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trans-4-Methoxycyclohexan-1-amine
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trans-4-Methoxycyclohexan-1-amine
Supplier:
Biotium
Description:
Cytochrome c is a well-characterized mobile electron transport protein that is essential to energy conversion in all aerobic organisms. In mammalian cells, this highly conserved protein is normally localized to the mitochondrial inter-membrane space. More recent studies have identified cytosolic Cytochrome c as a factor necessary for activation of apoptosis. During apoptosis, Cytochrome c is trans-located from the mitochondrial membrane to the cytosol, where it is required for activation of caspase-3 (CPP32). Overexpression of Bcl-2 has been shown to prevent the translocation of Cytochrome c, thereby blocking the apoptotic process. Overexpression of Bax has been shown to induce the release of Cytochrome c and to induce cell death. The release of Cytochrome c from the mitochondria is thought to trigger an apoptotic cascade, whereby Apaf-1 binds to Apaf-3 (caspase-9) in a Cytochrome c-dependent manner, leading to caspase-9 cleavage of caspase-3.
CF® dyes are Biotium's next-generation fluorescent dyes. CF®555 is a bright orange-red fluorescent dye (Ex/Em 555/565 nm) that is compatible with super-resolution imaging by STORM.
Catalog Number:
(10272-736)
Supplier:
Bioss
Description:
The Hox proteins play a role in development and cellular differentiation by regulating downstream target genes. Specifically, the Hox proteins direct DNA-protein and protein-protein interactions that assist in determining the morphologic features associated with the anterior-posterior body axis. The mammalian HOX gene complex consists of 39 genes that are located on four linkage groups, which are dispersed over four chromosomes. HOX genes that occupy the same relative position along the 5’ to 3’ coordinate (trans-paralogous genes) are more similar in sequence and expression pattern than adjacent HOX genes on the same chromosome. HoxA3, in conjunction with Pax1, mediates the development of the thymus, parathyroid gland, and carotid body. Its expression in the third pharyngeal arch and pouch is required for development of the third arch artery, and homozygous null HoxA3 mutants lack the carotid body. HoxA3 also regulates hindbrain development by controlling the axon projection pattern of motor neurons and sensory neurons of the proximal and distal ganglia.
Catalog Number:
(10272-750)
Supplier:
Bioss
Description:
The Hox proteins play a role in development and cellular differentiation by regulating downstream target genes. Specifically, the Hox proteins direct DNA-protein and protein-protein interactions that assist in determining the morphologic features associated with the anterior-posterior body axis. The mammalian HOX gene complex consists of 39 genes that are located on four linkage groups, which are dispersed over four chromosomes. HOX genes that occupy the same relative position along the 5’ to 3’ coordinate (trans-paralogous genes) are more similar in sequence and expression pattern than adjacent HOX genes on the same chromosome. HoxA3, in conjunction with Pax1, mediates the development of the thymus, parathyroid gland, and carotid body. Its expression in the third pharyngeal arch and pouch is required for development of the third arch artery, and homozygous null HoxA3 mutants lack the carotid body. HoxA3 also regulates hindbrain development by controlling the axon projection pattern of motor neurons and sensory neurons of the proximal and distal ganglia.
Catalog Number:
(10663-584)
Supplier:
Bioss
Description:
Terminally differentiating mammalian epidermal cells acquire an insoluble, 10 to 20 nm thick protein deposit on the intracellular surface of the plasma membrane known as the cross-linked cell envelope (CE). The CE is a component of the epidermis that is generated through formation of disulfide bonds and g-glutamyl-lysine isodipeptide bonds, which are formed by the action of transglutaminases (TGases). TGases are intercellularly localizing, Ca2+-dependent enzymes that catalyze the formation of isopeptide bonds by transferring an amine on to glutaminyl residues, thereby cross-linking glutamine residues and lysine residues in substrate proteins. TGases influence numerous biological processes, including blood coagulation, epidermal differentiation, seminal fluid coagulation, fertilization, cell differentiation and apoptosis. Human keratinocyte transglutaminase (TGase1) is a membrane associated, 817 amino acid protein. Human tissue transglutaminase (TGase2) is an endothelial cell specific, 687 amino acid protein.
