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Pullman, WA, United States

Karakus F.,Yuzuncu Yil University | Yilmaz A.,Bitlis Eren University | Hakan B.,Catak Ilce Gida Tarim ve Hayvancilik Mudurlugu | Stormo K.,Amplicon Express Inc | ulker H.,Yuzuncu Yil University
Animal Reproduction Science

The objective of this study was to evaluate the effectiveness of recombinant LHRH fusion protein, Ovalbumin-LHRH-7 (OL), using a single-dose vaccination protocol in combination with different adjuvants in suppressing reproductive functions in buck kids. For this purpose, either a mixture of free OL antigen and encapsulated OL antigen, or encapsulated OL antigen was used. Thirty-nine native buck kids at 12 weeks of age were divided into control (n=7) and treatment groups (n=8 bucks/group). The four treatment groups were formed according to the different vaccine formulations: Group CpG received 0.5. mg free OL protein together with 1.0. mg of encapsulated protein with CpG adjuvant. Group mFCA received 0.5. mg free OL protein together with 1.0. mg of encapsulated protein with modified Freund's complete adjuvant. Group IS received 1.5. mg encapsulated OL protein with a mix of inulin and saponin adjuvants. Group ISmFCA received 1.5. mg encapsulated OL protein with a mix of inulin, saponin and modified Freund's complete adjuvants. Scrotal circumference in CpG and mFCA groups were significantly smaller than that of Control, IS and ISmFCA groups (P<0.05). Numbers and percentage of bucks having spermatozoa in their ejaculate were significantly lower in CpG and mFCA groups (P<0.05). OL immunization completely suppressed sperm production, except one buck, in CpG and mFCA groups (P<0.05). These results imply that it is possible to use OL protein in a single injection protocol for the purpose of immunocastration. Further investigation with a larger number of animals should be carried out to determine the longevity of response to a single injection. © 2013 Elsevier B.V. Source

Ulker H.,Yuzuncu Yil University | Stormo K.,Amplicon Express Inc | deAvila D.,Washington State University | Reeves J.J.,Yuzuncu Yil University
Animal Science Papers and Reports

The objective of this study was to evaluate effectiveness of Ovalbumin-LHRH-7 (OL) protein when injected in crude, purified, free or encapsulated forms and using a single vaccination protocol along with CpG, inulin and saponin adjuvants. Fifty six C57BL/6 mice in seven groups (n=8) received various treatments and doses: Group 1 was control; Group 2 and 3 were injected twice with purified or crude OL protein, respectively, 4 wks apart. Group 4 and 5 were injected only once with purified or crude OL protein, respectively. Group 6 was injected only once with a mix of purified OL protein and encapsulated purified OL protein. Group 7 was injected only once with a mix of crude OL protein and encapsulated crude OL protein. There was an immunization effect observed on the I125 LHRH % binding (P<0.05). Antibodies (Abs) against LHRH were identified on week 5 of immunization in groups 2, 3 and 4. Boosting at week 5 caused a significant increase in LHRH antibody (Ab) concentrations in groups 2 and 3. Numbers of pregnant animals and prengnancy rates were suppressed in all treatment groups at various degrees (P<0.05). Numbers of pups born were affected by immunization (P<0.05). Concluding, immunization with OL protein generated either biological or both immunological and biological effects in the most of treatment groups. The study confirmed the earlier findings that purified OL protein with CpG adjuvant is effective in inducing immune response and suppressing reproductive functions. However, the original idea that the non-capsulated antigen/adjuvant mix would work as primary injection, while encapsulated counterpart would mimic booster injections in a single vaccination protocol could not be confirmed in this study. Further studies to determine affecting factors for single-injection LHRH immunization are needed. Source

Amplicon Express Inc. | Date: 2013-04-19

Diagnostic and testing kits consisting primarily of scientific apparatus and instruments, namely, thermocyclers and automated DNA sequencers used in identifying polynucleotides for the purpose of determining whether certain biological material is present in a sample in order to verify the authenticity or source of a product or good. Biomanufacturing services for others in the field of biochemical solutions, namely, manufacturing of concentrated solutions of various sequences of polynucleotides using biological organisms in the manufacturing process; polynucleotide manufacturing services, namely, the custom manufacture of DNA and RNA and its components. Biological analysis, namely, polynucleotide analysis; providing a database for storing and accessing polynucleotide sequence information; scientific research, namely, polynucleotide sequence development for the purpose of creating unique, known, private, or public strings of polynucleotide sequences to be used in a tagging/labeling system for verifying authenticity or source of a product or good.

Amplicon Express Inc. | Date: 2012-10-30

A substance identification method includes combining substances into four or more intermediate subpools in wells of a subpool plate and repooling the intermediate subpools into a number of final screening pools based on a repooling design providing the subpooled substances in at least three different final screening pools. The repooling design determines coordinates locating well positions for the substances. Another substance identification method includes using a two-dimensional array of wells arranged in rows and a number of columns that is at least 1.5 times the rows. Substances in the wells are combined into a number of screening pools. Individual screening pools include substances from wells having a row identifier in common with one other well. A pooling design provides the pooled substances in two different screening pools. The pooling design determines coordinates locating well positions for the substances.

Van Oeveren J.,Keygene NV | De Ruiter M.,Keygene NV | Jesse T.,Keygene NV | Van Der Poel H.,Keygene NV | And 8 more authors.
Genome Research

We present whole genome profiling (WGP), a novel next-generation sequencing-based physical mapping technology for construction of bacterial artificial chromosome (BAC) contigs of complex genomes, using Arabidopsis thaliana as an example. WGP leverages short read sequences derived from restriction fragments of two-dimensionally pooled BAC clones to generate sequence tags. These sequence tags are assigned to individual BAC clones, followed by assembly of BAC contigs based on shared regions containing identical sequence tags. Following in silico analysis of WGP sequence tags and simulation of a map of Arabidopsis chromosome 4 and maize, a WGP map of Arabidopsis thaliana ecotype Columbia was constructed de novo using a six-genome equivalent BAC library. Validation of the WGP map using the Columbia reference sequence confirmed that 350 BAC contigs (98%) were assembled correctly, spanning 97% of the 102-Mb calculated genome coverage. We demonstrate that WGP maps can also be generated for more complex plant genomes and will serve as excellent scaffolds to anchor genetic linkage maps and integrate whole genome sequence data. © 2011 by Cold Spring Harbor Laboratory Press. Source

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