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![Western Blot: PTH1R/PTHR1 Antibody (3D1.1) [NBP1-40067] - PTH1R protein expression by immunoblot of e13.5 tissue lysates from wild type and Ramp2-/- placentas. Image collected and cropped by CiteAb from the following publication (dx.plos.org/10.1371/journal.pone.0181597), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/PTH1R-PTHR1-Antibody-3D1-1-Western-Blot-NBP1-40067-img0004.jpg "<b>Biological Strategies Validation. </b>Western Blot: PTH1R/PTHR1 Antibody (3D1.1) [NBP1-40067] - PTH1R protein expression by immunoblot of e13.5 tissue lysates from wild type and Ramp2-/- placentas. Image collected and cropped by CiteAb from the following publication (dx.plos.org/10.1371/journal.pone.0181597), licensed under a CC-BY license.")
![<b>Biological Strategies Validation. </b>Immunohistochemistry: PTH1R/PTHR1 Antibody (3D1.1) [NBP1-40067] - Immunofluorescence for PTH1R in the labyrinth of wild type and Ramp2-/- placentas. Scale bars, 100 um. Image collected and cropped by CiteAb from the following publication (dx.plos.org/10.1371/journal.pone.0181597), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/PTH1R-PTHR1-Antibody-3D1-1-Immunohistochemistry-NBP1-40067-img0003.jpg)
![Immunohistochemistry-Paraffin: PTH1R/PTHR1 Antibody (3D1.1) [NBP1-40067] - Analysis of anti-PTH1R antibody with human liver at concentration 5 ug/ml.](http://images.novusbio.com/fullsize/PTH1R-PTHR1-Antibody-3D1-1-Immunohistochemistry-Paraffin-NBP1-40067-img0001.jpg)
![Immunohistochemistry: PTH1R/PTHR1 Antibody (3D1.1) [NBP1-40067] - Immunofluorescence for PTH1R in the labyrinth of wild type and Ramp2-/- placentas. Scale bars, 100 um. Image collected and cropped by CiteAb from the following publication (dx.plos.org/10.1371/journal.pone.0181597), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/PTH1R-PTHR1-Antibody-3D1-1-Immunohistochemistry-NBP1-40067-img0002.jpg)
![Cellular localization of OS-9 and PHD2.(A) A lectin gel-shift assay was conducted to test for glycosylated proteins. Total cell lysates of U2OS cells were incubated in the presence or absence of the endoglycosidases EndoH and PNGaseF for 6 h at 37°C. Digest products were separated on a reducing 10% SDS-PAGE gel which contained concanavalin A co-polymerized in the top layer of the separating gel to retard mobility of glycosylated proteins [56]. Glycosylated OS-9 is indicated as ‘g’, deglycosylated OS-9 as ‘d’. (B) Detection of OS-9 and PHD2 in the nuclear fraction. HEK293 cells with and without transfection of the plasmid pcDNA3-OS-9 were separated into nuclear fraction (N) and postnuclear supernatant (PS), the latter containing cytoplasm and organelles. Western blot analysis included BiP, GAPDH and lamin A as typical marker proteins for the ER, the cytoplasm and the nucleus, respectively. (C) Detection of OS-9 and PHD2 in the cytoplasm. HEK293 cells were co-transfected with pcDNA3-OS-9 and pPHD2-V5. For hypoxia, cells were exposed to 3% O2 for 4 h. Cells were treated with 50 µg/ml digitonin and centrifuged to obtain a cytoplasmic (C) and an organelle fraction (O) and subjected to immunoblotting. (D) Isolation of cellular endomembranes. HEK293 cells were lysed mechanically by several passages through a 30½G needle. The postnuclear supernatant was processed further by ultra-centrifugation to separate the organelles (O) from the cytosol (C). High salt treatment (1 M KCl) of the organelle fraction produced a wash fraction (W) that contained dissociated peripheral membrane proteins. For immunoblot analysis of subcellular fractionations, cell aliquots were normalized for cell number prior to loading (B–D). Representative Western blots are shown for each subfigure. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/21559462), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-40067_mouse-pth1r-pthr1-mab-3d1-1-23220248131978.jpg)
