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Fournisseur:  Biotium
Description:   This antibody neutralises HurTNFamediated cytotoxicity of L929 cells and inhibits tumour growth in mice. It protects mice against toxicity of HurTNFa. Tumor Necrosis Factor Alpha (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.
UOM:  1 * 50 µl
Numéro de catalogue: (BOSSBS-5693R-A350)

Fournisseur:  Bioss
Description:   As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage. In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response. It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair. Plays also a role in base excision repair (BER) probably through interaction with UNG. Through RFWD3 may activate CHEK1 and play a role in replication checkpoint control. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance.
UOM:  1 * 100 µl
Fournisseur:  Biotium
Description:   This antibody neutralises HurTNFamediated cytotoxicity of L929 cells and inhibits tumour growth in mice. It protects mice against toxicity of HurTNFa. Tumor Necrosis Factor Alpha (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.
Fournisseur:  Biotium
Description:   This antibody neutralises HurTNFamediated cytotoxicity of L929 cells and inhibits tumour growth in mice. It protects mice against toxicity of HurTNFa. Tumor Necrosis Factor Alpha (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.
Numéro de catalogue: (BOSSBS-4182R-A350)

Fournisseur:  Bioss
Description:   As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage. In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response. It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair. Plays also a role in base excision repair (BER) probably through interaction with UNG. Through RFWD3 may activate CHEK1 and play a role in replication checkpoint control. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-7116R-A488)

Fournisseur:  Bioss
Description:   Ro autoantigens are of clinical significance because directed against them are found in most patients with primary Sjqgren syndrome, subacute cutaneous lupus erythematosus (SLE), neonatal lupus erythematosus, ANA-negative lupus erythematosus, and systemic lupus erythematosus-like disease secondary to homozygous C2 or C4 complement deficiency (1). Ro/SSA is a ribonucleoprotein that binds to auto in 35 to 50% of patients with SLE and in up to 97% of patients with Sjqgren syndrome (2). The Ro/SSA particle consists of a single immunoreactive protein noncovalently bound with one of four small RNA molecules (2). Most anti-Ro/SSA-positive sera detect not only the main protein, but also a smaller Ro/SSA protein (2). The genes which encode the smaller and larger proteins map to human chromosomes 11p15.5 and 1q31, respectively (3?). La/SSB is an autoimmune RNA-binding protein that plays a role in the transcription of RNA polymerase III was originally defined by its reactivity with auto from patients with Sjé°ƒren syndrome and SLE (6).
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-11073R-A555)

Fournisseur:  Bioss
Description:   The cadherins are a family of Ca2+-dependent adhesion molecules that function to mediate cell-cell binding events that are critical to the maintenance of cell structure and morphogenesis. EY-cadherin, also known as CDH18 (cadherin 18), CDH14 (cadherin 14), CDH24 or CDH14L, is a 790 amino acid single-pass type I membrane protein that contains five cadherin domains. One of several members of the cadherin superfamily, EY-cadherin functions as a type II classical cadherin that is expressed specifically in the central nervous system (CNS), where it plays a role in cell-cell binding events. Specifically, EY-cadherin is thought to be involved in axon guidance and outgrowth, as well as synaptic adhesion within the CNS. EY-cadherin contains a highly conserved C-terminal domain characteristic of all cadherins, but lacks the HAV cell adhesion sequence that is specific to type I cadherins. The gene encoding EY-cadherin is located within a region on chromosome five that is commonly deleted in carcinomas, implicating EY-cadherin as a potential tumor suppressor.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-11948R-CY3)

Fournisseur:  Bioss
Description:   Three mammalian fringe family members, Manic, Radical and Lunatic Fringe, have been identified as proteins related to Drosophila Fringe, a protein involved in development. Fringe proteins act upstream of the Notch signaling pathway and are involved in boundary determination during segmentation. Each mammalian Fringe displays different patterns of expression, though all are expressed in the mouse embryo as well as in many adult tissues. Radical Fringe, also known as Beta-1,3-N-acetylglucosaminyltransferase Radical Fringe, is a 331 amino acid single-pass type II membrane protein that localizes to the membrane of the Golgi apparatus. Playing a key role in the development of the limb bud, Radical Fringe transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor. Lunatic Fringe is required for normal somite segmentation and patterning and is thought to be a target of the molecular clock. Manic Fringe, also involved in somatic development, has been shown to render mouse NIH/3T3 cells tumorigenic in SCID mice.
UOM:  1 * 100 µl

