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#28637492   2017/06/22 Save this To Up

Expression patterns of FSHD-causing DUX4 and myogenic transcription factors PAX3 and PAX7 are spatially distinct in differentiating human stem cell cultures.

Facioscapulohumeral muscular dystrophy (FSHD) is most commonly inherited in an autosomal dominant pattern and caused by the abnormal expression of DUX4 in skeletal muscle. The DUX4 transcription factor has DNA binding domains similar to several paired class homeotic transcription factors, but only myogenic factors PAX3 and PAX7 rescue cell viability when co-expressed with DUX4 in mouse myoblasts. This observation suggests competition for DNA binding sites in satellite cells might limit muscle repair and may be one aspect of DUX4-associated myotoxicity. The competition hypothesis requires that DUX4 and PAX3/7 be expressed in the same cells at some point during development or in adult tissues. We modeled myogenesis using human isogenic iPS and ES cells and examined expression patterns of DUX4, PAX3, and PAX7 to determine if conditions that promote PAX3 and PAX7 expression in cell culture also promote DUX4 expression in the same cells.

2769 related Products with: Expression patterns of FSHD-causing DUX4 and myogenic transcription factors PAX3 and PAX7 are spatially distinct in differentiating human stem cell cultures.

Macrophage Colony Stimula Macrophage Colony Stimula CELLKINES Natural Human I Human Stem Cell Factor SC Goat Anti-Human, Mouse AR Rabbit Anti-Human Androge Rabbit Anti-Human Androge Rabbit Anti-Cell death in Rabbit Anti-Cell death in Human Small Intestine Mic Human Large Intestine Mic Human Internal Mammary Ar

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#27685156   2016/09/30 Save this To Up

Generation of Two-color Antigen Microarrays for the Simultaneous Detection of IgG and IgM Autoantibodies.

Autoantibodies, which are antibodies against self-antigens, are present in many disease states and can serve as markers for disease activity. The levels of autoantibodies to specific antigens are typically detected with the enzyme-linked immunosorbent assay (ELISA) technique. However, screening for multiple autoantibodies with ELISA can be time-consuming and requires a large quantity of patient sample. The antigen microarray technique is an alternative method that can be used to screen for autoantibodies in a multiplex fashion. In this technique, antigens are arrayed onto specially coated microscope slides with a robotic microarrayer. The slides are probed with patient serum samples and subsequently fluorescent-labeled secondary antibodies are added to detect binding of serum autoantibodies to the antigens. The autoantibody reactivities are revealed and quantified by scanning the slides with a scanner that can detect fluorescent signals. Here we describe methods to generate custom antigen microarrays. Our current arrays are printed with 9 solid pins and can include up to 162 antigens spotted in duplicate. The arrays can be easily customized by changing the antigens in the source plate that is used by the microarrayer. We have developed a two-color secondary antibody detection scheme that can distinguish IgG and IgM reactivities on the same slide surface. The detection system has been optimized to study binding of human and murine autoantibodies.

1979 related Products with: Generation of Two-color Antigen Microarrays for the Simultaneous Detection of IgG and IgM Autoantibodies.

Mouse Anti-Ca19.9 Sialyl MOUSE ANTI BOVINE ROTAVIR anti HBsAg surface antige anti HBcAg core IgG2a (mo anti HBcAg core IgG2b (mo anti HBcAg core IgG2b (mo anti HBcAg core IgG2a (mo anti HBcAg core IgG2b (mo anti HBcAg core IgG2a (mo anti CD54 IgG2b k monoclo anti CD66e IgG1 monoclona Adenovirus antibody, Mono

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#26921630   2016/05/06 Save this To Up

Development of a custom pentaplex sandwich immunoassay using Protein-G coupled beads for the Luminex® xMAP® platform.

Multiplex bead-based assays have many advantages over ELISA, particularly for the analyses of large quantities of samples and/or precious samples of limited volume. Although many commercial arrays covering multitudes of biologically significant analytes are available, occasionally the development of custom arrays is necessary. Here, the development of a custom pentaplex sandwich immunoassay using Protein G-coupled beads, for analysis using the Luminex® xMAP® platform, is described. This array was required for the measurement of candidate biomarkers of vaccine safety in small volumes of mouse sera. Optimisation of this assay required a stepwise approach: testing cross-reactivity of the antibody pairs, the development of an in-house serum diluent buffer as well as heat-inactivation of serum samples to prevent interference from matrix effects. We then demonstrate the use of this array to analyse inflammatory mediators in mouse serum after immunisation. The work described here exemplifies how Protein G-coupled beads offer a flexible and robust approach to develop custom multiplex immunoassays, which can be applied to a range of analytes from multiple species.

