Millipore Sigma Vibrant Logo
 

431041-83-7


252 Results Gelişmiş Arama  
Showing
Products (0)
Dokümanlar (252)
Site Content (0)

Sonuçlarınızı Daraltın Use the filters below to refine your search

Aradığınızı Bulamadınız mı?
Müşteri Hizmetleri ile
İletişime Geçin

 
MilliporeSigma Documents

Doküman ararken yardıma ihtiyacınız var mı?
  • Analiz sertifikaları, Kalite Sertifikaları veya Güvenlik Bilgi Formlarını aramak için Doküman Arayıcı’yı kullanmayı deneyin.
     
  • Kullanım Kılavuzlarına erişmek için yardıma ihtiyacınız olur ise Müşteri Hizmetleri ile iletişime geçebilirsiniz.

  • A plastic relationship between vinculin-mediated tension and adhesion complex area defines adhesion size and lifetime. 26109125

    Cell-matrix adhesions are central mediators of mechanotransduction, yet the interplay between force and adhesion regulation remains unclear. Here we use live cell imaging to map time-dependent cross-correlations between vinculin-mediated tension and adhesion complex area, revealing a plastic, context-dependent relationship. Interestingly, while an expected positive cross-correlation dominated in mid-sized adhesions, small and large adhesions display negative cross-correlation. Furthermore, although large changes in adhesion complex area follow vinculin-mediated tension alterations, small increases in area precede vinculin-mediated tension dynamics. Modelling based on this mapping of the vinculin-mediated tension-adhesion complex area relationship confirms its biological validity, and indicates that this relationship explains adhesion size and lifetime limits, keeping adhesions focal and transient. We also identify a subpopulation of steady-state adhesions whose size and vinculin-mediated tension become stabilized, and whose disassembly may be selectively microtubule-mediated. In conclusion, we define a plastic relationship between vinculin-mediated tension and adhesion complex area that controls fundamental cell-matrix adhesion properties.
    Document Type:
    Reference
    Product Catalog Number:
    MAB374
    Product Catalog Name:
    Anti-Glyceraldehyde-3-Phosphate Dehydrogenase Antibody, clone 6C5

  • Influence of weight loss on plasma ghrelin responses to high-fat and high-carbohydrate test meals in obese women. 16384853

    BACKGROUND: Diet-induced weight loss is associated with an increase in fasting ghrelin. The influence of weight loss on postprandial ghrelin response remains discussed, but the specific response to macronutrients is not known. OBJECTIVE: The objective of the study was to assess the influence of weight loss in obese women on the plasma ghrelin response to a fat- or carbohydrate-rich meal. DESIGN: Seventeen obese women (mean body mass index 37.6 +/- 5 kg/m2) were given an energy-restricted diet (800 kcal/d) for 7 wk, followed by a maintenance diet for 1 wk. Before and after the weight reduction diet, each woman was given (in random order) two isoenergetic test meals, corresponding to 40% of daily energy needs. The test meals contained either 80% fat and 20% protein or 80% carbohydrate and 20% protein. Blood samples were collected over a 10-h period. Two-way ANOVA with repeated measures was used to assess the effect of the test meal on variables. RESULTS: Weight loss (-11.2 +/- 1.4 kg) was associated with a significant decrease in baseline plasma insulin (9.7 +/- 4.1 to 7.9 +/- 2.4 mU/ml; P 0.0001) and leptin (25.9 +/- 8.3 to 17.2 +/- 7.8 ng/ml; P 0.0001) and an increase in plasma ghrelin (1.86 +/- 1.05 to 2.28 +/- 1.48 ng/ml; P 0.05). Before weight loss, there was no significant difference in postprandial ghrelin response between the test meals. After weight reduction, the ghrelin response was more pronounced after the carbohydrate test meal than after the fat test meal (P 0.02). CONCLUSION: Weight loss is associated with an improved postprandial plasma ghrelin response to a carbohydrate meal, whereas the response to a fat meal is not modified.
    Document Type:
    Reference
    Product Catalog Number:
    GHRT-89HK
    Product Catalog Name:
    Human Ghrelin (TOTAL) RIA

  • Antimyelin antibodies as a predictor of clinically definite multiple sclerosis after a first demyelinating event. 12853586

