Pembuatan Aplikasi Sistem Informasi Persebaran Toko Batik Di Kota Pekalongan Berbasis Android

Pekalongan is located in the lowlands along the north coast of Java Island, at a height of approximately one meter above sea level. The geographical position of Pekalongan is between 6° 50\u27 42" to 6° 55\u27 44\u27\u27 North Latitude and 109° 37\u27 55\u27\u27to 109° 42\u27 19\u27\u27 East Longitude.Pekalongan area of about 42.25 km2 or approximately 0.14% from the area of Central Java Province.Pekalongan is known by the nickname city of Batik, because batik Pekalongan has distinctive and varied livery. Therefore, Pekalongan is espected to provide a practical and informative information for tourists, so it can be an attraction and increase the number of tourists coming to Pekalongan. This research uses of spatial and non spasial data in the form of batik store name, the owner\u27s name, phone number, address, and products sold with using the popularity of android smartphone as a platform system information.This application was developed using an SDK Andoidframework, java and PHP programming languages, and MySQL as base data, and Google Maps. The final result of this research is the Android application of the distribution of batik store in Pekalongan is accompanied by information (as has been mentioned above) from each store for easier searching the location of the batik stores in Pekalonga

Dot-blot and <i>in vitro</i> binding of recombinant proteins in human HSC.

<p>(<b>A</b>) Dot-blot analysis of purified recombinant proteins IFNγ, mimetic IFNγ, BiPPB-IFNγ and BiPPB-mimIFNγ using anti-IFNγ and anti-PPB antibody. (<b>B</b>) Representative pictures showing binding of BiPPB-IFNγ and BiPPB-mimIFNγ to human HSC (LX2). Mouse IFNγ and mimIFNγ did not show any binding (similar to control) to human LX2 cells due to species differences and lack of IFNγR or PDGFβR binding sites respectively.</p

Schematic representation of the prokaryotic vectors used for the expression of the recombinant proteins.

<p>IFNγ (<b>A</b>) and mimetic IFNγ (<b>B</b>) were cloned in-frame upstream of His-tag in pET42a (+) vector to achieve cytoplasmic protein expression. The fusion proteins BiPPB-IFNγ (<b>C</b>) and BiPPB-mimIFNγ (<b>D</b>) were expressed in pET39b (+) vector for periplasmic expression of fusion proteins to ensure proper folding and disulfide bonds formation. For the synthesis of fusion proteins, BiPPB was fused to the N-terminal of IFNγ or mimetic IFNγ sequence through a flexible 3 amino acid linker (AAA) maintaining the open reading frame.</p

<i>In vitro</i> effects of the recombinant proteins in human HSC and mouse macrophages.

<p>Representative pictures (<b>A</b>) and western blot analysis (<b>B</b>) of collagen-I stained LX2 cells, incubated with TGFβ (5 ng/ml) in combination with different recombinant proteins (1 µg/ml). In human LX2 cells, only BiPPB-modified proteins attenuated collagen expression, whereas unmodified mouse IFNγ and mimIFNγ did not cause any reduction due to species restriction and lack of receptor binding sites respectively. (<b>C</b>) Representative microscopic photographs depicting the activation of mouse RAW macrophages after 24 h of incubation with mouse IFNγ and BiPPB-IFNγ (1 µg/ml) along with 100 ng/ml LPS. (<b>D</b>) Dose-dependent release of nitrogen oxide (NOx) in mouse RAW macrophages after incubation with unmodified IFNγ and BiPPB modified IFNγ fusion protein. MimIFNγ and BiPPB-mimIFNγ did not induce any NOx release due to absence of IFNγR binding site and/or lack of PDGFβR on RAW macrophages.</p

Effects of recombinant proteins on IFNγ-related adverse effect in the acute CCl₄ model.