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G protein-coupled recepto Protein Purification Bea Protein Purification Bea Protein Purification Bea Protein Purification Bea Protein Purification Bea Protein Purification Bea Custom Immunoassay Develo G Protein Coupled Recepto G Protein Coupled Recepto G Protein Coupled Recepto G Protein Coupled Recepto

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#26172315   2015/08/05 Save this To Up

Antibody Arrays for Quality Control of Mesenchymal Stem Cells.

Quality control of mesenchymal stem cells is an important step before their clinical use in regenerative therapy. Among various characteristics of mesenchymal stem cells, reproducibility of population compositions should be analyzed according to characteristics, such as stem cell contents and differentiation stages. Such characterization may be possible by assessing the expression of several surface markers. Here we report our attempts to utilize antibody arrays for analyzing surface markers expressed in mesenchymal stem cell populations in a high-throughput manner. Antibody arrays were fabricated using a glass plate on which a micropatterned alkanethiol monolayer was formed. Various antibodies against surface markers including CD11b, CD31, CD44, CD45, CD51, CD73, CD90, CD105, and CD254 were covalently immobilized on the micropatterned surface in an array format to obtain an antibody array. To examine the feasibility of the array, cell binding assays were performed on the array using a mouse mesenchymal stem cell line. Our results showed that cell binding was observed on the arrayed spots with immobilized antibodies which exhibited reactivity to the cells in flow cytometry. It was further found that the density of cells attached to antibody spots was correlated to the mean fluorescent channel recorded in flow cytometry. These results demonstrate that data obtained by cell binding assays on the antibody array are comparable to those by the conventional flow cytometry, while throughput of the analysis is much higher with the antibody array-based method than flow cytometry. Accordingly, we concluded that the antibody array provides a high-throughput analytical method useful for the quality control of mesenchymal stem cells.

1521 related Products with: Antibody Arrays for Quality Control of Mesenchymal Stem Cells.

Rat Mesenchymal Stem Cell EZH2 KMT6 Control Peptid GFP control peptide anti Anti C Reactive Protein A MOUSE ANTI BOVINE ROTAVIR Macrophage Colony Stimula Macrophage Colony Stimula MOUSE ANTI BORRELIA BURGD glial cells missing homol succinate-CoA ligase, GDP formin-like 1 antibody So succinate-CoA ligase, ADP

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#25182840   2014/09/08 Save this To Up

Mesenchymal stem cells exert anti-proliferative effect on lipopolysaccharide-stimulated BV2 microglia by reducing tumour necrosis factor-α levels.

Progression of neurodegenerative diseases occurs when microglia, upon persistent activation, perpetuate a cycle of damage in the central nervous system. Use of mesenchymal stem cells (MSC) has been suggested as an approach to manage microglia activation based on their immunomodulatory functions. In the present study, we describe the mechanism through which bone marrow-derived MSC modulate the proliferative responses of lipopolysaccharide-stimulated BV2 microglia.

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Macrophage Colony Stimula Macrophage Colony Stimula Rat Mesenchymal Stem Cell ELISA Kit for Tumor Necr Anti C Reactive Protein A anti HSV (II) gB IgG1 (mo anti HCMV IE pp65 IgG1 (m anti HCMV gB IgG1 (monocl Epidermal Growth Factor ( Epidermal Growth Factor ( Human Stem Cell Factor SC Human Tumor Necrosis Fact

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#24675532   2014/05/05 Save this To Up

Biomarker-guided sequential targeted therapies to overcome therapy resistance in rapidly evolving highly aggressive mammary tumors.

