Supplier >
Bioss
Imprimer
Votre recherche pour:
92 270 les résultats ont été trouvés
Bioss
Numéro de catalogue:
(BOSSBS-15050R-CY3)
Fournisseur:
Bioss
Description:
C1orf191
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3349R-A680)
Fournisseur:
Bioss
Description:
postsynaptic density protein 95 is a molecular scaffolding protein that binds and clusters N-methyl-D-aspartate receptors at neuronal synapses; may be involved in guanine nucleotide-mediated signal transduction pathway. This gene encodes a member of the membrane-associated guanylate kinase (MAGUK) family. It heteromultimerizes with DLG2. With DLG2 it is recruited into the same NMDA receptor and potassium channel clusters. These two MAGUK proteins may interact at postsynaptic sites to form a multimeric scaffold for the clustering of receptors, ion channels, and associated signaling proteins.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3349R-CY7)
Fournisseur:
Bioss
Description:
postsynaptic density protein 95 is a molecular scaffolding protein that binds and clusters N-methyl-D-aspartate receptors at neuronal synapses; may be involved in guanine nucleotide-mediated signal transduction pathway. This gene encodes a member of the membrane-associated guanylate kinase (MAGUK) family. It heteromultimerizes with DLG2. With DLG2 it is recruited into the same NMDA receptor and potassium channel clusters. These two MAGUK proteins may interact at postsynaptic sites to form a multimeric scaffold for the clustering of receptors, ion channels, and associated signaling proteins.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-6864R-CY5)
Fournisseur:
Bioss
Description:
May mediate activation of CASP1 via ASC and promote activation of NF-kappa-B via IKK.NALP proteins are cytoplasmic proteins that form a subfamily within the larger CATERPILLER family and are thought to play a crucial role in cell proliferation and reproduction. Like all other NALP family members, NALP12, also known as Monarch-1, has a C-terminal leucine-rich repeat (LRR) region, an N-terminal Pyrin domain (PYD) followed by a NACHT domain, and a NACHT-associated domain. NALP12 is thought to act as an attenuating factor of inflammation by suppressing inflammatory responses such as NF-kB activation by TLR-signaling molecules MyD88, IRAK-1, TRAF6 and RIPK1 in activated monocytes. Recent evidence suggests that mutations in NALP12 result in hereditary periodic fever syndromes.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3349R-CY5)
Fournisseur:
Bioss
Description:
postsynaptic density protein 95 is a molecular scaffolding protein that binds and clusters N-methyl-D-aspartate receptors at neuronal synapses; may be involved in guanine nucleotide-mediated signal transduction pathway. This gene encodes a member of the membrane-associated guanylate kinase (MAGUK) family. It heteromultimerizes with DLG2. With DLG2 it is recruited into the same NMDA receptor and potassium channel clusters. These two MAGUK proteins may interact at postsynaptic sites to form a multimeric scaffold for the clustering of receptors, ion channels, and associated signaling proteins.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-0638R-A647)
Fournisseur:
Bioss
Description:
Transmembrane serine/threonine kinase forming with the TGF-beta type II serine/threonine kinase receptor, TGFBR2, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and the activation of TGFBR1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non-canonical, SMAD-independent TGF-beta signaling pathways. For instance, TGFBR1 induces TRAF6 autoubiquitination which in turn results in MAP3K7 ubiquitination and activation to trigger apoptosis. Also regulates epithelial to mesenchymal transition through a SMAD-independent signaling pathway through PARD6A phosphorylation and activation.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1703R-A555)
Fournisseur:
Bioss
Description:
Serine/threonine-protein kinase that acts as a regulatory link between the membrane-associated Ras GTPases and the MAPK/ERK cascade, and this critical regulatory link functions as a switch determining cell fate decisions including proliferation, differentiation, apoptosis, survival and oncogenic transformation. RAF1 activation initiates a mitogen-activated protein kinase (MAPK) cascade that comprises a sequential phosphorylation of the dual-specific MAPK kinases (MAP2K1/MEK1 and MAP2K2/MEK2) and the extracellular signal-regulated kinases (MAPK3/ERK1 and MAPK1/ERK2). The phosphorylated form of RAF1 (on residues Ser-338 and Ser-339, by PAK1) phosphorylates BAD/Bcl2-antagonist of cell death at 'Ser-75'. Phosphorylates adenylyl cyclases: ADCY2, ADCY5 and ADCY6, resulting in their activation. Phosphorylates PPP1R12A resulting in inhibition of the phosphatase activity. Phosphorylates TNNT2/cardiac muscle troponin T. Can promote NF-kB activation and inhibit signal transducers involved in motility (ROCK2), apoptosis (MAP3K5/ASK1 and STK3/MST2), proliferation and angiogenesis (RB1). Can protect cells from apoptosis also by translocating to the mitochondria where it binds BCL2 and displaces BAD/Bcl2-antagonist of cell death. Regulates Rho signaling and migration, and is required for normal wound healing. Plays a role in the oncogenic transformation of epithelial cells via repression of the TJ protein, occludin (OCLN) by inducing the up-regulation of a transcriptional repressor SNAI2/SLUG, which induces down-regulation of OCLN. Restricts caspase activation in response to selected stimuli, notably Fas stimulation, pathogen-mediated macrophage apoptosis, and erythroid differentiation.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1407R-A488)
Fournisseur:
Bioss
Description:
Required for activity of the Ah (dioxin) receptor. This protein is required for the ligand-binding subunit to translocate from the cytosol to the nucleus after ligand binding. The complex then initiates transcription of genes involved in the activation of PAH procarcinogens. The heterodimer with HIF1A or EPAS1/HIF2A functions as a transcriptional regulator of the adaptive response to hypoxia.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-0236R-A555)
Fournisseur:
Bioss
Description:
The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is adenylate cyclase inhibition. Signaling promotes phospholipase C activity, leading to the release of inositol trisphosphate (IP3); this then triggers calcium ion release into the cytosol.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1953R-A555)
Fournisseur:
Bioss
Description:
May play a role in vesicle-mediated protein trafficking to lysosomal compartments and in membrane docking/fusion reactions of late endosomes/lysosomes.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13254R-CY3)
Fournisseur:
Bioss
Description:
This gene encodes acid alpha-glucosidase, which is essential for the degradation of glycogen to glucose in lysosomes. Different forms of acid alpha-glucosidase are obtained by proteolytic processing. Defects in this gene are the cause of glycogen storage disease II, also known as Pompe's disease, which is an autosomal recessive disorder with a broad clinical spectrum. Three transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008].
