Millipore Sigma Vibrant Logo
 

laboratorio"


259 Results Búsqueda avanzada  
Mostrar
Productos (9)
Documentos (7)
Páginas (243)

Acote sus resultados Utilice los filtros siguientes para refinar su búsqueda

Tipo de documento

  • (6)
  • (1)
¿No encuentra lo que está buscando?
Póngase en contacto con
el Servicio de Atención
al Cliente

 
¿Necesita ayuda para encontrar un documento?
  • «
  • <
  • 1
  • >
  • »

  • Monocarboxylate transporter 1 is up-regulated in basal-like breast carcinoma. 20636790

    Monocarboxylate transporters (MCTs) have been considered promising targets for cancer therapy, since they facilitate lactate efflux in glycolytic tumours. However, their role in solid tumours is still poorly understood. Thus, the present work aimed to contribute to understanding the involvement of MCT1 and MCT4 in breast cancer progression as well as MCT regulation by CD147.
    Tipo de documento:
    Referencia
    Referencia del producto:
    AB3316P
    Nombre del producto:
    Anti-Monocarboxylate Transporter 4 Antibody

  • E-cadherin impairment increases cell survival through Notch-dependent upregulation of Bcl-2. 21989054

    The role of E-cadherin in tumorigenesis has been attributed to its ability to suppress invasion and metastization. However, E-cadherin impairment may have a wider impact on tumour development. We have previously shown that overexpression of mutant human E-cadherin in Drosophila produces a phenotype characteristic of downregulated Notch. Hence, we hypothesized that Notch signalling may be influenced by E-cadherin and may mediate tumour development associated with E-cadherin deficiency. De novo expression of wild-type E-cadherin in two cellular models led to a significant decrease in the activity of the Notch pathway. In contrast, the ability to inhibit Notch-1 signalling was lost in cells transfected with mutant forms of E-cadherin. Increased Notch-1 activity in E-cadherin-deficient cells correlated with increased expression of Bcl-2, and increased resistance to apoptotic stimuli. After Notch-1 inhibition, E-cadherin-deficient cells were re-sensitized to apoptosis in a similar degree to wild-type E-cadherin cells. We also show that Notch-inhibiting drugs are able to significantly inhibit the growth of E-cadherin-deficient cells xenografted into nude mice. This effect was comparable with the one observed in animals treated with the chemotherapeutic agent taxol, a chemical inducer of cell death. In conclusion, our results show that aberrant Notch-1 activation, Bcl-2 overexpression and increased cell survival are likely to play a crucial role in neoplastic transformation associated with E-cadherin impairment. These findings highlight the possibility of new targeted therapeutical strategies for the treatment of tumours associated with E-cadherin inactivation.
    Tipo de documento:
    Referencia
    Referencia del producto:
    Múltiplo
    Nombre del producto:
    Múltiplo

  • The Suv39h-HP1 histone methylation pathway is dispensable for enrichment and protection of cohesin at centromeres in mammalian cells. 18075750

    Sister chromatids are physically connected by cohesin complexes. This sister chromatid cohesion is essential for the biorientation of chromosomes on the mitotic and meiotic spindle. In many species, cohesion between chromosome arms is partly dissolved in prophase of mitosis, whereas cohesion is protected at centromeres until the onset of anaphase. In vertebrates, the protein Sgo1, protein phosphatase 2A, and several other proteins are required for protection of centromeric cohesin in early mitosis. In fission yeast, the recruitment of heterochromatin protein Swi6/HP1 to centromeres by the histone-methyltransferase Clr4/Suv39h is required for enrichment of cohesin at centromeres already in interphase. We have tested if the Suv39h-HP1 histone methylation pathway is also required for enrichment and mitotic protection of cohesin at centromeres in mammalian cells. We show that cohesin and HP1 proteins partially colocalize at mitotic centromeres but that cohesin localization is not detectably altered in mouse embryonic fibroblasts that lack Suv39h genes and in which HP1 proteins can, therefore, not be properly enriched in pericentric heterochromatin. Our data indicate that the Suv39h-HP1 pathway is not essential for enrichment and mitotic protection of cohesin at centromeres in mammalian cells.
    Tipo de documento:
    Referencia
    Referencia del producto:
    05-499
    Nombre del producto:
    Anti-Histone H3 Antibody, clone 6.6.2

  • Localization of muscarinic receptors M1R, M2R and M3R in the human colon. 20146726

    Muscarinic acetylcholine receptors (MR) are involved in multiple intestinal reflexes. The cellular localization of subtypes of MRs within enteric circuits mediating muscle and mucosal reflexes remains to be demonstrated. This study aimed to localize the three functionally significant subtypes of MRs in human colon.
    Tipo de documento:
    Referencia
    Referencia del producto:
    AB1529
    Nombre del producto:
    Anti-Nitric Oxide Synthase I Antibody

  • Functional protein microarrays: just how functional are they? 16006113

    Arrays of immobilized proteins have been developed for the discovery and characterization of protein functions ranging from molecular recognition to enzymatic activity. The success of these applications is highly dependent upon the maintenance of protein structure and function while in an immobilized state - a largely untested hypothesis. However, the immobilization of functional proteins is not without precedent. Active enzymes have been successfully immobilized for industrial applications for several decades. Furthermore, a survey of recent protein microarray literature reveals that an even wider range of proteins can maintain 'proper' function while immobilized. These reports help to validate the functionality of so-called functional protein microarrays.
    Tipo de documento:
    Referencia
    Referencia del producto:
    05-311
    Nombre del producto:
    Anti-GST Tag Antibody, clone DG122-2A7

  • Persistent Nav1.6 current at axon initial segments tunes spike timing of cerebellar granule cells. 20173079

    Cerebellar granule (CG) cells generate high-frequency action potentials that have been proposed to depend on the unique properties of their voltage-gated ion channels. To address the in vivo function of Nav1.6 channels in developing and mature CG cells, we combined the study of the developmental expression of Nav subunits with recording of acute cerebellar slices from young and adult granule-specific Scn8a KO mice. Nav1.2 accumulated rapidly at early-formed axon initial segments (AISs). In contrast, Nav1.6 was absent at early postnatal stages but accumulated at AISs of CG cells from P21 to P40. By P40-P65, both Nav1.6 and Nav1.2 co-localized at CG cell AISs. By comparing Na(+) currents in mature CG cells (P66-P74) from wild-type and CG-specific Scn8a KO mice, we found that transient and resurgent Na(+) currents were not modified in the absence of Nav1.6 whereas persistent Na(+) current was strongly reduced. Action potentials in conditional Scn8a KO CG cells showed no alteration in threshold and overshoot, but had a faster repolarization phase and larger post-spike hyperpolarization. In addition, although Scn8a KO CG cells kept their ability to fire action potentials at very high frequency, they displayed increased interspike-interval variability and firing irregularity in response to sustained depolarization. We conclude that Nav1.6 channels at axon initial segments contribute to persistent Na(+) current and ensure a high degree of temporal precision in repetitive firing of CG cells.
    Tipo de documento:
    Referencia
    Referencia del producto:
    AB5204
    Nombre del producto:
    Anti-Sodium Channel Antibody, Voltage Gated, Brain Type I
  • «
  • <
  • 1
  • >
  • »