Combinatorial targeted therapies are more effective in treating cancer by blocking by-pass mechanisms or inducing synthetic lethality. However, their clinical application is hampered by resistance and toxicity. To meet this important challenge, we developed and tested a novel concept of biomarker-guided sequential applications of various targeted therapies using ErbB2-overexpressing/PTEN-low, highly aggressive breast cancer as our model. Strikingly, sustained activation of ErbB2 and downstream pathways drives trastuzumab resistance in both PTEN-low/trastuzumab-resistant breast cancers from patients and mammary tumors with intratumoral heterogeneity from genetically-engineered mice. Although lapatinib initially inhibited trastuzumab-resistant mouse tumors, tumors by-passed the inhibition by activating the PI3K/mTOR signaling network as shown by the quantitative protein arrays. Interestingly, activation of the mTOR pathway was also observed in neoadjuvant lapatinib-treated patients manifesting lapatinib resistance. Trastuzumab + lapatinib resistance was effectively overcome by sequential application of a PI3K/mTOR dual kinase inhibitor (BEZ235) with no significant toxicity. However, our p-RTK array analysis demonstrated that BEZ235 treatment led to increased ErbB2 expression and phosphorylation in genetically-engineered mouse tumors and in 3-D, but not 2-D, culture, leading to BEZ235 resistance. Mechanistically, we identified ErbB2 protein stabilization and activation as a novel mechanism of BEZ235 resistance, which was reversed by subsequent treatment with lapatinib + BEZ235 combination. Remarkably, this sequential application of targeted therapies guided by biomarker changes in the tumors rapidly evolving resistance doubled the life-span of mice bearing exceedingly aggressive tumors. This fundamentally novel approach of using targeted therapies in a sequential order can effectively target and reprogram the signaling networks in cancers evolving resistance during treatment.

2131 related Products with: Biomarker-guided sequential targeted therapies to overcome therapy resistance in rapidly evolving highly aggressive mammary tumors.

Recombinant Human Interfe Native Influenza HA (A To Native Influenza HA (A To Native Influenza HA (A To Cell Meter™ Fluorimetri Cell Meter™ Fluorimetri T-2 Toxin Mycotoxins ELIS Apoptosis antibody array Cell cycle antibody array Cytokine antibody array i Signal transduction antib AKT Phospho-Specific Arra

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#24368301   2014/01/29 Save this To Up

A platform to screen for C-type lectin receptor-binding carbohydrates and their potential for cell-specific targeting and immune modulation.

Myeloid C-type lectin receptors (CLRs) in innate immunity represent a superfamily of pattern recognition receptors that recognize carbohydrate structures on pathogens and self-antigens. The primary interaction of an antigen-presenting cell and a pathogen shapes the following immune response. Therefore, the identification of CLR ligands that can either enhance or modulate the immune response is of interest. We have developed a screening platform based on glycan arrays to identify immune modulatory carbohydrate ligands of CLRs. A comprehensive library of CLRs was expressed by fusing the extracellular part of each respective CLR, the part containing the carbohydrate-recognition domain (CRD), to the Fc fragment of human IgG1 molecules. CLR-Fc fusion proteins display the CRD in a dimeric form, are properly glycosylated, and can be detected by a secondary antibody with a conjugated fluorophore. Thus, they are valuable tools for high-throughput screening. We were able to identify novel carbohydrate binders of CLRs using the glycan array technology. These CLR-binding carbohydrates were then covalently attached to the model antigen ovalbumin. The ovalbumin neoglycoconjugates were used in a dendritic cell/T cell co-culture assay to stimulate transgenic T cells in vitro. In addition, mice were immunized with these conjugates to analyze the immune modulatory properties of the CLR ligands in vivo. The CLR ligands induced an increased Th1 cytokine production in vitro and modulated the humoral response in vivo. The platform described here allows for the identification of CLR ligands, as well as the evaluation of each ligand's cell-specific targeting and immune modulatory properties.

1014 related Products with: A platform to screen for C-type lectin receptor-binding carbohydrates and their potential for cell-specific targeting and immune modulation.

MOUSE ANTI BOVINE ROTAVIR MOUSE ANTI BORRELIA BURGD NATIVE HUMAN PROLACTIN, P RABBIT ANTI GSK3 BETA (pS 10x ELISA WASH BUFFER, Pr 10X PHOSPHATE BUFFERED SA PERMANENT AQUEOUS MOUNTIN MOUSE ANTI CANINE DISTEMP MOUSE ANTI HUMAN CD15, Pr NATIVE HUMAN PROLACTIN, P MOUSE ANTI HUMAN CD19 RPE MOUSE ANTI HUMAN CD15, Pr

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#24316450   2014/01/14 Save this To Up

Micropallet arrays for the capture, isolation and culture of circulating tumor cells from whole blood of mice engrafted with primary human pancreatic adenocarcinoma.

