Legitimitet i förhållande till hjälporganistioner : En kvalitativ studie om legitimitetsskapande och synen på nya typer av aktörer

Denna studie har ett syfte att undersöka hur legitimitet kan skapas i hjälporganisationer. Det är en fråga vi anser vara aktuell att undersöka i och med uppkomsten av nya hjälporganisationer vars trovärdighet i somliga fall kan anses högst tveksam. Studiens resultat kommer att illustreras i en verklig hjälporganisation. Denna organisation kommer förbli anonym genom hela uppsatsen men med sitt kontroversiella arbetssätt och moderna arbetsmetoder anses den förespråka den typ av organisation som vi vill undersöka inom det hjälporganisatoriska fältet.

Additional file 2: Figure S1. of Synthetic circuits that process multiple light and chemical signal inputs

TCP fusion proteins induce rtTAm-dependent expression of GFP. We transfected HEK cells with mCherry, mCherry-TCP, or mCherry-NLS-TCP constitutive expression plasmids, respectively, also transfected TRE3G promoter controlled GFP expression plasmid to all the three groups of cells. We divided mCherry transfected cells into two dishes and treated one dish of the cells with 1 μg/ml Dox at 24 h after transfection. The images were collected at 72 h after transfection. (TIF 532 kb

Additional file 3: Figure S2. of Synthetic circuits that process multiple light and chemical signal inputs

Kinetics of the circuit. (A) Kinetics of the circuit responding to blue light illumination with constitutive rtTAm expression. The cells were illuminated by blue LED (1.25 W m−2) for 0 h, 5 h, 10 h, 20 h and 40 h, respectively. The data are presented as mean ± SD (n = 6). (B) Kinetics of the circuit responding to Dox with constitutive rtTAm expression. The cells were treated with 1 μg/ml of Dox for 0 h, 5 h, 10 h and 20 h, respectively. The data are presented as mean ± SD (n = 6). (C) Kinetics of the circuit responding to cumate with constitutive mCherry-TCP expression. The cells were treated with 30 μg/ml of cumate for 0 h, 5 h, 10 h, 20 h and 40 h, respectively. The data are presented as mean ± SD (n = 6). (TIF 1013 kb

Inhibitory effect of commercial rhIGFBP-3 on human MCF-7 breast cancer cells and HT-29 colon cancer cells.

<p>Different concentrations of commercial rhIGFBP-3 ranged from 9.375 ng/ml to 300 ng/ml were used to treat MCF-7 and HT-29 cells. Data are shown as means ± SD.</p

Inhibitory effect of different concentration of rice-produced rhIGFBP-3 on HT-29 human colon cancer cells.

<p>Different concentration of seed proteins (ranged from 1.042 to 15.625 mg) from WT and transgenic SBK-66 and SB-57 lines were used to treat HT-29 cells. Data are shown as means ± SD. *<i>p</i> < 0.05 and ** <i>p</i> < 0.01 denote statistically significant and very significant differences, respectively, between transgenic lines and WT.</p

Transgenic integration of modified hIGFBP-3 in rice.

<p>Genomic DNA extracted from rice leaves of independent transformants was digested with BamHI and separated on 0.8% agarose gel, blotted on nylon membrane and hybridized with DIG-labeled hIGFBP-3 probe. Lanes 1-3: three independent pSB130/Gt1/hIGFBP-3 transformants (B1 to B3); lane 4: wild type (WT) rice plant; lanes 5-6: two independent pSB130/Gt1/SP/hIGFBP-3 transformants (SB1 to SB2); lanes 7-9: three independent pSB130/Gt1/SP/hIGFBP-3::KDEL transformants (SBK1 to SBK3).</p

Inhibitory effect of rice-produced rhIGFBP-3 on MCF-7 human breast cancer cells.

<p>(A) Equal amount (3.125 mg seed) of WT, SB and SBK total seed protein extracts were added to the MCF-7 cells separately. Data are shown as means ± SD. *<i>p</i> < 0.05 and ** <i>p</i> < 0.01 denote statistically significant and very significant differences, respectively, between transgenic lines and WT.</p

Glycoprotein staining of transgenic lines and WT line in rice seeds.

<p>Total protein was extracted from mature dehulled seeds of SB-57 and SBK-66 transgenic lines and WT. RNase B was used as the glycoprotein control. To evaluate endoglycosidase digestion efficiency, RNase B was digested by PNGase F and Endo H. Lane 1: marker; lane 2: WT; lane 3: SBK-66; lane 4: SK-57; lane 5: RNase B control without digestion; lane 6: RNase B digested by PNGase F; and lane 7: RNase B digested by Endo H. Band 1: PNGase F; band 2: RNase B; band 3: RNase B with Endo H digestion, and band 4: RNase B with PNGase F digestion.</p

Western blot analysis of transgenic rice grains.

<p>Total protein was extracted from mature rice grains of different transformants. Recombinant hIGFBP-3 protein was used as positive control. (A) Lanes 1-5: five independent pSB130/Gt1/hIGFBP-3 transformants (B1-5); lane 6: WT; lane 7: positive control (+ve) - commercial rhIGFBP-3 protein. (B) Lanes 1-5: five independent pSB130/Gt1/SP/hIGFBP-3 transformants (SB1-5); lane 6: WT; lane 7: +ve - commercial rhIGFBP-3 protein. (C) Lanes 1-5: five independent pSB130/Gt1/SP/hIGFBP-3::KDEL transformants (SBK1-5); lane 6: WT; lane 7: +ve - commercial rhIGFBP-3 protein.</p

Western blot analysis of rhIGFBP-3 digested by Endo H in transgenic rice seeds.

<p>Total protein was extracted from mature dehulled seeds of SB-57 and SBK-66 transgenic lines and digested by Endo H. Lane 1: SB-57; lane 2: SB-57 digested by Endo H; lane 3: marker; lane 4: SBK-66; and lane 5: SBK-66 digested by Endo H.</p