Catalog Number:
(10663-568)
Supplier:
Bioss
Description:
Terminally differentiating mammalian epidermal cells acquire an insoluble, 10 to 20 nm thick protein deposit on the intracellular surface of the plasma membrane known as the cross-linked cell envelope (CE). The CE is a component of the epidermis that is generated through formation of disulfide bonds and g-glutamyl-lysine isodipeptide bonds, which are formed by the action of transglutaminases (TGases). TGases are intercellularly localizing, Ca2+-dependent enzymes that catalyze the formation of isopeptide bonds by transferring an amine on to glutaminyl residues, thereby cross-linking glutamine residues and lysine residues in substrate proteins. TGases influence numerous biological processes, including blood coagulation, epidermal differentiation, seminal fluid coagulation, fertilization, cell differentiation and apoptosis. Human keratinocyte transglutaminase (TGase1) is a membrane associated, 817 amino acid protein. Human tissue transglutaminase (TGase2) is an endothelial cell specific, 687 amino acid protein.
Catalog Number:
(PI90407)
Supplier:
Invitrogen
Description:
The Thermo Scientific™ Pierce™ Antibody Biotinylation Kit for IP provides biotinylation reagents designed specifically for the labeling of primary antibodies used in immunoprecipitation applications.Optimized for IP—reagents and protocols developed specifically to address antibody labeling for immunoprecipitation applicationsEasy to use—kit configuration specifically optimized to accommodate 50–200 µg of antibody in a 100 µL reaction; desalting columns are provided to remove excess biotinylation reagent after labelingAmine reactive—reacts with primary amines (-NH2) of antibodiesEnhanced solubility—pegylation improves water solubility of the biotinylated antibody and prevents aggregation upon storageReduced steric hindrance—longer spacer arm (29 angstroms) minimize steric hindrance when binding to avidin moleculesThe Pierce Antibody Biotinylation Kit reagents have been optimized and validated to biotin label antibodies for IP and co-IP reactions
Catalog Number:
(76109-482)
Supplier:
Bioss
Description:
Terminally differentiating mammalian epidermal cells acquire an insoluble, 10 to 20 nm thick protein deposit on the intracellular surface of the plasma membrane known as the cross-linked cell envelope (CE). The CE is a component of the epidermis that is generated through formation of disulfide bonds and g-glutamyl-lysine isodipeptide bonds, which are formed by the action of transglutaminases (TGases). TGases are intercellularly localizing, Ca2+-dependent enzymes that catalyze the formation of isopeptide bonds by transferring an amine on to glutaminyl residues, thereby cross-linking glutamine residues and lysine residues in substrate proteins. TGases influence numerous biological processes, including blood coagulation, epidermal differentiation, seminal fluid coagulation, fertilization, cell differentiation and apoptosis. Human keratinocyte transglutaminase (TGase1) is a membrane associated, 817 amino acid protein. Human tissue transglutaminase (TGase2) is an endothelial cell specific, 687 amino acid protein.
Catalog Number:
(10272-742)
Supplier:
Bioss
Description:
The Hox proteins play a role in development and cellular differentiation by regulating downstream target genes. Specifically, the Hox proteins direct DNA-protein and protein-protein interactions that assist in determining the morphologic features associated with the anterior-posterior body axis. The mammalian HOX gene complex consists of 39 genes that are located on four linkage groups, which are dispersed over four chromosomes. HOX genes that occupy the same relative position along the 5’ to 3’ coordinate (trans-paralogous genes) are more similar in sequence and expression pattern than adjacent HOX genes on the same chromosome. HoxA3, in conjunction with Pax1, mediates the development of the thymus, parathyroid gland, and carotid body. Its expression in the third pharyngeal arch and pouch is required for development of the third arch artery, and homozygous null HoxA3 mutants lack the carotid body. HoxA3 also regulates hindbrain development by controlling the axon projection pattern of motor neurons and sensory neurons of the proximal and distal ganglia.
Catalog Number:
(10663-580)
Supplier:
Bioss
Description:
Terminally differentiating mammalian epidermal cells acquire an insoluble, 10 to 20 nm thick protein deposit on the intracellular surface of the plasma membrane known as the cross-linked cell envelope (CE). The CE is a component of the epidermis that is generated through formation of disulfide bonds and g-glutamyl-lysine isodipeptide bonds, which are formed by the action of transglutaminases (TGases). TGases are intercellularly localizing, Ca2+-dependent enzymes that catalyze the formation of isopeptide bonds by transferring an amine on to glutaminyl residues, thereby cross-linking glutamine residues and lysine residues in substrate proteins. TGases influence numerous biological processes, including blood coagulation, epidermal differentiation, seminal fluid coagulation, fertilization, cell differentiation and apoptosis. Human keratinocyte transglutaminase (TGase1) is a membrane associated, 817 amino acid protein. Human tissue transglutaminase (TGase2) is an endothelial cell specific, 687 amino acid protein.