Circulating tumor cells (CTCs) are important biomarkers of cancer progression and metastatic potential. The rarity of CTCs in peripheral blood has driven the development of technologies to isolate these tumor cells with high specificity; however, there are limited techniques available for isolating target CTCs following enumeration. A strategy is described to capture and isolate viable tumor cells from whole blood using an array of releasable microstructures termed micropallets. Specific capture of nucleated cells or cells expressing epithelial cell adhesion molecules (EpCAM) was achieved by functionalizing micropallet surfaces with either fibronectin, Matrigel or anti-EpCAM antibody. Surface grafting of poly(acrylic acid) followed by covalent binding of protein A/G enabled efficient capture of EpCAM antibody on the micropallet surface. MCF-7 cells, a human breast adenocarcinoma, were retained on the array surface with 90±8% efficiency when using an anti-EpCAM-coated array. To demonstrate the efficiency of tumor cell retention on micropallet arrays in the presence of blood, MCF-7 cells were mixed into whole blood and added to small arrays (71 mm(2)) coated with fibronectin, Matrigel or anti-EpCAM. These approaches achieved MCF-7 cell capture from ≤10 µL of whole blood with efficiencies greater than 85%. Furthermore, MCF-7 cells intermixed with 1 mL blood and loaded onto large arrays (7171 mm(2)) were captured with high efficiencies (≥97%), could be isolated from the array by a laser-based approach and were demonstrated to yield a high rate of colony formation (≥85%) after removal from the array. Clinical utility of this technology was shown through the capture, isolation and successful culture of CTCs from the blood of mice engrafted with primary human pancreatic tumors. Direct capture and isolation of living tumor cells from blood followed by analysis or culture will be a valuable tool for cancer cell characterization.

2766 related Products with: Micropallet arrays for the capture, isolation and culture of circulating tumor cells from whole blood of mice engrafted with primary human pancreatic adenocarcinoma.

AccuPrep Genomic DNA Extr Anti C Reactive Protein A NycoPrep™ 1.077, for is Human Pancreatic Microvas Human Cord Blood CD34+ Ce Human Red Blood Cells Uni AccuzolTM Total RNA Extra Leptin ELISA Kit, Human A Astra Blue 6GLL, Stain fo Rabbit Anti-Human Red Blo Uroguanylin (circulating Bone Morphogenetic Protei

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#23909808   2014/02/04 Save this To Up

Emergent properties of nanosensor arrays: applications for monitoring IgG affinity distributions, weakly affined hypermannosylation, and colony selection for biomanufacturing.

It is widely recognized that an array of addressable sensors can be multiplexed for the label-free detection of a library of analytes. However, such arrays have useful properties that emerge from the ensemble, even when monofunctionalized. As examples, we show that an array of nanosensors can estimate the mean and variance of the observed dissociation constant (KD), using three different examples of binding IgG with Protein A as the recognition site, including polyclonal human IgG (KD μ = 19 μM, σ(2) = 1000 mM(2)), murine IgG (KD μ = 4.3 nM, σ(2) = 3 μM(2)), and human IgG from CHO cells (KD μ = 2.5 nM, σ(2) = 0.01 μM(2)). Second, we show that an array of nanosensors can uniquely monitor weakly affined analyte interactions via the increased number of observed interactions. One application involves monitoring the metabolically induced hypermannosylation of human IgG from CHO using PSA-lectin conjugated sensor arrays where temporal glycosylation patterns are measured and compared. Finally, the array of sensors can also spatially map the local production of an analyte from cellular biosynthesis. As an example, we rank productivity of IgG-producing HEK colonies cultured directly on the array of nanosensors itself.

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MOUSE ANTI BOVINE ROTAVIR RABBIT ANTI GSK3 BETA (pS MOUSE ANTI CANINE DISTEMP MOUSE ANTI HUMAN CD19 RPE MOUSE ANTI APAAP COMPLEX, NATIVE HUMAN PROLACTIN, P 10x ELISA WASH BUFFER, Pr 10X PHOSPHATE BUFFERED SA PERMANENT AQUEOUS MOUNTIN MarkerGene™ LysoLive™ MOUSE ANTI HUMAN CD15, Pr NATIVE HUMAN PROLACTIN, P

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#23868936   2013/08/15 Save this To Up

Induction of ATF3 gene network by triglyceride-rich lipoprotein lipolysis products increases vascular apoptosis and inflammation.

Elevation of triglyceride-rich lipoproteins (TGRLs) contributes to the risk of atherosclerotic cardiovascular disease. Our work has shown that TGRL lipolysis products in high physiological to pathophysiological concentrations cause endothelial cell injury; however, the mechanisms remain to be delineated.

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F box and leucine rich re pYLEX1 - Expression Vect MIC2 Gene Protein, CD99; MIC2 Gene Protein, CD99; MIC2 Gene Protein, CD99; ATF3 Expression Media Products Expression Media Products Expression Media Products T4 SSB (gene 32) protein T4 SSB (gene 32) protein T4 SSB (gene 32) protein

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