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Many veterans purchased U.S. savings bonds while serving in the military through a payroll savings program. When those bonds mature and stop earning interest, it is time to redeem them. Redeeming bonds is easy - just take them to a local bank or send them to the Bureau of the Fiscal Service. Directions are available on our web site at If you are unsure whether you own a matured savings bond, a secure search engine is available at New information about matured savings bonds is added monthly to Treasury Hunt.


"American citizens hold approximately $30 billion in matured, unredeemed savings bonds. We encourage all bond owners, especially veterans, to claim funds owed to them" says Stephen Hofmann, military veteran and Project Manager for the Bureau's Office of Retail Securities Services. Redeeming a matured savings bond is easy. And who couldn't use some extra money these days?

Engineered tissues can be used to model human pathophysiology and test the efficacy and safety of drugs. Yet, to model whole-body physiology and systemic diseases, engineered tissues with preserved phenotypes need to physiologically communicate. Here we report the development and applicability of a tissue-chip system in which matured human heart, liver, bone and skin tissue niches are linked by recirculating vascular flow to allow for the recapitulation of interdependent organ functions. Each tissue is cultured in its own optimized environment and is separated from the common vascular flow by a selectively permeable endothelial barrier. The interlinked tissues maintained their molecular, structural and functional phenotypes over 4 weeks of culture, recapitulated the pharmacokinetic and pharmacodynamic profiles of doxorubicin in humans, allowed for the identification of early miRNA biomarkers of cardiotoxicity, and increased the predictive values of clinically observed miRNA responses relative to tissues cultured in isolation and to fluidically interlinked tissues in the absence of endothelial barriers. Vascularly linked and phenotypically stable matured human tissues may facilitate the clinical applicability of tissue chips.

Results: We demonstrated the economic generation of >1108 mature hPSC-CMs per PDMS-lined roller bottle. Compared with their counterparts generated on tissue culture plastic substrates, PDMS-matured hPSC-CMs exhibited increased cardiac gene expression and more mature structural and functional properties in vitro. More important, intracardiac grafts formed with PDMS-matured myocytes showed greatly enhanced structure and alignment, better host-graft electromechanical integration, less proarrhythmic behavior, and greater beneficial effects on contractile function.

A superior matured balsamic vinegar with rich, sweet and sour flavours. Colour, sweetness, density and harmony of flavour distinguish this as vinegar of authentic quality and provenance, hence its Four Leaf seal award.An essential larder staple, it's delicious as a condiment for dressings, roasted meats, marinades and even desserts.

Rift Valley fever virus (RVFV), genus Phlebovirus, family Bunyaviridae is a zoonotic arthropod-borne virus able to transition between distant host species, causing potentially severe disease in humans and ruminants. Viral proteins are encoded by three genomic segments, with the medium M segment coding for four proteins: nonstructural NSm protein, two glycoproteins Gn and Gc and large 78 kDa glycoprotein (LGp) of unknown function. Goat anti-RVFV polyclonal antibody and mouse monoclonal antibody, generated against a polypeptide unique to the LGp within the RVFV proteome, detected this protein in gradient purified RVFV ZH501 virions harvested from mosquito C6/36 cells but not in virions harvested from the mammalian Vero E6 cells. The incorporation of LGp into the mosquito cell line - matured virions was confirmed by immune-electron microscopy. The LGp was incorporated into the virions immediately during the first passage in C6/36 cells of Vero E6 derived virus. Our data indicate that LGp is a structural protein in C6/36 mosquito cell generated virions. The protein may aid the transmission from the mosquitoes to the ruminant host, with a possible role in replication of RVFV in the mosquito host. To our knowledge, this is a first report of different protein composition between virions formed in insect C6/36 versus mammalian Vero E6 cells.

RVFV, just as other arthropod-borne viruses, has the ability to efficiently transition from insect to mammalian hosts and to successfully replicate in both. Mechanisms and factors facilitating the transition have yet to be elucidated; however, physical properties of virions may be one of the contributing factors. Differences in the lipid composition of the envelope, the N-glycosylation of the attachment proteins, the configuration of envelope glycoproteins, and the ribonuclear structure between virions matured in mammalian cells versus mosquito cells were detected [11], [12], [13]. To date, differences in protein composition of arboviral virions were not reported.

Purification flow of RVFV virions matured in C6/36 cells (second passage in C6/36 cells) is on the left panels of the figure; purification flow of the Vero E6 matured virions (first passage of C6/36 virus in Vero cells) is on the right panels of the figure. Fig. 5.A. Immunoblot using goat antiserum against RVFV of the fractions collected after concentration/semipurification through 20% sucrose onto 70% sucrose cushion. Beside structural proteins Gn/Gc and N, the LGp, as well as nonstructural proteins NSs and NSm were detected in the semipurified virion preparation. The assignment of RVFV proteins to protein bands reacting with the goat RVFV-antiserum was based on expected protein sizes, and known reactivity of the antiserum with respective recombinant proteins. Fig. 5.B. RVFV RNA profiles of fractions collected from the discontinuous 20 to 70% gradient (collected from the bottom). Fractions 10 and 11 were then pelleted down and lysed in the loading buffer for the SDS-PAGE. Fig. 5.C. Silver stain of the proteins from the gradient purified virion fractions separated by SDS-PAGE. Fig. 5.D. Aliquots of the samples from Fig.5.C. analyzed by immunoblotting using goat anti-RVFV serum (left panels designated L) or the SW9-22E antibody (right panels designated R). LGp was detected only in the C6/36 RVFV virions, both virion preparations had detectable levels of structural N and Gn/Gc proteins only.

