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Fournisseur:  Tonbo Biosciences
Description:   The PC61.5 antibody is specific for mouse CD25, a 55 kDa surface protein also known as the Interleukin-2 Receptor alpha chain, or IL-2R alpha. CD25 may bind IL-2 by itself, although with low affinity and without induction of cell signaling. CD25 is also expressed within a high-affinity complex, along with the IL-2R beta chain (CD122) and the common gamma chain (CD132), to form a signaling receptor complex. Expression of CD25 varies during developmental stages of T and B cells, is induced on activated mature T and B cells, and is present on subsets of dendritic cells. CD25 signaling as part of the IL-2 receptor complex triggers T cell activation and proliferation, as well as modulating the differentiation and function of Th17 cells, T regulatory (Treg) cells, and dendritic cells. The PC61.5 antibody is used as a marker for T cells, B cells and dendritic cell subsets. Expression of CD25, CD4 and the transcription factor Foxp3 is regarded as a phenotypic signature for Treg cells. As such, this antibody is widely used for depletion of Treg cells in vivo, as well as to distinguish Treg cells from naive or conventional T cells which are CD25-.
Numéro de catalogue: (BOSSBS-7342R)

Fournisseur:  Bioss
Description:   The Sp transcription factor family includes Sp1, Sp2, Sp3 (SPR-2) and Sp4 (SPR-1). Sp transcription factors share similar structures but do not share simi-lar functions. All four proteins contain a highly conserved DNA-binding domain composed of three zinc fingers at the C-terminus. Sp family members bind the consensus sequence GGGGCGGGGC and other closely related sequences which are known as GC boxes. Sp1, Sp3 and Sp4 share a high affinity for GC boxes while Sp2 does not. Sp2 only weakly binds to GT boxes. Sp1, Sp2 and Sp3 are ubiquitously expressed, while Sp4 is abundantly expressed in brain with limited expression in other tissues. Sp1 and Sp3, but not Sp2 or Sp4, interact with E2, a regulatory element for the ∫4 subunit of neuronal nicotinic acetylcholine receptors. Sp3 is the only Sp member to inhibit Sp1 and Sp4 media
UOM:  1 * 100 µl

Fournisseur:  Bioss
Description:   Talin, a multifunctional constituent of cell-substratum attachment sites, is a high molecular weight protein (225-270 kDa) found in variety of tissues and cell types. It is localised at a subset of adherens junctions, specialized cell-cell and cell-matrix associations that are characterised by the presence of filamentous actin at the cytoplasmic face of the junctional complex. In cultured cells, talin is absent from cell-cell junctions and found predominantly at adhesion plaques and in fibrillar streaks underlying cell surface fibronectin. Talin interacts with at least two other proteins that are localised at adhesion plaques, vinculin and integrin. Talin and vinculin have been shown to interact with each other and both have been proposed to be involved in generating the transmembrane connection, between the extracellular matrix and the cytoskeleton, that occurs at adhesion plaques. At physiological ionic strength, talin is an elongate, flexible, monomeric protein with the ability to self-associate into dimers at higher protein concentrations.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-3619R-CY5.5)

