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Masterflex+Single-use+Flow+Sensor
Numéro de catalogue:
(BOSSBS-3686R-A488)
Fournisseur:
Bioss
Description:
Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF1B. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. EGLN1 is the most important isozyme under normoxia and, through regulating the stability of HIF1, involved in various hypoxia-influenced processes such as angiogenesis in retinal and cardiac functionality. Target proteins are preferencially recognized via a LXXLAP motif.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3686R-A647)
Fournisseur:
Bioss
Description:
Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF1B. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. EGLN1 is the most important isozyme under normoxia and, through regulating the stability of HIF1, involved in various hypoxia-influenced processes such as angiogenesis in retinal and cardiac functionality. Target proteins are preferencially recognized via a LXXLAP motif.
UOM:
1 * 100 µl
Numéro de catalogue:
(ENZOALX801035C100)
Fournisseur:
ENZO LIFE SCIENCES
Description:
Bile Salts
Bile salts are important physiological agents that serve a number of functions, including absorption, solubilization, transport and secretion of lipids. In the liver, they participate in the generation of bile flow and the secretion of cholesterol and phospholipids, such as phosphatidylcholine. When released into the intestine, they facilitate the uptake of cholesterol, fat-soluble vitamins and other lipids. Moreover, the biosynthesis of bile acids from cholesterol is the most significant pathway for the elimination of cholesterol from the body. However, because of their detergent properties, bile acids are inherently cytotoxic and disruptions in their normal transport or secretion can result in a variety of pathophysiological conditions. BSEP Bile formation is an important function of the liver. It is mediated by hepatocytes which generate bile flow within the bile canaliculi by continuous vectorial secretion of bile salts and other solutes across their canalicular (apical) membrane. Bile secretion is mediated by several ATP-binding cassette (ABC) transporters located in the canalicular membrane of hepatocytes. Among these ABC transporters, the bile salt export pump (BSEP or ABCB11) represents the primary, if not sole transport system for the canalicular excretion of bile salts. Bile secretory failure results in cholestasis and progressive familial intrahepatic cholestasis (PFIC) in infancy represents a group of inherited cholestatic diseases that are classified into three subtypes. One of these subtypes, PFIC II, is associated with mutations in the BSEP gene. PFIC patients with mutations in the BSEP gene have normal γ-glutamyltransferase activity, low concentrations of bile salts in bile, and an absence of bile duct proliferation. Additionally, human obesity is associated with altered cholesterol homeostasis including increased production and turnover, as well as secretion of excess cholesterol from the liver into bile. BSEP is a multifunctional polypeptide with two homologous halves, each containing a hydrophobic membrane-ancoring domain and an ATP-binding cassette (ABC) domain. The membrane-anchoring domain is composed of six helixes buried in the lipid bilayer of the plasma membrane and the ATP binding ABCs are exposed to the cytosol. The membrane-anchoring domain helixes are thought to form channels spanning the plasma membrane.
UOM:
1 * 1 EA
New Product
Numéro de catalogue:
(1.04148.0001)
Fournisseur:
Merck
Description:
Rapides, ces tests facilitent le screening des micro-organismes pathogènes. Tests complets pour la détection des germes pathogènes et des toxines. Les résultats sont fiables et disponibles en seulement 20 minutes après pré-enrichissement. Les milieux d'enrichissement spécifiques aident à garantir la précision et la fiabilité des résultats des tests. Le format One-Step évite les erreurs durant la manipulation.
