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  • Prion protein oligomers in Creutzfeldt-Jakob disease detected by gel-filtration centrifuge columns. 19389076

    Prion diseases are diagnosed by the detection of accumulation of abnormal prion protein (PrP) using immunohistochemistry or the detection of protease-resistant abnormal PrP (PrP(res)). Although the abnormal PrP is neurotoxic by forming aggregates, recent studies suggest that the most infectious units are smaller than the amyloid fibrils. In the present study, we developed a simplified method by applying size-exclusion gel-filtration chromatography to examine PrP oligomers without proteinase K digestion in Creutzfeldt-Jakob disease (CJD) samples, and evaluated the correlation between disease severity and the polymerization degree of PrP. Brain homogenates of human CJD and non-CJD cases were applied to the gel-filtration spin columns, and fractionated PrP molecules in each fraction were detected by western blot. We observed that PrP oligomers could be detected by the simple gel-filtration method and distinctly separated from monomeric cellular PrP (PrP(c)). PrP oligomers were increased according to the disease severity, accompanied by the depletion of PrP(c). The separated PrP oligomers were already protease-resistant in the case with short disease duration. In the cases with quite severe pathology the oligomeric PrP reached a plateau, which may indicate that PrP molecules could mostly develop into amyloid fibrils in the advanced stages. The increase of PrP oligomers correlated with the degree of histopathological changes such as spongiosis and gliosis. The decrease of monomeric PrP(c) was unexpectedly obvious in the diseased cases. Dynamic changes of both oligomerization of the human PrP and depletion of normal PrP(c) require further elucidation to develop a greater understanding of the pathogenesis of human prion diseases.
    Dokumententyp:
    Referenz
    Produkbestellnummer:
    AP192P
    Produktbezeichnung:
    Donkey Anti-Mouse IgG Antibody, HRP conjugate, Species Adsorbed

  • Prion protein detection using nanomechanical resonator arrays and secondary mass labeling. 18271602

    Nanomechanical resonators have shown potential application for mass sensing and have been used to detect a variety of biomolecules. In this study, a dynamic resonance-based technique was used to detect prion proteins (PrP), which in conformationally altered forms are known to cause neurodegenerative diseases in animals as well as humans. Antibodies and nanoparticles were used as mass labels to increase the mass shift and thus amplify the frequency shift signal used in PrP detection. A sandwich assay was used to immobilize PrP between two monoclonal antibodies, one of which was conjugated to the resonator's surface while the other was either used alone or linked to the nanoparticles as a mass label. Without additional mass labeling, PrP was not detected at concentrations below 20 microg/mL. In the presence of secondary antibodies the analytical sensitivity was improved to 2 microg/mL. With the use of functionalized nanoparticles, the sensitivity improved an additional 3 orders of magnitude to 2 ng/mL.
    Dokumententyp:
    Referenz
    Produkbestellnummer:
    17-191
    Produktbezeichnung:
    MAP Kinase/Erk Assay Kit, non-radioactive

  • CCAAT-enhancer-binding protein β (C/EBPβ) and downstream human placental growth hormone genes are targets for dysregulation in pregnancies complicated by maternal obesity ... 23782703

    Human chorionic somatomammotropin (CS) and placental growth hormone variant (GH-V) act as metabolic adaptors in response to maternal insulin resistance, which occurs in "normal" pregnancy. Maternal obesity can exacerbate this "resistance," suggesting that CS, GH-V, or transcription factors that regulate their production might be targets. The human CS genes, hCS-A and hCS-B, flank the GH-V gene. A significant decrease in pre-term placental CS/GH-V RNA levels was observed in transgenic mice containing the CS/GH-V genes in a model of high fat diet (HFD)-induced maternal obesity. Similarly, a decrease in CS/GH-V RNA levels was detected in term placentas from obese (body mass index (BMI) ≥ 35 kg/m(2)) versus lean (BMI 20-25 kg/m(2)) women. A specific decrease in transcription factor CCAAT-enhancer-binding protein β (C/EBPβ) RNA levels was also seen with obesity; C/EBPβ is required for mouse placenta development and is expressed, like CS and GH-V, in syncytiotrophoblasts. Binding of C/EBPβ to the CS gene downstream enhancer regions, which by virtue of their position distally flank the GH-V gene, was reduced in placenta chromatin from mice on a HFD and in obese women; a corresponding decrease in RNA polymerase II associated with CS/GH-V promoters was also observed. Detection of decreased endogenous CS/GH-V RNA levels in human placental tumor cells treated with C/EBPβ siRNA is consistent with a direct effect. These data provide evidence for CS/GH-V dysregulation in acute HFD-induced obesity in mouse pregnancy and chronic obesity in human pregnancy and implicate C/EBPβ, a factor associated with CS regulation and placental development.
    Dokumententyp:
    Referenz
    Produkbestellnummer:
    04-1153

  • The immunoregulatory protein human B7H3 is a tumor-associated antigen that regulates tumor cell migration and invasion. 18690846