Fournisseur:  Bioss
Description:   Talin, a multifunctional constituent of cell-substratum attachment sites, is a high molecular weight protein (225-270 kDa) found in variety of tissues and cell types. It is localized at a subset of adherens junctions, specialized cell-cell and cell-matrix associations that are characterized by the presence of filamentous actin at the cytoplasmic face of the junctional complex. In cultured cells, talin is absent from cell-cell junctions and found predominantly at adhesion plaques and in fibrillar streaks underlying cell surface fibronectin. Talin interacts with at least two other proteins that are localized at adhesion plaques, vinculin and integrin. Talin and vinculin have been shown to interact with each other and both have been proposed to be involved in generating the transmembrane connection, between the extracellular matrix and the cytoskeleton, that occurs at adhesion plaques. At physiological ionic strength, talin is an elongate, flexible, monomeric protein with the ability to self-associate into dimers at higher protein concentrations.
UOM:  1 * 100 µl
Fournisseur:  Biotium
Description:   Recognizes a protein of 70 kDa, which is identified as CD86 (HLDA V; WS Code BP BP072. HLDA V; WS Code A A109. HLDA VI; WS Code BP 95. HLDA VI; WS Code B CD86.9). CD86 is a type I transmembrane glycoprotein and a member of the immunoglobulin superfamily of cell surface receptors. It is expressed at high levels on resting peripheral monocytes and dendritic cells and at very low density on resting B and T lymphocytes. CD86 expression is rapidly upregulated by B cell specific stimuli with peak expression at 18 to 42 hours after stimulation. CD86, along with CD80/B71, is an important accessory molecule in T cell co-stimulation via its interaction with CD28 and CD152/CTLA4. Since CD86 has rapid kinetics of induction, it is believed to be the major CD28 ligand expressed early in the immune response. It is also found on malignant Hodgkin and Reed Sternberg (HRS) cells in Hodgkin's disease.
Fournisseur:  Biotium
Description:   Recognizes a protein of 70 kDa, which is identified as CD86 (HLDA V; WS Code BP BP072. HLDA V; WS Code A A109. HLDA VI; WS Code BP 95. HLDA VI; WS Code B CD86.9). CD86 is a type I transmembrane glycoprotein and a member of the immunoglobulin superfamily of cell surface receptors. It is expressed at high levels on resting peripheral monocytes and dendritic cells and at very low density on resting B and T lymphocytes. CD86 expression is rapidly upregulated by B cell specific stimuli with peak expression at 18 to 42 hours after stimulation. CD86, along with CD80/B71, is an important accessory molecule in T cell co-stimulation via its interaction with CD28 and CD152/CTLA4. Since CD86 has rapid kinetics of induction, it is believed to be the major CD28 ligand expressed early in the immune response. It is also found on malignant Hodgkin and Reed Sternberg (HRS) cells in Hodgkin's disease.
Fournisseur:  WTW
Description:   Technologie de capteur haute qualité amélioré associée aux éléments électroniques de mesure les plus modernes. Les électrodes sont dotées d'un raccord de connexion qui peut être connecté à un câble IDS ou à un module sans fil.
Fournisseur:  ANSELL HEALTH CARE
Description:   Ce gant tricoté sans couture, avec fils issus de la technologie INTERCEPT™ et revêtement en polyuréthane trempé sur la paume et le bout des doigts, fournit une protection élevée contre les coupures.
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Fournisseur:  Bioss
Description:   Netrin proteins are a family of laminin-related secreted proteins that provide guidance signals for axonal growth and cell migration during development. Netrin Signalling is dependent on the concentration of calcium outside the cell and the level of PKA activity. In axonal cells, a reduction in PKA activity converts the responsiveness of the axons to the netrin proteins as the cells are repelled, rather than attracted, by the netrin gradient. Neogenin serves as the primary guidance receptor for netrin-3. Netrin-2 and the corresponding mouse homolog netrin-3 are expressed primarily in the lower two-thirds of the spinal cord, and, like netrin-1, they can either attract or repel commissural axons at a distance. Netrin-3 proteins are associated with the axon fibers projecting from motor neurons and from neurons within sympathetic and sensory ganglia, suggesting that netrin-3 may be involved in pathfinding and fasciculation of axon projection. Neogenin serves as the primary guidance receptor for netrin-3. During peripheral nerve development, high netrin-3 expression has been detected in mesenchymal cells, sensory ganglia and muscles. In humans, the gene encoding for the netrin-3 protein is localised to chromosome 16p13.3.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-11180R-A350)

Fournisseur:  Bioss
Description:   ATP-binding cassette (ABC) transporters are an evolutionarily conserved family of widely-expressed proteins that use ATP hydrolysis to catalyze the transport of various molecules across extracellular and intracellular membranes. Eukaryotic ABC transporters are largely responsible for trafficking hydrophobic compounds either within the cell as part of a metabolic process, outside the cell for transport to other organs, or for secretion from the body. The cholesterol-responsive transporter, ABCA7, maps to human chromosome 19 and mouse chromosome 10 and has been reported as a candidate regulator of ceramide transport in epidermal lipid reorganization. High expression levels of ABCA7 have been reported in myelolymphatic tissues, reticuloendothelial cells, peripheral leukocytes, thymus, spleen and bone marrow. This expression pattern of the two alternatively-spliced isoforms also indicates an involvement in lipid homeostasis in cells of the immune system, though the complete role of ABCA7 is not yet known. Full-length type I ABCA7 has shown plasma membrane localization, while the type II splicing variant has shown expression predominantly in the endoplasmic reticulum.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-11180R-A488)

Fournisseur:  Bioss
Description:   ATP-binding cassette (ABC) transporters are an evolutionarily conserved family of widely-expressed proteins that use ATP hydrolysis to catalyze the transport of various molecules across extracellular and intracellular membranes. Eukaryotic ABC transporters are largely responsible for trafficking hydrophobic compounds either within the cell as part of a metabolic process, outside the cell for transport to other organs, or for secretion from the body. The cholesterol-responsive transporter, ABCA7, maps to human chromosome 19 and mouse chromosome 10 and has been reported as a candidate regulator of ceramide transport in epidermal lipid reorganization. High expression levels of ABCA7 have been reported in myelolymphatic tissues, reticuloendothelial cells, peripheral leukocytes, thymus, spleen and bone marrow. This expression pattern of the two alternatively-spliced isoforms also indicates an involvement in lipid homeostasis in cells of the immune system, though the complete role of ABCA7 is not yet known. Full-length type I ABCA7 has shown plasma membrane localization, while the type II splicing variant has shown expression predominantly in the endoplasmic reticulum.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-11059R-A647)

