![]() ![]() (C) Specificity of antibodies was also confirmed by testing cellular extracts from myc-tagged mIRIP (pEF/myc/mIRIP)-transfected cells with antibodies which were preadsorbed with GST-mIRIP. The recombinant protein was detected only in cells transfected with mIRIP. (B) Cellular extracts were prepared from HeLa and NIH 3T3 cells transiently transfected with myc-tagged mIRIP construct (+) or cells transfected with expression vector (−). The purified GST-mIRIP was detected by antibodies in Western blots. coli was used for generation of rabbit polyclonal antibodies. (A) Purified mIRIP protein expressed in E. ![]() Generation of anti-IRIP antibiotics and expression of IRIP in cell lines and kidney subcellular fractions. On the basis of these results, we propose that IRIP regulates the activity of a variety of transporters under normal and pathological conditions. We measured transport kinetics of OCT2-mediated uptake and demonstrated that IRIP overexpression significantly decreased V(max) but did not affect K(m). Conversely, inhibition of IRIP expression by small interfering RNA or antisense RNA increased MPP+ uptake. The activities of exogenous organic cation transporters (OCT2 and OCT3), organic anion transporter (OAT1), and monoamine transporters were also inhibited by IRIP. IRIP overexpression inhibited endogenous 1-methyl-4-phenylpyridinium (MPP+) uptake activity in HeLa cells. A possible role of IRIP in regulating transporter activity was subsequently investigated. The interaction between IRIP and RS1 was further confirmed in coimmunoprecipitation assays. The transporter regulator RS1 was identified as an IRIP-interacting protein in yeast two-hybrid screening. Besides ischemia/reperfusion, endotoxemia also activated the expression of IRIP in the liver, lung, and spleen. Mouse IRIP mRNA was expressed in all tissues tested, the highest level being in the testis, secretory, and endocrine organs. IRIP cDNA was isolated in a differential display analysis of an ischemia/reperfusion-treated kidney RNA sample. This application requires that you have iTunes installed and an iPod connected to the computer.We report the identification and characterization of a new ischemia/reperfusion-inducible protein (IRIP), which belongs to the SUA5/YrdC/YciO protein family.Thus, by only connecting it to a PC and installing the software we will be able to download all the songs that we want without problems. Thanks to iRip, we will be able to share our music library with anyone on any PC, a good idea is to activate the Use as Drive option of the iPod and store the iRip application on the iPod itself. It will also offer the option to download the full library, but in this case, the transfer may need quite a long time, depending on the amount of MP3 files that we have stored on the iPod. ![]() This simple application will show us the full list of songs that we have stored on our iPod or iPhone and it will allow us to select those that we want to transfer. With many MP3 players, the files can be managed by means of the Windows Explorer, simply copying and pasting, but to be able to do the same with an iPod or iPhone, it is necessary to use iRip (that used to be called iPodRip). Transfer files from iPhone or iPod to Mac This is a major problem if we want to share an MP3 file with anyone and we only have it stored on our iPod. So if you want to store an MP3 on any iPod, it is necessary to synchronize it with the corresponding library. One of the main problems with Apple's MP3 players is that they can only be managed by means of iTunes. ![]()
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