Catalog Number:
(76118-408)
Supplier:
Bioss
Description:
NAD-dependent oxidoreductase with broad substrate specificity that shows both oxidative and reductive activity (<i>in vitro</i>). Has 17-beta-hydroxysteroid dehydrogenase activity towards various steroids (<i>in vitro</i>). Converts 5-alpha-androstan-3-alpha,17-beta-diol to androsterone and estradiol to estrone (<i>in vitro</i>). Has 3-alpha-hydroxysteroid dehydrogenase activity towards androsterone (<i>in vitro</i>). Has retinol dehydrogenase activity towards all-trans-retinol (<i>in vitro</i>). Can convert androsterone to epi-androsterone. Androsterone is first oxidized to 5-alpha-androstane-3,17-dione and then reduced to epi-andosterone. Can act on both C-19 and C-21 3-alpha-hydroxysteroids.Tissue specificity; Detected in liver and prostate (at protein level). Detected in adult liver, lung, brain, placenta, prostate, adrenal gland, testis, mammary gland, spleen, spinal cord and uterus. Detected in caudate nucleus, and at lower levels in amygdala, corpus callosum, hippocampus, substantia nigra and thalamus. Detected in fetal lung, liver and brain.Sequence similarities; Belongs to the short-chain dehydrogenases/reductases (SDR) family.
Catalog Number:
(10663-582)
Supplier:
Bioss
Description:
Terminally differentiating mammalian epidermal cells acquire an insoluble, 10 to 20 nm thick protein deposit on the intracellular surface of the plasma membrane known as the cross-linked cell envelope (CE). The CE is a component of the epidermis that is generated through formation of disulfide bonds and g-glutamyl-lysine isodipeptide bonds, which are formed by the action of transglutaminases (TGases). TGases are intercellularly localizing, Ca2+-dependent enzymes that catalyze the formation of isopeptide bonds by transferring an amine on to glutaminyl residues, thereby cross-linking glutamine residues and lysine residues in substrate proteins. TGases influence numerous biological processes, including blood coagulation, epidermal differentiation, seminal fluid coagulation, fertilization, cell differentiation and apoptosis. Human keratinocyte transglutaminase (TGase1) is a membrane associated, 817 amino acid protein. Human tissue transglutaminase (TGase2) is an endothelial cell specific, 687 amino acid protein.
Catalog Number:
(10663-586)
Supplier:
Bioss
Description:
Terminally differentiating mammalian epidermal cells acquire an insoluble, 10 to 20 nm thick protein deposit on the intracellular surface of the plasma membrane known as the cross-linked cell envelope (CE). The CE is a component of the epidermis that is generated through formation of disulfide bonds and g-glutamyl-lysine isodipeptide bonds, which are formed by the action of transglutaminases (TGases). TGases are intercellularly localizing, Ca2+-dependent enzymes that catalyze the formation of isopeptide bonds by transferring an amine on to glutaminyl residues, thereby cross-linking glutamine residues and lysine residues in substrate proteins. TGases influence numerous biological processes, including blood coagulation, epidermal differentiation, seminal fluid coagulation, fertilization, cell differentiation and apoptosis. Human keratinocyte transglutaminase (TGase1) is a membrane associated, 817 amino acid protein. Human tissue transglutaminase (TGase2) is an endothelial cell specific, 687 amino acid protein.
Catalog Number:
(89145-514)
Supplier:
Enzo Life Sciences
Description:
Immunophilins are a family of soluble cytosolic receptors capable of binding to one of two major immunosuppressant agents - cyclosporin A (CsA) or FK506. Proteins that bind FK506 are termed FK506 Binding Proteins (FKBPs) and those that bind cyclosporin A are called cyclophilins (CyP).