Fournisseur:  Bioss
Description:   Netrin proteins are a family of laminin-related secreted proteins that provide guidance signals for axonal growth and cell migration during development. Netrin signaling is dependent on the concentration of calcium outside the cell and the level of PKA activity. In axonal cells, a reduction in PKA activity converts the responsiveness of the axons to the netrin proteins as the cells are repelled, rather than attracted, by the netrin gradient. Neogenin serves as the primary guidance receptor for netrin-3. Netrin-2 and the corresponding mouse homolog netrin-3 are expressed primarily in the lower two-thirds of the spinal cord, and, like netrin-1, they can either attract or repel commissural axons at a distance. Netrin-3 proteins are associated with the axon fibers projecting from motor neurons and from neurons within sympathetic and sensory ganglia, suggesting that netrin-3 may be involved in pathfinding and fasciculation of axon projection. Neogenin serves as the primary guidance receptor for netrin-3. During peripheral nerve development, high netrin-3 expression has been detected in mesenchymal cells, sensory ganglia and muscles. In humans, the gene encoding for the netrin-3 protein is localized to chromosome 16p13.3.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-11059R-A555)

Fournisseur:  Bioss
Description:   Netrin proteins are a family of laminin-related secreted proteins that provide guidance signals for axonal growth and cell migration during development. Netrin signaling is dependent on the concentration of calcium outside the cell and the level of PKA activity. In axonal cells, a reduction in PKA activity converts the responsiveness of the axons to the netrin proteins as the cells are repelled, rather than attracted, by the netrin gradient. Neogenin serves as the primary guidance receptor for netrin-3. Netrin-2 and the corresponding mouse homolog netrin-3 are expressed primarily in the lower two-thirds of the spinal cord, and, like netrin-1, they can either attract or repel commissural axons at a distance. Netrin-3 proteins are associated with the axon fibers projecting from motor neurons and from neurons within sympathetic and sensory ganglia, suggesting that netrin-3 may be involved in pathfinding and fasciculation of axon projection. Neogenin serves as the primary guidance receptor for netrin-3. During peripheral nerve development, high netrin-3 expression has been detected in mesenchymal cells, sensory ganglia and muscles. In humans, the gene encoding for the netrin-3 protein is localized to chromosome 16p13.3.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-9474R-CY5.5)

Fournisseur:  Bioss
Description:   Members of the NFAT (nuclear factor of activated T cells) family of transcription factors are related to NFkB/Rel proteins and form cooperative complexes with the AP-1 proteins, Fos and Jun, on DNA to regulate cytokine expression in T cells. NFAT proteins are widely expressed and alternatively modified to generate splice variants, and they are localized to both the cytosol (NFATc) and to the nucleus (NFATn). NFAT1, NFAT2, and NFAT4 are predominantly expressed in immune cells, and NFAT2 and NFAT3 are expressed at high levels in cardiac tissues. In addition to activating cytokine gene transcription, NFAT2 is also implicated in cardiac valve development, and NFAT3 is involved in cardiac hypertrophy. NFAT5 is detected in both immune and nonimmune cells and, like other NFAT proteins, contains a highly conserved Rel-like binding domain that mediates NFAT proteins associating with specific consensus sequences on DNA. NFAT proteins are activated by increases in intracellular calcium, which leads to the calmodulin-dependent phosphatase, calcineurin, dephosphorylating NFAT proteins. This activating event induces a conformational change in the protein structure that exposes the nuclear localization signal and facilitates the translocation of NFAT proteins from the cytosol into the nucleus.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-11562R)

Fournisseur:  Bioss
Description:   Spinal muscular atrophy (SMA) is an autosomal recessive neurodegenerative disease characterized by loss of motor neurons in the spinal cord. SMA is caused by deletion or loss-of-function mutations in the SMN (survival of motor neuron) gene. Gemin2 (formerly known as SIP1 for SMN interacting protein) associates directly with SMN and is a part of the SMN complex containing Gemin3 (a DEAD-box RNA helicase), Gemin4, Gemin5 and Gemin6, as well as several spliceosomal snRNP proteins. The SMN complex plays an essential role in splicesomal snRNP assembly in the cytoplasm and is required for pre-mRNA splicing of the nucleus. It is found in both the cytoplasm and the nucleus. The nuclear form is concentrated in subnuclear bodies called gems (Gemini of the coiled bodies). The SMN-Gemin2 complex is associated with spliceosomal snRNAs U1 and U5. Gemin2 is expressed in spinal cord. It can be induced by TGF∫ treatment and expression is high in several E-cadherin negative human carcinoma cell lines. SMN is expressed in a wide variety of tissues including brain, kidney, liver and spinal cord, and moderately in skeletal and cardiac muscle. The gene encoding Gemin2 maps to human chromosome 14q13.
UOM:  1 * 100 µl
Fournisseur:  ANSELL HEALTH CARE
Description:   La doublure de nylon tricotée avec revêtement en mousse nitrile sur les paumes est idéale pour les environnements secs ou légèrement huileux nécessitant une protection mécanique légère et une grande finesse de manipulation.
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