In agreement with previously published reports [9], [22], analysis of gradient purified virions from Vero E6 cells did not indicate presence of LGp in the virions. The LGp appeared to be incorporated only into the C6/36 produced virions based on immunoblots with the anti-LGp mouse monoclonal antibody SW9-22E and the goat anti-RVFV serum, and analysis by mass spectrophotometry (Fig. 6). The blots originally probed with the SW9-22E antibody (Fig.6.A.b, 6.A.d. and Fig.6.C.b) were stripped and re-probed with goat anti-RVFV serum confirming the findings. Although the goat RVFV-antiserum was able to recognize two forms of the LGp on the immunoblots (Figure 3.A-right panel), due to re-probing of a membrane originally used for blotting with the monoclonal SW9-22E antibody, only the more abundant, larger form of the LGp was clearly apparent on the blots shown in Figures 5.D/right panel for C6/36 virions and in Figures 6.A.c and 6.A.e. The mouse monoclonal antibody recognized only one, the less abundant smaller, form of the LGp in the C6/36 matured virions (Figure 5.D, left panel for C6/36 virions, and Figures 6.A.b and 6.A.d. Structural proteins of C6/36 derived virions comprised N, Gn/Gc and LGp, and only N and Gc/Gn were confirmed in Vero E6 cell derived virions (Fig.6.A.c and Fig.6.A.e compared to Fig.6.C.c.). Silver staining of protein gels of the virion preparations (Fig.6.A.a and Fig.6.C.a) was beside assessment of purity also used to assess the loading of the gels. Attempts were made to use the NanoOrange Protein Quantitation Kit. Unfortunately, we had to use 1% SDS solution in order to be able to remove the protein virion preparations from the zoonotic AgBSL3 laboratory. This amount exceeded the percentage tolerable by the assay. Intensity of bands on the silver stained gels was used instead. We compared the RVFV N protein quantities based on their ratio to the 28 kDa marker used as a standard. The respective band intensities are recorded in Fig.6.D.a, and indicate higher N protein loading for Vero E6virions in Fig.6.A.a compared to Fig. 6.C.a. The N protein to 28 kDa marker ratio for C6/36 cell matured virions was 1.08, and the ratio for the Vero E6 matured virions in lane 1 was 1.68, while in lane 2 the ratio was higher than 2.5. Although the gel with Vero E6 virions was overloaded, no LGp was observed in virion preparations from this cell line.

In addition, mass spectrophotometry was performed to confirm detection of the LGp in C6/36 virions. Gel slices were excised from protein separation gels of both types of virion preparations in the areas corresponding to the approximately 80 kDa molecular size where positive protein band was detected on the immunoblots with C6/36 matured virions using the mouse monoclonal antibody SW9-E22 or goat anti-RVFV serum. The.analysis by mass spectrophotometry detected 51% coverage of the LGp (353 of 697 amino acids; Fig.6.D.b), including the VSLSSTR sequon unique to LGp in the RVFV, Chlorocebus aetiops and Aedes albopictus proteomes, and the TSSQELYR sequon shared by LGp and the NSm protein. Total of five samples per C6/36 virion preparations as well as Vero-E6 preparations were analyzed, with only C6/36 virions being positive for presence of the LGp.

Presence of the large glycoprotein LGp on the surface of C6/36 derived virions was further confirmed by immune-electron microscopy in semipurified virion preparations (see Fig. 5), due to difficulties with purification of intact virions, especially the ones produced in Vero E6 cells. Monoclonal antibody SW9-22E detected the LGp only on virions matured in C6/36 cells, as the gold particles were found associated solely with the virion structures (Fig.7.A.). The relatively sparse labeling of the RVFV virions matured in C6/36 cells with the monoclonal antibody SW9-22E may be due to virions having both glycosylation forms of the LGp incorporated into their structure with only the less abundant form recognized by this antibody and labeled with the gold particles. In the Vero E6 matured RVFV virion preparations, the gold particles could be found only occasionally and always associated with debris. (Fig. 7.B.) Attempts were made to label the virions also with anti-Gn monoclonal antibody, unfortunately although the antibody worked well on immunoblots [16] it was not reacting with the virions. The negatively stained C6/36 matured virions (bottom panels) appeared also somewhat larger than the Vero E6 virions (upper panels, Fig. 7.C.). These observations warrant future structural and functional studies, as nothing is known about the actual structure of the virions generated in C6/36 cells, including the ratio of Gn:LGp:Gc incorporated into the virions. 041b061a72

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