Fournisseur:  Bioss
Description:   Three mammalian fringe family members, Manic, Radical and Lunatic Fringe, have been identified as proteins related to Drosophila Fringe, a protein involved in development. Fringe proteins act upstream of the Notch signaling pathway and are involved in boundary determination during segmentation. Each mammalian Fringe displays different patterns of expression, though all are expressed in the mouse embryo as well as in many adult tissues. Radical Fringe, also known as Beta-1,3-N-acetylglucosaminyltransferase Radical Fringe, is a 331 amino acid single-pass type II membrane protein that localizes to the membrane of the Golgi apparatus. Playing a key role in the development of the limb bud, Radical Fringe transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor. Lunatic Fringe is required for normal somite segmentation and patterning and is thought to be a target of the molecular clock. Manic Fringe, also involved in somatic development, has been shown to render mouse NIH/3T3 cells tumorigenic in SCID mice.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-11698R-A488)

Fournisseur:  Bioss
Description:   Huntingtin yeast partner E is a 458 amino acid single-pass membrane protein. HYPE is thought to interact with Huntingtin, a protein which induces neurodegeneration when mutated. HYPE also contains two tetratricopeptide repeats (TPR), which may be involved in protein-protein interaction. The gene that encodes HYPE is located on chromosome 12, which encodes over 1,100 genes within 132 million bases and makes up about 4.5% of the human genome. A number of skeletal deformities are linked to chromosome 12 including hypochondrogenesis, achondrogenesis and Kniest dysplasia. Chromosome 12 is also home to a homeobox gene cluster which encodes crucial transcription factors for morphogenesis, and the natural killer complex gene cluster encoding C-type lectin proteins which mediate the NK cell response to MHC I interaction. Trisomy 12p leads to facial development defects, seizure disorders and a host of other symptoms varying in severity depending on the extent of mosaicism and is most severe in cases of complete trisomy.
UOM:  1 * 100 µl

Fournisseur:  Bioss
Description:   Three mammalian fringe family members, Manic, Radical and Lunatic Fringe, have been identified as proteins related to Drosophila Fringe, a protein involved in development. Fringe proteins act upstream of the Notch signaling pathway and are involved in boundary determination during segmentation. Each mammalian Fringe displays different patterns of expression, though all are expressed in the mouse embryo as well as in many adult tissues. Radical Fringe, also known as Beta-1,3-N-acetylglucosaminyltransferase Radical Fringe, is a 331 amino acid single-pass type II membrane protein that localizes to the membrane of the Golgi apparatus. Playing a key role in the development of the limb bud, Radical Fringe transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor. Lunatic Fringe is required for normal somite segmentation and patterning and is thought to be a target of the molecular clock. Manic Fringe, also involved in somatic development, has been shown to render mouse NIH/3T3 cells tumorigenic in SCID mice.
UOM:  1 * 100 µl

Fournisseur:  Bioss
Description:   Three mammalian fringe family members, Manic, Radical and Lunatic Fringe, have been identified as proteins related to Drosophila Fringe, a protein involved in development. Fringe proteins act upstream of the Notch Signalling pathway and are involved in boundary determination during segmentation. Each mammalian Fringe displays different patterns of expression, though all are expressed in the mouse embryo as well as in many adult tissues. Radical Fringe, also known as Beta-1,3-N-acetylglucosaminyltransferase Radical Fringe, is a 331 amino acid single-pass type II membrane protein that localizes to the membrane of the Golgi apparatus. Playing a key role in the development of the limb bud, Radical Fringe transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor. Lunatic Fringe is required for normal somite segmentation and patterning and is thought to be a target of the molecular clock. Manic Fringe, also involved in somatic development, has been shown to render mouse NIH/3T3 cells tumourigenic in SCID mice.
UOM:  1 * 100 µl

