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Rabbit Anti-N Cadherin Polyclonal Antibody, Unconjugated


Antibody ID


Target Antigen

N Cadherin mouse, rat, reacts with human, mouse, rat and xenopus laevisnot yet tested in other speciespredicted to react with chicken (95 identity with immunogen) and cow (95 identity with immunogen) due to sequence homology

Proper Citation

(Abcam Cat# ab18203, RRID:AB_444317)


polyclonal antibody


validation status unknown, seller recommendations provided in 2012: Immunocytochemistry; Immunofluorescence; Western Blot; Flow Cytometry, Immunocytochemistry/Immunofluorescence, Immunohistochemistry-Fr, Immunohistochemistry-P, Western Blot

Host Organism




Cat Num


Publications that use this research resource

Highly multiplexed immunofluorescence imaging of human tissues and tumors using t-CyCIF and conventional optical microscopes.

  • Lin JR
  • Elife
  • 2018 Jul 11

Literature context:


The architecture of normal and diseased tissues strongly influences the development and progression of disease as well as responsiveness and resistance to therapy. We describe a tissue-based cyclic immunofluorescence (t-CyCIF) method for highly multiplexed immuno-fluorescence imaging of formalin-fixed, paraffin-embedded (FFPE) specimens mounted on glass slides, the most widely used specimens for histopathological diagnosis of cancer and other diseases. t-CyCIF generates up to 60-plex images using an iterative process (a cycle) in which conventional low-plex fluorescence images are repeatedly collected from the same sample and then assembled into a high dimensional representation. t-CyCIF requires no specialized instruments or reagents and is compatible with super-resolution imaging; we demonstrate its application to quantifying signal transduction cascades, tumor antigens and immune markers in diverse tissues and tumors. The simplicity and adaptability of t-CyCIF makes it an effective method for pre-clinical and clinical research and a natural complement to single-cell genomics.

Funding information:
  • Biotechnology and Biological Sciences Research Council - BB/G006474/2(United Kingdom)
  • Dana-Farber/Harvard Cancer Center - Claudia Adams Barr Program()
  • Dana-Farber/Harvard Cancer Center - GI SPORE Developmental Research Project Award()
  • National Institutes of Health - K08CA222663()
  • National Institutes of Health - P50GM107618()
  • National Institutes of Health - R41-CA224503()
  • National Institutes of Health - U54HL127365()

Visceral endoderm and the primitive streak interact to build the fetal-placental interface of the mouse gastrula.

  • Rodriguez AM
  • Dev. Biol.
  • 2017 Dec 1

Literature context:


Hypoblast/visceral endoderm assists in amniote nutrition, axial positioning and formation of the gut. Here, we provide evidence, currently limited to humans and non-human primates, that hypoblast is a purveyor of extraembryonic mesoderm in the mouse gastrula. Fate mapping a unique segment of axial extraembryonic visceral endoderm associated with the allantoic component of the primitive streak, and referred to as the "AX", revealed that visceral endoderm supplies the placentae with extraembryonic mesoderm. Exfoliation of the AX was dependent upon contact with the primitive streak, which modulated Hedgehog signaling. Resolution of the AX's epithelial-to-mesenchymal transition (EMT) by Hedgehog shaped the allantois into its characteristic projectile and individualized placental arterial vessels. A unique border cell separated the delaminating AX from the yolk sac blood islands which, situated beyond the limit of the streak, were not formed by an EMT. Over time, the AX became the hindgut lip, which contributed extensively to the posterior interface, including both embryonic and extraembryonic tissues. The AX, in turn, imparted antero-posterior (A-P) polarity on the primitive streak and promoted its elongation and differentiation into definitive endoderm. Results of heterotopic grafting supported mutually interactive functions of the AX and primitive streak, showing that together, they self-organized into a complete version of the fetal-placental interface, forming an elongated structure that exhibited A-P polarity and was composed of the allantois, an AX-derived rod-like axial extension reminiscent of the embryonic notochord, the placental arterial vasculature and visceral endoderm/hindgut.

