an alternate splicing of a single NF-1 gene. NF-1 binds its consensus DNA element as a homodimer via an amino-terminal DNA binding domain, and activates transcription through a putatively novel, proline-rich, carboxy terminal transactivation domain. The NF-1 protein has been shown to recognize and bind the adenovirus type 2 promoter and activate transcription of herpes simplex virus thymidine kinase genes. The NF-1 consensus element has been found in the upstream promoter region of myriad eukaryotic genes, including that of Ha-Ras, alpha-globin, HSP 70, GRP 78, Histone H1, myelin basic protein and in the Xenopus laevis vitellogenin gene promoter.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-4250R-CY5.5)
Supplier: Bioss
Description: The three dimensional structure of many extracellular proteins is stabilized by the formation of disulphide bonds. Studies suggest that a microsomal enzyme known as Protein Disulphide Isomerase (PDI) is involved in disulphide-bond formation and isomerization, as well as the reduction of disulphide bonds in proteins. PDI, which catalyses disulphide interchange between thiols and protein dilsulphides, has also been referred to as thiol:protein-disulphide oxidoreductase and as glutathione:insulin transhydrogenase because of its role in reduction of disulphide bonds. The highly conserved sequence Lys-Asp-Glu-Leu (KDEL) is present at the carboxy-terminus of PDI and other soluble endoplasmic reticulum (ER) resident proteins including the 78 and 94 kDa glucose regulated proteins (GRP78 and GRP94 respectively). The presence of carboxy-terminal KDEL appears to be necessary for ER retention and appears to be sufficient to reduce the secretion of proteins from the ER. This retention is reported to be mediated by a KDEL receptor.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11898R-A350)
Supplier: Bioss
Description: NF-1, also designated CTF, consists of a family of CCAAT box binding proteins that stimulate DNA replication and activate transcription. Analysis of human NF-1 messenger RNA has revealed two forms of the NF-1 protein arising from an alternate splicing of a single NF-1 gene. NF-1 binds its consensus DNA element as a homodimer via an amino-terminal DNA binding domain, and activates transcription through a putatively novel, proline-rich, carboxy terminal transactivation domain. The NF-1 protein has been shown to recognize and bind the adenovirus type 2 promoter and activate transcription of herpes simplex virus thymidine kinase genes. The NF-1 consensus element has been found in the upstream promoter region of myriad eukaryotic genes, including that of Ha-Ras, alpha-globin, HSP 70, GRP 78, Histone H1, myelin basic protein and in the Xenopus laevis vitellogenin gene promoter.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11898R-A555)
Supplier: Bioss
Description: NF-1, also designated CTF, consists of a family of CCAAT box binding proteins that stimulate DNA replication and activate transcription. Analysis of human NF-1 messenger RNA has revealed two forms of the NF-1 protein arising from an alternate splicing of a single NF-1 gene. NF-1 binds its consensus DNA element as a homodimer via an amino-terminal DNA binding domain, and activates transcription through a putatively novel, proline-rich, carboxy terminal transactivation domain. The NF-1 protein has been shown to recognize and bind the adenovirus type 2 promoter and activate transcription of herpes simplex virus thymidine kinase genes. The NF-1 consensus element has been found in the upstream promoter region of myriad eukaryotic genes, including that of Ha-Ras, alpha-globin, HSP 70, GRP 78, Histone H1, myelin basic protein and in the Xenopus laevis vitellogenin gene promoter.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-4250R-A750)
Supplier: Bioss
Description: The three dimensional structure of many extracellular proteins is stabilised by the formation of disulphide bonds. Studies suggest that a microsomal enzyme known as Protein Disulphide Isomerase (PDI) is involved in disulphide-bond formation and isomerization, as well as the reduction of disulphide bonds in proteins. PDI, which catalyses disulphide interchange between thiols and protein dilsulphides, has also been referred to as thiol:protein-disulphide oxidoreductase and as glutathione:insulin transhydrogenase because of its role in reduction of disulphide bonds. The highly conserved sequence Lys-Asp-Glu-Leu (KDEL) is present at the carboxy-terminus of PDI and other soluble endoplasmic reticulum (ER) resident proteins including the 78 and 94 kDa glucose regulated proteins (GRP78 and GRP94 respectively). The presence of carboxy-terminal KDEL appears to be necessary for ER retention and appears to be sufficient to reduce the secretion of proteins from the ER. This retention is reported to be mediated by a KDEL receptor.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-4250R-A647)
Supplier: Bioss
Description: The three dimensional structure of many extracellular proteins is stabilized by the formation of disulphide bonds. Studies suggest that a microsomal enzyme known as Protein Disulphide Isomerase (PDI) is involved in disulphide-bond formation and isomerization, as well as the reduction of disulphide bonds in proteins. PDI, which catalyses disulphide interchange between thiols and protein dilsulphides, has also been referred to as thiol:protein-disulphide oxidoreductase and as glutathione:insulin transhydrogenase because of its role in reduction of disulphide bonds. The highly conserved sequence Lys-Asp-Glu-Leu (KDEL) is present at the carboxy-terminus of PDI and other soluble endoplasmic reticulum (ER) resident proteins including the 78 and 94 kDa glucose regulated proteins (GRP78 and GRP94 respectively). The presence of carboxy-terminal KDEL appears to be necessary for ER retention and appears to be sufficient to reduce the secretion of proteins from the ER. This retention is reported to be mediated by a KDEL receptor.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-4250R-A350)
Supplier: Bioss
Description: The three dimensional structure of many extracellular proteins is stabilized by the formation of disulphide bonds. Studies suggest that a microsomal enzyme known as Protein Disulphide Isomerase (PDI) is involved in disulphide-bond formation and isomerization, as well as the reduction of disulphide bonds in proteins. PDI, which catalyses disulphide interchange between thiols and protein dilsulphides, has also been referred to as thiol:protein-disulphide oxidoreductase and as glutathione:insulin transhydrogenase because of its role in reduction of disulphide bonds. The highly conserved sequence Lys-Asp-Glu-Leu (KDEL) is present at the carboxy-terminus of PDI and other soluble endoplasmic reticulum (ER) resident proteins including the 78 and 94 kDa glucose regulated proteins (GRP78 and GRP94 respectively). The presence of carboxy-terminal KDEL appears to be necessary for ER retention and appears to be sufficient to reduce the secretion of proteins from the ER. This retention is reported to be mediated by a KDEL receptor.
UOM: 1 * 100 µl


Catalog Number: (PRSI3685)
Supplier: ProSci Inc.
Description: XBP-1 Antibody: X box binding protein 1 (XBP-1) is a key protein in the mammalian unfolded protein response (UPR) that protects the cell against the stress of malfolded proteins in the endoplasmic reticulum (ER). Upon sensing unfolded proteins, an ER transmembrane endonuclease and kinase termed IRE1p is activated and excises an intron from XBP-1 mRNA. The spliced XBP-1 mRNA results in a 371 amino acid protein (XBP-1s) which is then translocated to the nucleus where it binds to the regulatory elements of downstream genes. Together with other UPR transcription factors such as ATF6, XBP-1 stimulates the production of ER stress proteins including the ER resident protein chaperones glucose regulated protein (GRP) 78 and GRP94.
UOM: 1 * 100 µG


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Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the call is still displayed and you need assistance, please call us on +353 1 88 22222.
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