    BACKGROUND: Most patients with multiple sclerosis initially present with a clinically isolated syndrome. Despite the fact that clinically definite multiple sclerosis will develop in up to 80 percent of these patients, the course of the disease is unpredictable at its onset and requires long-term observation or repeated magnetic resonance imaging (MRI). We investigated whether the presence of serum antibodies against myelin oligodendrocyte glycoprotein (MOG) and myelin basic protein (MBP) in patients with a clinically isolated syndrome predicts the interval to conversion to clinically definite multiple sclerosis. METHODS: A total of 103 patients with a clinically isolated syndrome, positive findings on cerebral MRI, and oligoclonal bands in the cerebrospinal fluid were studied. At base line, serum samples were collected to test for anti-MOG and anti-MBP antibodies with Western blot analysis, and the lesions detected by cerebral MRI were quantified. Neurologic examinations for relapse or disease progression (defined as conversion to clinically definite multiple sclerosis) were performed at base line and subsequently every three months. RESULTS: Patients with anti-MOG and anti-MBP antibodies had relapses more often and earlier than patients without these antibodies. Only 9 of 39 antibody-seronegative patients (23 percent) had a relapse, and the mean (+/-SD) time to relapse was 45.1+/-13.7 months. In contrast, 21 of 22 patients (95 percent) with antibodies against both MOG and MBP had a relapse within a mean of 7.5+/-4.4 months, and 35 of 42 patients (83 percent) with only anti-MOG antibodies had a relapse within 14.6+/-9.6 months (P0.001 for both comparisons with antibody-seronegative patients). The adjusted hazard ratio for the development of clinically definite multiple sclerosis was 76.5 (95 percent confidence interval, 20.6 to 284.6) among the patients who were seropositive for both antibodies and 31.6 (95 percent confidence interval, 9.5 to 104.5) among the patients who were seropositive only for anti-MOG antibodies, as compared with the seronegative patients. CONCLUSIONS: Analysis of antibodies against MOG and MBP in patients with a clinically isolated syndrome is a rapid, inexpensive, and precise method for the prediction of early conversion to clinically definite multiple sclerosis. This finding may be important for the counseling and care of patients with a first demyelinating event suggestive of multiple sclerosis.
    Document Type:
    Reference
    Product Catalog Number:
    MAB381
    Product Catalog Name:
    Anti-Myelin Basic Protein Antibody, a.a. 119-131, clone 2

  • Immobilization of glutaryl-7-aminocephalosporanic acid acylase on silica gel and enhancement of its stability. 12665670

    Glutaryl-7-aminocephalosporanic acid (GL-7-ACA) acylase is an enzyme that converts GL-7-ACA to 7-aminocephalosporanic acid, a starting material for semisynthetic cephalosporin antibiotics. In this study, optimal conditions for the immobilization of GL-7-ACA acylase were determined by experimental observations and statistical methods. The optimal conditions were as follows: 1.1 M phosphate buffer (pH 8.3) as buffer solution, immobilization temperature of 20 degrees C, and immobilization time of 120 min. Unreacted aldehyde groups were quenched by reaction with a low-molecular-weight material such as L-lysine, glycine, and ethanolamine after immobilization in order to enhance the activity of immobilized GL-7-ACA acylase. The activities of immobilized GL-7-ACA acylase obtained by using the low-molecular-weight materials were higher than those obtained by immobilized GL-7-ACA acylase not treated with low-molecular-weight materials. In particular, the highest activity of immobilized GL-7-ACA acylase was obtained using 0.4% (v/v) ethanolamine. We also investigated the effect of sodium cyanoborohydride in order to increase the stability of the linkage between the enzyme and the support. The effect on operational stability was obvious: the activity of immobilized GL-7-ACA acylase treated with 4% (w/w) sodium cyanoborohydride remained almost 100% after 20 times of reuse.
    Document Type:
    Reference
    Product Catalog Number:
    03-104
    Product Catalog Name:
    RIPAb+ CUGBP1 - RIP Validated Antibody and Primer Set

  • MAL/MRTF-A controls migration of non-invasive cells by upregulation of cytoskeleton-associated proteins. 22223881

    Monomeric actin regulates gene expression through serum response factor (SRF) by inhibiting its transcriptional coactivator myocardin-related transcription factor (MAL/MRTF). Many affected genes encode cytoskeletal components. We have analysed the migratory effects of actin-MAL signalling and of new target genes in non-invasive highly adherent cells. Expression of active MAL impaired migration of both fibroblasts and epithelial cells, whereas dominant-negative constructs and partial knockdown of MAL/MRTF enhanced motility. Knockdown of three newly characterised G-actin-regulated MAL targets, integrin α5, plakophilin 2 (Pkp2) and FHL1, enhanced cell migration. All three were upregulated by external stimulation through actin-MAL-SRF signalling, and MAL and SRF were inducibly recruited to cis-regulatory elements of the integrin α5 and Pkp2 genes. Finally, the reduced migration of epithelial cells stably expressing MAL was partially reversed by knockdown of Pkp2 and FHL1. We conclude that the actin-MAL pathway promotes adhesive gene expression, including integrin α5, Pkp2 and FHL1, and that this is anti-motile for non-invasive cells harbouring high basal activity.
    Document Type:
    Reference
    Product Catalog Number:
    AB1928
    Product Catalog Name:
    Anti-Integrin α5 Antibody, CT, Intracellular