 ที่มา:Protein Expression and Purificationหัวเรื่อง:Overproduction of the N-terminal anticodon-binding domain of the non-discriminating aspartyl-tRNA synthetase from Helicobacter pylori for crystallization and NMR measurements |
ที่มา:Protein Expression and Purificationหัวเรื่อง:Overproduction of the N-terminal anticodon-binding domain of the non-discriminating aspartyl-tRNA synthetase from Helicobacter pylon for crystallization and NMR measurements |
ที่มา:Protein Expression and Purificationหัวเรื่อง:Expression of foot and mouth disease virus nonstructural polyprotein 3ABC with inactive 3C(pro) in Escherichia coli |
ที่มา:Protein Expression and Purificationหัวเรื่อง:Adenosine deaminase from Streptomyces coelicolor: Recombinant expression, purification and characterization |
ที่มา:Protein Expression and Purificationหัวเรื่อง:Expression of foot and mouth disease virus nonstructural polyprotein 3ABC with inactive 3Cpro in Escherichia coli |
ที่มา:Protein Expression and Purificationหัวเรื่อง:Adenosine deaminase from Streptomyces coelicolor: Recombinant expression, puri?cation and characterization |
ที่มา:Protein Expression and Purificationหัวเรื่อง:Overproduction of the N-terminal anticodon-binding domain of the non-discriminating aspartyl-tRNA synthetase from Helicobacter pylon for crystallization and NMR measurements |
ที่มา:Protein Expression and Purificationหัวเรื่อง:Expression and purification of dalcochinase, a beta-glucosidase from Dalbergia cochinchinensis Pierre, in yeast and bacterial hosts |
ที่มา:Protein Expression and Purificationหัวเรื่อง:Expression and purification of dalcochinase, a ฮฒ-glucosidase from Dalbergia cochinchinensis Pierre, in yeast and bacterial hosts |
 ผลงานตีพิมพ์ในวารสารวิชาการCloning, overexpression, and purification of a gene of unknown function of prophage loci from ‘Candidatus Liberibacter asiaticus,’ the destructive bacterial pathogen of huanglongbing disease in citrus plantsผู้แต่ง: Sudhan, D, Puttamuk, T,  Dr.Supachai Vuttipongchaikij, Associate Professor , Dr.Pitak Chuawong, Associate Professor , วารสาร:  
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ผลงานตีพิมพ์ในวารสารวิชาการExpression and purification of dalcochinase, a ฮฒ-glucosidase from Dalbergia cochinchinensis Pierre, in yeast and bacterial hostsผู้แต่ง:Dr.Prachumporn Kongsaeree, Associate Professor , Metheenukul, P., Sujiwattanarat, P., Paiboon, P., Tongtubtim, N., Ketudat-Cairns M., Ketudat-Cairns, J., Svasti, J., วารสาร: |
ผลงานตีพิมพ์ในวารสารวิชาการSecretory expression of beta-mannanase from Bacillus circulans NT 6.7 in Lactobacillus plantarumผู้แต่ง:Intaratrakul, K, Dr.Sunee Nitisinprasert, Associate Professor , Nguyen, TH, Haltrich, D, Dr.Suttipun Keawsompong, Associate Professor , วารสาร: |
ผลงานตีพิมพ์ในวารสารวิชาการRefolded recombinant major capsid protein (MCP) from Infectious Spleen and Kidney Necrosis Virus (ISKNV) effectively stimulates serum specific antibody and immune related genes response in Nile tilapia (Oreochromis niloticus)ผู้แต่ง:Throngnumchai, Boonyalit, Jitrakorn, Sarocha, Sangsuriya, Pakkakul, Dr.Sasimanas Unajak, Associate Professor , Khunrae, Pongsak, Dong, Ha Thanh, Vanvimon Saksmerprome, Rattanarojpong, Triwit, วารสาร: 
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ผลงานตีพิมพ์ในวารสารวิชาการExpression of foot and mouth disease virus nonstructural polyprotein 3ABC with inactive 3C(pro) in Escherichia coliผู้แต่ง:Sariya, L, Thangthumniyom, N, Dr.Worawidh Wajjwalku, Associate Professor, Mrs.Wilairat Chumsing , Ramasoota, P, Dr.Porntippa Lekcharoensuk, Professor , วารสาร: |
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 หัวเรื่อง:ไม่มีชื่อไทย (ชื่ออังกฤษ : Cloning, Expression, Purification and Biological Activities of Recombinant Mouse Interleukin-2 in E. coli M15) ผู้เขียน:สรรชัย จันทะจร, ดร.รัชนี ฮงประยูร, รองศาสตราจารย์ , ดร.ทวีศักดิ์ ส่งเสริม, ศาสตราจารย์ สื่อสิ่งพิมพ์:pdf AbstractMolecular cloning, sequencing and expression of recombinant mouse interleukin 2 (rmIL-2) were described. The interleukin-2 (IL-2) cDNA, 450 base pairs in length with repeating CAG, was amplified using specific primers. The IL-2 cDNA showed high homology at 100%, 100%, 91%, 96% and 94% with five strains of mice previously reported (GeneBank accession number AY147902.1, MMU41494, MMU41504, MMU41505 and MMU41506). The IL-2 gene was cloned into the pDrive cloning vector and consequently expressed using pQE30 expression vector which provided high expression level of the recombinant protein. The predicted rmIL-2 sequence is 161 amino acids with a molecular weight of 19 kDa. The expressed protein was then purified by Ni-NTA column under denaturing condition. Analysis of the rmIL-2 by SDS-PAGE demonstrated two bands of 19 and 38 kDa representing monomeric and dimeric forms of this protein. The biological activity in stimulating T-cell proliferation was also described and the binding signal to the receptor was easily observed by immunofluorescence. |
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