Fournisseur:  Bioss
Description:   The cadherins represent a family of Ca²⁺ dependent adhesion molecules that function to mediate cell to cell binding that is critical for the maintenance of structure and morphogenesis. Cadherins each contain a large extracellular domain at the N-terminus, which is characterised by a series of five homologous repeats, the most distal of which is thought to be responsible for binding specificity. The relatively short C-terminal intracellular domain interacts with a variety of cytoplasmic proteins, including -catenin, to regulate cadherin function. The cadherin superfamily includes cadherins, protocadherins, desmogleins and desmocollins. FAT3 (FAT tumour suppressor homolog 3, also known as CDHF15 or CDHR10, is a 4,589 amino acid single-pass type I membrane protein expressed in ES cells, primitive neuroectoderm, fetal brain, infant brain, adult neural tissues and prostate. Containing thirty-three cadherin domains, four EGF-like domains and one laminin G-like domain, FAT3 may participate in the interactions between neurites derived from specific subsets of neurons during development.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-11571R-A750)

Fournisseur:  Bioss
Description:   The leucine-rich (LRR) repeat is a 20 to 30 amino acid motif that forms a hydrophobic Alpha/Beta horseshoe fold, allowing it to accommodate several leucine residues within a tightly packed core. All LRR repeats contain a variable segment and a highly conserved segment, the latter of which accounts for 11 or 12 residues of the entire LRR motif. The LRRTM protein family plays a role in the regulation of various cellular events during nervous system development. Localizing predominantly to the nervous system, LRRTM family members are known to exhibit synaptogenic activity. LRRTM3 (leucine rich repeat transmembrane neuronal 3) is a 581 amino acid single-pass type I membrane protein belonging to the LRRTM family. LRRTM3 is involved in the development and maintenance of the vertebrate nervous system, and contains ten LRR repeats. Expressed in neuronal tissues, LRRTM3 is encoded by a gene that maps to a region of chromosome 10 that has been linked to late-onset Alzheimer disease and elevated plasma Beta-Amyloid. As a result of alternative splicing events, two LRRTM3 isoforms exist.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-11571R-A680)

Fournisseur:  Bioss
Description:   The leucine-rich (LRR) repeat is a 20 to 30 amino acid motif that forms a hydrophobic Alpha/Beta horseshoe fold, allowing it to accommodate several leucine residues within a tightly packed core. All LRR repeats contain a variable segment and a highly conserved segment, the latter of which accounts for 11 or 12 residues of the entire LRR motif. The LRRTM protein family plays a role in the regulation of various cellular events during nervous system development. Localizing predominantly to the nervous system, LRRTM family members are known to exhibit synaptogenic activity. LRRTM3 (leucine rich repeat transmembrane neuronal 3) is a 581 amino acid single-pass type I membrane protein belonging to the LRRTM family. LRRTM3 is involved in the development and maintenance of the vertebrate nervous system, and contains ten LRR repeats. Expressed in neuronal tissues, LRRTM3 is encoded by a gene that maps to a region of chromosome 10 that has been linked to late-onset Alzheimer disease and elevated plasma Beta-Amyloid. As a result of alternative splicing events, two LRRTM3 isoforms exist.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-12321R)

Fournisseur:  Bioss
Description:   Tect3 is a 607 amino acid single-pass type I membrane protein that belongs to the tectonic family and exists as four alternatively spliced isoforms. Tect3 interacts with MKS1 and may be involved in apoptosis regulation. The gene that encodes Tect3 contains approximately 31,560 bases and maps to human chromosome 10q24.1. Spanning nearly 135 million base pairs and encoding nearly 1,200 genes, chromosome 10 makes up approximately 4.5% of the human genome. Several protein-coding genes, including those that encode chemokines, cadherins, excision repair proteins, early growth response factors (Egrs) and fibroblast growth receptors (FGFRs), are located on chromosome 10. Defects in some of the genes that map to chromosome 10 are associated with Charcot-Marie Tooth disease, Jackson-Weiss syndrome, Usher syndrome, nonsyndromatic deafness, Wolman’s syndrome, Cowden syndrome, Cockayne syndrome, multiple endocrine neoplasia type 2 and porphyria. Tetrahydrobiopterin deficiency and a number of syndromes involving defective skull and facial bone fusion are also linked to chromosome 10.
UOM:  1 * 100 µl
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