UOM:
1 * 25 Tests
Fournisseur:
Biotium
Description:
This MAb recognizes human 17-26 kDa protein, which is identified as cytokine TNF-alpha (Tumor Necrosis Factor-alpha). TNF-alpha can be expressed as a 17 kDa free molecule, or as a 26 kDa membrane protein. TNF-alpha is a protein secreted by lipopolysaccharide-stimulated macrophages, and causes tumor necrosis when injected into tumor bearing mice. TNF alpha is believed to mediate pathogenic shock and tissue injury associated with endotoxemia. TNF alpha exists as a multimer of two, three, or five non-covalently linked units, but shows a single 17 kDa band following SDS PAGE under non-reducing conditions. TNF alpha is closely related to the 25 kDa protein Tumor Necrosis Factor beta (lymphotoxin), sharing the same receptors and cellular actions. TNF alpha causes cytolysis of certain transformed cells, being synergistic with interferon gamma in its cytotoxicity. Although it has little effect on many cultured normal human cells, TNF alpha appears to be directly toxic to vascular endothelial cells. Other actions of TNF alpha include stimulating growth of human fibroblasts and other cell lines, activating polymorphonuclear neutrophils and osteoclasts, and induction of interleukin 1, prostaglandin E2 and collagenase production. TNF alpha is currently being evaluated in treatment of certain cancers and AIDS Related Complex.
Numéro de catalogue:
(BOSSBS-3271R-HRP)
Fournisseur:
Bioss
Description:
c-Met, a member of the tyrosine kinase superfamily, is the receptor for hepatocyte growth factor, also known as scatter factor (HGF/SF). The mature c-Met protein is a disulfide-linked heterodimer with Mr=190 kDa composed of a heavily glycosylated alpha subunit that is completely extracellular in localization, and a beta subunit comprising an extracellular ligand binding domain, a single transmembrane domain, and a cytoplasmic tyrosine kinase domain. Cells expressing c-Met include epithelial cells, endothelial cells, blood cells of various types, and glomerular mesenchymal cells.HGF/SF binding to c-Met stimulates receptor dimerization and the phosphorylation of numerous residues within the receptor’s cytoplasmic domain. Signaling proteins that are phosphorylated and/or localized in response to c-Met phosphorylation include: Grb2, Shc, Cbl, Crk, cortactin, paxillin, GAB1, PI3K, FAK, Src, Ras, ERK1 and 2, JNK, PLC gamma, AKT, and STAT3. HGF/SF stimulation of c-Met expressing cells enhances proliferation, migration, morphogenesis, and protease synthesis, characteristics that are associated with invasive cell phenotype. Many types of cancer exhibit sustained c-Met stimulation, overexpression, or mutation, including carcinomas of the colon, breast, ovary, lung, liver, prostate, thyroid, kidney, as well as melanomas and sarcomas. In addition to cancer studies, other research areas in which c-Met is under investigation include organogenesis, organ regeneration, angiogenesis and surgical wound healing.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1922R-A750)
Fournisseur:
Bioss
Description:
Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and plays a central role in telomere maintenance and protection against end-to-end fusion of chromosomes. In addition to its telomeric DNA-binding role, required to recruit a number of factors and enzymes required for telomere protection, including the shelterin complex, TERF2IP/RAP1 and DCLRE1B/Apollo. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded 5'-TTAGGG-3' repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Together with DCLRE1B/Apollo, plays a key role in telomeric loop (T loop) formation by generating 3' single-stranded overhang at the leading end telomeres: T loops have been proposed to protect chromosome ends from degradation and repair. Required both to recruit DCLRE1B/Apollo to telomeres and activate the exonuclease activity of DCLRE1B/Apollo. Preferentially binds to positive supercoiled DNA. Together with DCLRE1B/Apollo, required to control the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B) needed for telomere replication during fork passage and prevent aberrant telomere topology. Recruits TERF2IP/RAP1 to telomeres, thereby participating in to repressing homology-directed repair (HDR), which can affect telomere length.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1922R-A488)
Fournisseur:
Bioss
Description:
Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and plays a central role in telomere maintenance and protection against end-to-end fusion of chromosomes. In addition to its telomeric DNA-binding role, required to recruit a number of factors and enzymes required for telomere protection, including the shelterin complex, TERF2IP/RAP1 and DCLRE1B/Apollo. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded 5'-TTAGGG-3' repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Together with DCLRE1B/Apollo, plays a key role in telomeric loop (T loop) formation by generating 3' single-stranded overhang at the leading end telomeres: T loops have been proposed to protect chromosome ends from degradation and repair. Required both to recruit DCLRE1B/Apollo to telomeres and activate the exonuclease activity of DCLRE1B/Apollo. Preferentially binds to positive supercoiled DNA. Together with DCLRE1B/Apollo, required to control the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B) needed for telomere replication during fork passage and prevent aberrant telomere topology. Recruits TERF2IP/RAP1 to telomeres, thereby participating in to repressing homology-directed repair (HDR), which can affect telomere length.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3686R-HRP)
Fournisseur:
Bioss
Description:
Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF1B. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. EGLN1 is the most important isozyme under normoxia and, through regulating the stability of HIF1, involved in various hypoxia-influenced processes such as angiogenesis in retinal and cardiac functionality. Target proteins are preferencially recognized via a LXXLAP motif.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-10994R-CY7)
Fournisseur:
Bioss
Description:
Serine/threonine-protein kinase that acts as a molecular sensor for DNA damage. Involved in DNA nonhomologous end joining (NHEJ) required for double-strand break (DSB) repair and V(D)J recombination. Must be bound to DNA to express its catalytic properties. Promotes processing of hairpin DNA structures in V(D)J recombination by activation of the hairpin endonuclease artemis (DCLRE1C). The assembly of the DNA-PK complex at DNA ends is also required for the NHEJ ligation step. Required to protect and align broken ends of DNA. May also act as a scaffold protein to aid the localization of DNA repair proteins to the site of damage. Found at the ends of chromosomes, suggesting a further role in the maintenance of telomeric stability and the prevention of chromosomal end fusion. Also involved in modulation of transcription. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates 'Ser-139' of histone variant H2AX/H2AFX, thereby regulating DNA damage response mechanism. Phosphorylates DCLRE1C, c-Abl/ABL1, histone H1, HSPCA, c-jun/JUN, p53/TP53, PARP1, POU2F1, DHX9, SRF, XRCC1, XRCC1, XRCC4, XRCC5, XRCC6, WRN, c-myc/MYC and RFA2. Can phosphorylate C1D not only in the presence of linear DNA but also in the presence of supercoiled DNA. Ability to phosphorylate TP53/p53 in the presence of supercoiled DNA is dependent on C1D.
UOM:
1 * 100 µl
Fournisseur:
Bohlender
Description:
Unité d'affichage pour commander le b.safe Splitter, qui est disponible en option conjointement avec les capteurs de niveau de remplissage connectés dans les b.safe Waste Caps et b.safe System Waste Caps.
Numéro de catalogue:
(BOSSBS-11420R-CY5)
Fournisseur:
Bioss
Description:
Neuromedin U is a neuropeptide with high activity on smooth muscle. It is widely expressed in gastrointestinal systems and central nervous system (CNS). Peripheral activities of neuromedin U include smooth muscle stimulation, ion transport alterations in the gut and the regulation of local blood flow and adrenocortical function. Neuromedin U receptors 1 and 2 (NMUR1 and NMUR2) are multi-pass membrane proteins that belong to the G-protein coupled receptor 1 family of proteins. Both NMUR1 and NMUR2 act as receptors for the neuromedin U neuropeptide. NMUR1 is detected in peripheral organs, particularly in urogenital and gastrointestinal systems, with highest levels in testis. It’s expression in CNS is low, but the protein has been detected in cerebellum, hippocampus, dorsal root ganglia and spinal cord. NMUR2 is predominantly detected in central nervous system with highest levels detected in medulla oblongata, spinal cord and thalamus. It may also be detected in testis but has low levels of expression in peripheral tissues.
UOM:
1 * 100 µl
Fournisseur:
VWR Collection
Description:
Électrodes de pH avec câble fixe d'un mètre.
Fournisseur:
SI Analytics
Description:
The ViscoSystem AVS 470 is the first measuring device that allows suction and pressure measurements completely independent of a PC.
Fournisseur:
TESTO
Description:
The testo 826 infrared thermometer allows quick temperature scans by means of infrared measurement without damaging the products. Non-contact measurement of surface temperature, ideally suitable for the food sector.
Fournisseur:
MEMMERT
Description:
Interface de boucle, pour courant 4 - 20 mA, température d'un capteur Pt100 librement positionné dans 3 chambres maximum, ICH
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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
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