    The monoclonal antibody (mAb) 376.96 has been used for detection of micrometastatic tumor cells due to its high binding specificity for a wide range of tumor cells, but the identity and function of its target antigen have not been known. Here, using immunoprecipitation and siRNA technology, we demonstrate that the antigen is the human 4Ig-B7H3 (4Ig-hB7H3) protein, previously known as an immunoregulatory protein in immune cells. Immunoblots of whole cell lysates, subcellular fractionation and tunicamycin treatment of human tumor cells indicated that 4Ig-hB7H3 is a approximately 100-kDa N-linked glycosylated membrane protein. The tumor promoter phorbol 12-myristate 13-acetate (PMA) enhanced the expression of 4Ig-hB7H3 in FEMX-I (melanoma), MA11 (breast cancer), and OHS (osteosarcoma) cells, suggesting that 4Ig-hB7H3 may be implicated in tumorigenesis. Most importantly, siRNA-downregulation of hB7H3 reduced cell adhesion to fibronectin of melanoma and breast cancer cells by up to 50 %, and migration and matrigel-invasion by more than 70 %, but surprisingly had no apparent impact on cell proliferation. In conclusion, our data present 4Ig-hB7H3 as a tumor-associated antigen and suggests a novel biological role of 4Ig-hB7H3 in tumor progression and metastasis.
    Dokumententyp:
    Referenz
    Produkbestellnummer:
    Mehrere
    Produktbezeichnung:
    Mehrere

  • An improved method of protein localization in artworks through SERS nanotag-complexed antibodies. 21079929

    There are several analytical techniques currently in use in conservation science to identify proteins in artworks. However, as is often the case, the determination of the exact location of a protein in a complex layer structure is challenging due to difficulty in separating layers. Localization of the protein in a cross-section has been demonstrated through attenuated total reflectance-Fourier transform infrared mapping and imaging as well as chemiluminescent and fluorescent-labeled antibodies; however, these techniques either require expensive instrumental setups or produce results that can be challenging to interpret. This paper will present research using surface-enhanced Raman scattering (SERS) nanotags complexed to secondary antibodies in conjunction with primary antibodies for the localization of ovalbumin, collagen, and casein in cross-sections from replicas and artworks containing avian egg, animal glue, or casein binders. The advantages of this technique over the others are (1) the detection method is a Raman microscope, equipment found in several museum laboratories; (2) the distinctive SERS signal from the nanotag increases the detection limit of the protein and decreases the interference from other colorants present in the cross-section layers; and finally, (3) the large (120 nm) SERS-labeled antibodies do not appear to penetrate into the cross-section, eliminating the risk of spurious signal and misidentification. Any agglomerations due to surface texture are clearly visible under normal illumination and can be avoided easily during analysis or removed with a light polish. This technique not only allows protein localization in multilayered samples while preserving the stratigraphic information but also retains the protein specificity of the antibody approach.
    Dokumententyp:
    Referenz
    Produkbestellnummer:
    AP132F
    Produktbezeichnung:
    Goat Anti-Rabbit IgG Antibody, FITC conjugate

  • Immuno-spin trapping of protein and DNA radicals: tagging free radicals to locate and understand the redox process. 19159679

    Biomolecule-centered radicals are intermediate species produced during both reversible (redox modulation) and irreversible (oxidative stress) oxidative modification of biomolecules. These oxidative processes must be studied in situ and in real time to understand the molecular mechanism of cell adaptation or death in response to changes in the extracellular environment. In this regard, we have developed and validated immuno-spin trapping to tag the redox process, tracing the oxidatively generated modification of biomolecules, in situ and in real time, by detecting protein- and DNA-centered radicals. The purpose of this methods article is to introduce and update the basic methods and applications of immuno-spin trapping for the study of redox biochemistry in oxidative stress and redox regulation. We describe in detail the production, detection, and location of protein and DNA radicals in biochemical systems, cells, and tissues, and in the whole animal as well, by using immuno-spin trapping with the nitrone spin trap 5,5-dimethyl-1-pyrroline N-oxide.
    Dokumententyp:
    Referenz
    Produkbestellnummer:
    12-348
    Produktbezeichnung:
    Goat Anti-Rabbit IgG Antibody, HRP-conjugate

  • Expression of small heat shock-related protein 20 (HSP20) in rat myometrium is markedly decreased during late pregnancy and labour. 17504924

    The underlying mechanisms regulating uterine contractions during labour are still poorly understood. Heat shock protein 20 (HSP20) is known to be present at high levels in smooth muscle and implicated in muscle relaxation, but HSP20 expression in the myometrium is completely undetermined. Since HSP20 has been implicated in smooth muscle relaxation, we hypothesized that HSP20 would be highly expressed in the rat myometrium during early and mid-pregnancy when the myometrium is relatively quiescent. Northern blot analysis particularly demonstrated that HSP20 mRNA detection was significantly decreased from day (d) 22 of pregnancy to 1-day post-partum (PP) compared with d6 (P less than 0.05). HSP20 mRNA detection was also significantly decreased from d22 to d23 of gestation compared with non-pregnant (NP) samples. Immunoblot analysis showed that detection of HSP20 was significantly decreased at d23 compared with d12 and d15 (P less than 0.05). HSP20 detection also significantly decreased at PP compared with d15 (P less than 0.05). Immunofluorescence analysis demonstrated that after d15, plasma membrane-associated localization of HSP20 decreased markedly in both circular and longitudinal muscle layers. In addition, HSP20 was detectable near cell membranes at much higher levels in the longitudinal muscle layer of progesterone-treated pregnant rats (delayed labour) at all gestational time points examined, compared with controls. Our results demonstrate that HSP20 mRNA and protein are highly expressed during early and mid-pregnancy and then the expression markedly decreases during late pregnancy and labour. The observed patterns of HSP20 expression are consistent with a potential role for HSP20 in facilitating myometrium quiescence during early and mid-pregnancy.
    Dokumententyp:
    Referenz
    Produkbestellnummer:
    07-490