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11268R-A488)
Fournisseur:
Bioss
Description:
Degradation in endoplasmic reticulum proteins, also designated Derlins or DERtrins, are crucial for the degradation of misfolded endoplasmic reticulum (ER) luminal proteins. Derlin proteins are multi-pass membrane proteins localizing to the ER. Derlins are involved in transferring misfolded proteins from the ER to the cytosol, where the misfolded proteins are destroyed in an ubiquitin-dependent manner by the proteasome. In the case of cytomegalovirus infection, Derlin-1, as opposed to Derlins-2 and -3, is involved in the export of MHC class I heavy chains from the ER via its interaction with the viral protein US11. Derlins may also be important for cell proliferation.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3567R-HRP)
Fournisseur:
Bioss
Description:
SHIP1 is a member of the inositol polyphosphate-5-phosphatase (INPP5) family and contains an N-terminal SH2 domain, an inositol phosphatase domain, and two C-terminal protein interaction domains. Expression of this protein is restricted to hematopoietic cells where its movement from the cytosol to the plasma membrane is mediated by tyrosine phosphorylation in response to multiple cytokine and B and T cell receptor activation. At the plasma membrane, the protein hydrolyzes the 5' phosphate from phosphatidylinositol (3,4,5)-trisphosphate and inositol-1,3,4,5-tetrakisphosphate, thereby affecting multiple signaling pathways. Overall the protein functions as a negative regulator of myeliod cell proliferation and survival.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3568R-CY5.5)
Fournisseur:
Bioss
Description:
Involved in chromosome cohesion during cell cycle and in DNA repair. Central component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. Involved in DNA repair via its interaction with BRCA1 and its related phosphorylation by ATM, or via its phosphorylation by ATR. Works as a downstream effector both in the ATM/NBS1 branch and in the ATR/MSH2 branch of S-phase checkpoint.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3568R-CY5)
Fournisseur:
Bioss
Description:
Involved in chromosome cohesion during cell cycle and in DNA repair. Central component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. Involved in DNA repair via its interaction with BRCA1 and its related phosphorylation by ATM, or via its phosphorylation by ATR. Works as a downstream effector both in the ATM/NBS1 branch and in the ATR/MSH2 branch of S-phase checkpoint.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13265R-A350)
Fournisseur:
Bioss
Description:
GALE is a 348 amino acid protein that functions as the third enzyme in the Leloir pathway of galactose metabolism. A member of the sugar epimerase family, GALE exists as a homodimer, binds FAD as a cofactor and catalyzes the epimerization of UDP-N-acetylglucosamine to UDP-N-acetylgalactosamine and UDP-glucose to UDP-galactose. The gene encoding GALE maps to human chromosome 1p36.11 and mutations in this gene lead to the development of complex disorder known as epimerase-deficiency galactosemia (EDG) or galactosemia type 3, which is characterized by mental retardation, liver damage, cataracts and deafness.
UOM:
1 * 100 µl
Appel de prix
Le stock de cet article est limité mais peut être disponible dans un entrepôt proche de vous. Merci de vous assurer que vous êtes connecté sur le site afin que le stock disponible soit affiché. Si l'
 est toujours affiché et vous avez besoin d'aide, s'il vous plaît appelez-nous au 016 385 011
Le stock de cet article est limité mais peut être disponible dans un entrepôt proche de vous. Merci de vous assurer que vous êtes connecté sur le site afin que le stock disponible soit affiché. Si l'
est toujours affiché et vous avez besoin d'aide, s'il vous plaît appelez-nous au 016 385 011
Ces articles ne peuvent être ajoutés au Panier. Veuillez contacter votre service client ou envoyer un e-mail à vwr.be@vwr.com
Une documentation supplémentaire peut être nécessaire pour l'achat de cet article. Un représentant de VWR vous contactera si nécessaire.
Ce produit a été bloqué par votre organisation. Contacter votre service d'achat pour plus d'informations.
Le produit original n'est plus disponible. Le remplacement représenté est disponible
Les produits marqués de ce symbole ne seront bientôt plus disponibles - vente jusqu'à épuisement de stock. Des alternatives peuvent être disponibles en recherchant le code article VWR indiqué ci-dessus. Si vous avez besoin d'une assistance supplémentaire, veuillez contacter notre Service Clientèle au 016 385 011.
|
|||||||||
Vue liste