Multiple roles of afadin in the ultrastructural morphogenesis of mouse hippocampal mossy fiber synapses.

  • Sai K
  • J. Comp. Neurol.
  • 2017 Aug 15

Literature context:


A hippocampal mossy fiber synapse, which is implicated in learning and memory, has a complex structure in which mossy fiber boutons attach to the dendritic shaft by puncta adherentia junctions (PAJs) and wrap around a multiply-branched spine, forming synaptic junctions. Here, we electron microscopically analyzed the ultrastructure of this synapse in afadin-deficient mice. Transmission electron microscopy analysis revealed that typical PAJs with prominent symmetrical plasma membrane darkening undercoated with the thick filamentous cytoskeleton were observed in the control synapse, whereas in the afadin-deficient synapse, atypical PAJs with the symmetrical plasma membrane darkening, which was much less in thickness and darkness than those of the control typical PAJs, were observed. Immunoelectron microscopy analysis revealed that nectin-1, nectin-3, and N-cadherin were localized at the control typical PAJs, whereas nectin-1 and nectin-3 were localized at the afadin-deficient atypical PAJs to extents lower than those in the control synapse and N-cadherin was localized at their nonjunctional flanking regions. These results indicate that the atypical PAJs are formed by nectin-1 and nectin-3 independently of afadin and N-cadherin and that the typical PAJs are formed by afadin and N-cadherin cooperatively with nectin-1 and nectin-3. Serial block face-scanning electron microscopy analysis revealed that the complexity of postsynaptic spines and mossy fiber boutons, the number of spine heads, the area of postsynaptic densities, and the density of synaptic vesicles docked to active zones were decreased in the afadin-deficient synapse. These results indicate that afadin plays multiple roles in the complex ultrastructural morphogenesis of hippocampal mossy fiber synapses.

Aberrant TGF-β Signaling Drives Castration-Resistant Prostate Cancer in a Male Mouse Model of Prostate Tumorigenesis.

  • Pu H
  • Endocrinology
  • 2017 Jun 1

Literature context:


The androgen receptor (AR) plays a critical role as a driver of castration-resistant prostate cancer (CRPC). Our previous studies demonstrated that disruption of transforming growth factor-β (TGF-β) signaling via introduction of dominant-negative transforming growth factor-β type II receptor (DNTGFβRII) in the prostate epithelium of transgenic adenocarcinoma of the prostate mice accelerated tumor. This study investigated the consequences of disrupted TGF-β signaling on prostate tumor growth under conditions of castration-induced androgen deprivation in the preclinical model of DNTGFβRII. Our results indicate that in response to androgen deprivation therapy (ADT) the proliferative index in prostate tumors from DNTGFβRII mice was higher compared with prostate tumors from TGFβRII wild-type (WT) mice, whereas there was a reduced incidence of apoptosis in tumors from DNTGFβRII. Protein and gene expression profiling revealed that tumors from DNTGFβRII mice exhibit a strong nuclear AR localization among the prostate tumor epithelial cells and increased AR messenger RNA after ADT. In contrast, TGFβRII WT mice exhibited a marked loss in nuclear AR in prostate tumor acini (20 weeks), followed by a downregulation of AR and transmembrane protease serine 2 messenger RNA. There was a significant increase in nuclear AR and activity in prostate tumors from castrate DNTGFβRII compared with TGFβRII WT mice. Consequential to aberrant TGF-β signaling, ADT enhanced expression and nuclear localization of Smad4 and β-catenin. Our findings support that under castrate conditions, aberrant TGF-β signaling leads to AR activation and β-catenin nuclear localization, an adaptation mechanism contributing to emergence of CRPC. The work defines a potentially significant new targeting platform for overcoming therapeutic resistance in CRPC.

Funding information:
  • NIDDK NIH HHS - R01 DK083761()