根據NCBI 基因資料庫顯示，ROGDI 位於人類染色體16p13.3上，遺傳編碼區為864 bp，轉譯出蛋白質有287 個胺基酸；目前是一尚未知功能的基因。生物資訊預測其可能為一個親水性的蛋白質，並含有leucine zipper domain 的結構，而已知的一些轉錄因子則以leucine zipper 結構為其作用功能區。實驗室之前已選殖出此基因，進一步將此基因的遺傳編碼區，由 pGEX-6P-1-ROGDI 以BamHI 及EcoRI 酵素所切割下的片斷產物轉殖入pcDNA3.1/His C vector，建構基因表達質體 pcDNA3.1/His C-ROGDI ，並轉染入HEK 293T 細胞株 ，藉以探討此基因對HEK 293T 細胞株的影響。由西方點墨法的結果，我們依此基因在HEK293T 細胞內蛋白表現量區分為高、中、低不同的細胞clones。細胞群落形成分析、生長曲線、固著非依賴性生長分析和細胞代謝活性分析結果皆顯示：蛋白表現量高的HEK293T 細胞 clones 之細胞增生速率較蛋白表現量低的細胞clones 快速。因此，推測ROGDI 基因可能為一細胞週期正調節蛋白且在HEK293T 細胞增生過程中扮演重要角色。

According to GenBank, ROGDI is located on chromosome
16p13.3 and the size of its coding region is 864 bp which encodes
287 amino acids. It is a novel gene which has unknown function. By
bioinformatic analysis, the product of this gene was predicted as a hydrophilic protein containing leucine zipper domain. Some transcription factors utilize their leucine zipper structures as function domains. A full-length coding region cDNA of this gene was cloned in our laboratory. After the ROGDI gene was transfected into HEK293T cells, cell clones with different ROGDI protein expression levels were selected and classified into groups of high, middle and low. According to the results of foci formation assay, growth curve, anchorage indepentdent growth assay and MTS assay, it is found that clones with higher ROGDI protein level could enhance faster proliferation rate of HEK293T cells. Thus ROGDI may be a positive regulator of cell cycle and may play a role in cell proliferation.

中文摘要
英文摘要
目錄
前言……………………………………………….……….1
實驗目的..…………………………………………………6
材料與方法…………………………………….………….7
結果與討論…………………………………….………...18
結論………………………………………….…………...26
參考文獻……………………………………….………...28
圖表………………………………………….…………...31

陳桂秋，2006。人類基因ROGDI蛋白質多株抗體製備及初步特性分析，碩士論文，國立中山大學生物科學系研究所。
Abba M. C., Hu Y., Sun H., Drake J. A., Gaddis S., Baggerly K.,
Sahin A., Aldaz C. M. Gene expression signature of estrogen
receptor alpha status in breast cancer. BMC Genomics. 2005；Mar
11;6(1):37.
Claassen G., Ke N., Yu D., Chatterton J. E., Hu X., Albers A.,
Nguy V., Chionis J., Truong T., Meyhack B., Wong-Staal1 F., Li1
Q.X. Comprehensive Assessment of Cell Growth Properties Using
an Integrated and Nonsubjective Approach.Research
Articles.2004； 2(6) :435-439.
Gao F., Cao Ml., Wang L. Brain hyaluronan binding protein
inhibits tumor growth.Chinese Medical Journal. 2004 ；
117(7):1072-1078.
Horng JT, Huang HD, Wang SH, Chen MY, Huang SL, Hwang JK.
Computing motif correlations in proteins. Journal of
Computational Chemistry. 2003； 24(16):2032-2043.
Landschulz WH., Johnson PF., McKnight SL. The leucine zipper:
a hypothetical structure common to a new class of DNA-binding
proteins. Science. 1988； 240:1759-1764.
Meyer IM., Durbin R. Gene structure conservation aids similarity
based gene prediction. Nucleic Acids Research. 2004 ；
32(2):776-783.
29
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K.,et al. Complete sequencing and
characterization of 21,243 full-length human cDNAs. Nat.
Genet.2004； 36 (1): 40-45.
Pandey A., Mann M., Proteomics to study genes and genomes.
Nature. 2000 ; 405： 837-846.
Riss TL., Moravec RA. Use of Multiple Assay Endpoints to
Investigate the Effects of Incubation Time, Dose of Toxin, and
Plating Density in Cell-Based Cytotoxicity Assays. ASSAY and
Drug Development Technologies.2004； 2(1):51-62.
Wollacott AM., Desjarlais JR. Virtual interaction profiles of
proteins. Journal of Molecular Biology. 2001 ; 313(2): 317-342.
Wonsey DR., Follettie MT. Loss of the Forkhead Transcription
Factor FoxM1 Causes Centrosome Amplification and Mitotic
Catastrophe.Cancer Research. 2005；June 15；65(12): 5181-5189.