• Title/Summary/Keyword: GEN1

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A New Genus and a New Species of Aquatic Oribatid Mite (Acari: Oribatida) from Korea (한국산 수서성 날개응애의 1신속 1신종)

  • 최성식
    • The Korean Journal of Soil Zoology
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    • v.1 no.1
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    • pp.1-4
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    • 1996
  • This paper deals with a new genus, Mainothrus gen. n., and a new species, M. aquaticus sp. n., belonging to Trhypochthoniidae Willmann, 1931 from Korea. The key characters of the new genus distinguishable from other genera of Trhypochthoniidae are 1) six pairs of genital setae, 2) two pairs of anal setae, 3) fifteen pairs of notogastral setae, and 4) epimeral setal formula; 3-1-3-2.

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비즈니스 인사이드 - 한국후지제록스, 아이젠 150 프레스.아이젠 4 출시

  • Im, Nam-Suk
    • 프린팅코리아
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    • v.13 no.1
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    • pp.96-97
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    • 2014
  • 한국후지제록스(대표 우에노 야스아키, www.fujixerox.co.kr)는 고속 컬러 디지털 인쇄기 '아이젠 150 프레스(iGen 150 Press)'와 '아이젠 4 EXp(iGen4 EXP)' 출시를 기념하는 행사를 구랍 12일 서울 홍은동 그랜드힐튼호텔 그랜드볼룸에서 가졌다. 이 날 행사에는 한국후지제록스의 고객과 임직원 100여명이 참석해 성황을 이뤘다.

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A New Genus and Species, Koreoxyomus koreanus, from Korea and Taxonomic Discussion on the Genus Mozartius of Japan(Coleoptera, Aphodiidae) (韓國産 똥풍이科의 1新屬, 1新種의 記載 및 日本産 Mozartius屬의 分類學的 檢討)

  • 김진일
    • Animal Systematics, Evolution and Diversity
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    • v.12 no.2
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    • pp.101-105
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    • 1996
  • A new genus and species belonging to the family Aphodiidae (Coleoptera) Koreoxyomus koreanus gen. et sp. nov., is described from Korea. And a genus known from Japan, Mozartius is discussed because it is almost same taxa with present new genus but its original description is not stable taxonomically.

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Sequence Analysis of the Coat Protein Gene of a Korean Isolate of Iris Severe Mosaic Potyvirus from Iris Plant

  • Park, Won-Mok;Lee, Sang-Seon;Park, Sun-Hee;Ju;Ryu, Ki-Hyun
    • The Plant Pathology Journal
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    • v.16 no.1
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    • pp.36-42
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    • 2000
  • The coat protein gene of iris severe mosaic potyvirus, which was isolated in Korea, ISMV-K, from iris plant was cloned and its nucleotide sequence was determined. The coat protein of the virus contained 252 amino acid residues, including five potential N-glyxosylation site motifs. The coat protein of ISMV-K has 99.1% and 98.4% sequence identities with those of the Netherlands isolate of ISMV (ISMV-Ne) form crocus for the nucleotide and amino acids, respectively. The coat protein of ISMV-K has 50.4% to 60.3% nucleotide sequence identities and 47.3% to 55.7% amino acid identities with those of other 21 potyviruses, indicating ISMV to be a distinct species of the genus. The coat protein of ISMV-K was closely related with bean yellow mosaic virus and clover yellow vein virus in the phylogenetic tree analysis among the potyviruses analyzed. ISMV was easily and reliably detected from virus-infected iris leaves by RT-PCR with a set of the virus-specific primers.

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Overproduction of Recombinant Human VEGF (Vascular Endothelial Growth Factor) in Chinese Hamster Ovary Cells

  • Lee, Seong-Baek;Park, Jeong-Soo;Lee, Seung-Hee;Park, Jun-Ho;Yu, Sung-Ryul;Kim, Hee-Chan;Kim, Dong-Jun;Byun, Tae-Ho;Baek, Kwang-Hee;Ahn, Young-Joon;Yoon, Jae-Seung
    • Journal of Microbiology and Biotechnology
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    • v.18 no.1
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    • pp.183-187
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    • 2008
  • Vascular endothelial growth factors (VEGFs) are a family of proteins that mediate angiogenesis. $VEGF_{165}$ is a VEGF-A isoform and has been extensively studied owing to its potential use in therapeutic angiogenesis. This study established Chinese hamster ovary (CHO) cells overexpressing recombinant human $VEGF_{165}$ $(rhVEGF_{165})$ protein. The production rate of the established CHO cells was over 80mg/l of $rhVEGF_{165}$ protein from a 7-day batch culture process using a 7.5-l bioreactor with a 5-l working volume and serum-free medium. The $rhVEGF_{165}$ protein was purified to homogeneity from the culture supernatant using a two-step chromatographic procedure that resulted in a 48% recovery rate. The purified $rhVEGF_{165}$ protein was a glycosylated homodimeric protein with a higher molecular weight (MW) than the protein expressed from insect cells, suggesting that the glycosylation of the $rhVEGF_{165}$ protein in CHO cells differed from that in insect cells. The purified $rhVEGF_{165}$ protein in this study was functionally active with a half-maximal effective concentration of 3.8ng/ml and specific activity of $2.5{\times}10^5U/mg$.

A New Genus and Two New Species of Copepoda(Poecilostomatoida, Sabelliphilidae) Associated with the Tubicolous Polychaetes in the Yellow Sea

  • Hoi, I-I
    • Animal cells and systems
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    • v.5 no.1
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    • pp.1-9
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    • 2001
  • Terebelliphilus simplex n. gen., n. sp. and Myxomolgus invulgus n. sp. are described from the tubicolous polychaetes found in the intertidal shores in the Yellow Sea. The new genus Terebelliphilus belongs to the family Sabelliphilidae but is characteristic in bearing the reduced segmentations In legs 1-4, an unusual sexual dimorphism in antennule, and the ventral location of genital areas. Myxomolgus invulgus is readily distinguishable from its congeners by the morphological features of rostrum, antennule, mandible, maxilla, leg 4 and female leg 5.

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Enhancing the Solubility of Recombinant Akt1 in Escherichia coli with an Artificial Transcription Factor Library

  • Park Kyung-Soon;Lee Ho-Rim;Kim Jin-Soo
    • Journal of Microbiology and Biotechnology
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    • v.16 no.2
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    • pp.299-302
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    • 2006
  • A combinatorial library of artificial transcription factors (ATFs) was introduced into the bacterial cells that expressed the Akt1-GFP fusion protein. By measuring the level of fluorescence generated by the transformed E. coli cells, we were able to obtain clones in which ATFs increased the solubility of the Akt1. Our results show that ATF library is a useful tool for increasing the solubility of selected recombinant proteins in E. coli.