Both CyP:CsA and FKBP:FK506 complexes have been shown to inhibit calcineurin, a calcium and calmodulin dependent protein phosphatase which has been implicated as an important signalling enzyme in T-cell activation, providing a possible mechanism of immunosuppression by CsA and FK506. Immunophilins function as peptidyl prolyl cis-trans-isomerases (PPIase) whose activity is inhibited by their respective immunosuppressant compounds. As PPIase's, immunophilins accelerate folding of some proteins both in vivo and in vitro by catalyzing slow steps in the initial folding and rearrangement of proline containing proteins. Within the cyclophilin family, there are several different proteins which show a high degree of homology including CyPA, CyPB and CyPC. CyPA, also termed CyP-18, is the most abundant and ubiquitous cyclophilin found in all vertebrate tissues and is present in T-cells.
Catalog Number:
(10672-168)
Supplier:
Bioss
Description:
IGSF11 is also known as BTIGSF (brain and testis-specific immunoglobulin superfamily protein) or VSIG3 (V-set and immunoglobulin domain-containing protein 3) and is a 431 amino acid protein that is expressed as three isoforms. IGSF11 is highly expressed in testis and ovary and is also expressed in brain, kidney and skeletal muscle, localized to the cellular membrane as a single-pass membrane protein. IGSF11 is an immunoglobulin with V-type and C2-type domains that function in molecular recognition. When IGSF11 is in the trans position, it plays an important role in cell-cell adhesion via both homophilic and heterophilic interactions with other molecules. These cell–cell interactions are also thought to be important for neuronal cell interactions, such as neuron–neuron or neuron–glia interactions, which are important for the development and function of the central nervous system. In addition, IGSF11 might also be involved interactions between Sertoli cells and spermatocytes, which are important associations during spermatogenesis. The IGSF11 gene is commonly upregulated in gastric cancer and IGSF11 is highly expressed in many types of human tumors, indicating that it may be useful as a target for immunotherapy.
Catalog Number:
(10669-006)
Supplier:
Bioss
Description:
IGSF11 is also known as BTIGSF (brain and testis-specific immunoglobulin superfamily protein) or VSIG3 (V-set and immunoglobulin domain-containing protein 3) and is a 431 amino acid protein that is expressed as three isoforms. IGSF11 is highly expressed in testis and ovary and is also expressed in brain, kidney and skeletal muscle, localized to the cellular membrane as a single-pass membrane protein. IGSF11 is an immunoglobulin with V-type and C2-type domains that function in molecular recognition. When IGSF11 is in the trans position, it plays an important role in cell-cell adhesion via both homophilic and heterophilic interactions with other molecules. These cell–cell interactions are also thought to be important for neuronal cell interactions, such as neuron–neuron or neuron–glia interactions, which are important for the development and function of the central nervous system. In addition, IGSF11 might also be involved interactions between Sertoli cells and spermatocytes, which are important associations during spermatogenesis. The IGSF11 gene is commonly upregulated in gastric cancer and IGSF11 is highly expressed in many types of human tumors, indicating that it may be useful as a target for immunotherapy.
Catalog Number:
(75789-564)
Supplier:
Prosci
Description:
Nectin-1 is a type I transmembrane glycoprotein belonging to the Ig superfamily. Nectin-1 promotes cell-cell contacts by forming homophilic or heterophilic trans-dimers. Heterophilic interactions have been detected between Nectin-1 and Nectin-3 and between Nectin-1 and Nectin-4. Nectin ECDs contain three Ig like domains: an N terminal V type that mediates ligand binding, and two C2 type. Nectin-1 binds viral Glycoprotein D to mediate Herpesvirus (but not Poxvirus) entry into vaginal mucosa, sensory neurons and fibroblasts. In forming adherens junctions and synapses, Nectin-1 and Nectin-3 initiate cell-cell interactions, recruiting alphav beta 3 integrin extracellularly and cadherins intracellularly through afadin and other junctional proteins. These interactions organize the cytoskeleton, strengthen attachment to basement membrane and promote further cell-cell connections. Nectin-1 and Nectin-3 have been found to localize assymetrically along the chemical synapse, with Nectin-1 primarily on the axonal side and Nectin-3 on the dendritic side. Deficiency of Nectin-1 can result in cleft lip/palate ectodermal dysplasia. Nectin-1 downregulation in epithelial cancers is mediated in part by ectodomain shedding, but it may contribute to invasiveness.
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