<p>Graph represents platelet counts measured in CCl₄-treated mice receiving PBS (n = 6) or the different recombinant proteins IFNγ (n = 6), MimIFNγ (n = 5), BiPPB-IFNγ (n = 6), BiPPB-mimIFNγ (n = 6). Bars represent mean ± SEM of 5–6 mice per group. The results showed a significant reduction in platelet counts following two intravenous administration of IFNγ, which was significantly improved following treatment with BiPPB-mimIFNγ and to a lesser extent with BiPPB-IFNγ. MimIFNγ did not show significant change in platelets counts due to lack of binding to IFNγR or PDGFβR. *P<0.05, **P<0.01 denotes significance versus PBS treated CCl₄ mice. #P<0.05 denotes the significance versus IFNγ-treated CCl₄ mice.</p

Primers used for plasmids construction.

<p>Primers used for plasmids construction.</p

Effects of recombinant proteins on fibrotic parameters in vivo.

<p>(<b>A</b>) Representative pictures of collagen I and α-SMA stained liver sections from olive oil treated mice (normal) or CCl₄-treated mice (acute model) that were treated with IFNγ (n = 6), MimIFNγ (n = 5), BiPPB-IFNγ (n = 6), BiPPB-mimIFNγ (n = 6) or PBS alone (n = 6). Scale bars, 200 µm. (<b>B</b>) Whole-liver lysates from treated animals were subjected to western blot analysis using anti-collagen I antibody. Graph represents collagen I expression (normalized with β-actin) depicted as mean ± SEM from n = 5–6 mice per group. #P<0.05 denotes significance versus PBS treated olive oil mice and *P<0.05, **P<0.01 denotes significance versus PBS treated-CCl₄ mice. For quantitative analysis, the groups were normalized to vehicle group (PBS treated-CCl₄ mice). (<b>C</b>) Effect of recombinant proteins on intrahepatic fibrinolysis as determined by the ratio of MMP13 and TIMP-1 transcripts. The groups were normalized to vehicle group (PBS treated-CCl₄ mice). Bars represent mean ± SEM of 5–6 mice per group. *P<0.05, **P<0.01 denotes significance versus PBS treated-CCl₄ mice.</p

Hepatic stellate cells activation and proliferation in the livers of wild-type and NS3/4A-Tg mice after CCl₄ administration.

<p>Representative pictures of <b>(A)</b> desmin- and <b>(B)</b> α-SMA-stained liver sections of 4-weeks and 8-weeks olive-oil treated and CCl_<b>4</b>-treated wild-type and NS/4A-Tg mice. Scale bars, 200μm (<b>C</b>) quantitative analysis of desmin- and α-SMA stained liver sections. (D) mRNA expression of desmin and α-SMA (normalized with GAPDH) in the livers of wild-type and NS3/4A-Tg. For quantitative histological and mRNA analysis, groups were normalized to olive-oil treated wild-type mice. Bars represent mean ± SEM of n = 5 per group. *p<0.05; **p<0.01; #p<0.05; ##p<0.01; n.s. denotes non-significant.</p

Visualization 2: Preclinical detection of liver fibrosis using dual-modality photoacoustic/ultrasound system

3D photoacoustic visualization (control liver) Originally published in Biomedical Optics Express on 01 December 2016 (boe-7-12-5081

Hepatocyte proliferation and apoptosis in wild-type and NS3/4A-Tg mice after CCl₄ administration.

<p><b>(A)</b> Representative pictures of Ki67-stained liver sections of 4-weeks and 8-weeks olive-oil treated and CCl_<b>4</b>-treated wild-type and NS3/4A-Tg mice. Scale bars, 200μm. Quantitative real-time PCR analysis (normalized with GAPDH) of <b>(B)</b> cyclin D1 and <b>(C)</b> Bax/Bcl2 ratio in the livers of wild-type and NS3/4A-Tg. For quantitative PCR analysis, groups were normalized to olive-oil treated wild-type mice. Bars represent mean ± SEM of n = 5 per group. *p<0.05; **p<0.01; #p<0.05; n.s. denotes non-significant.</p