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InVivoMAb anti-human N-cadherin (CD325)

Clone	Catalog #	Category
8C11	BE0184	InVivoMab Antibodies

$95 - $3250

SDS Sheet

About InVivoMAb anti-human N-cadherin (CD325)

The 8C11 monoclonal antibody reacts with human N-Cadherin, also known as CD325. N-Cadherin is a 130 kDa transmembrane protein and a member of the Cadherin superfamily. N-cadherin is expressed by stem cells, myeloblasts, endothelial cells, and fibroblasts as well as in neural and muscle tissues. N-cadherin is involved in organ development during gastrulation and is required for establishment of left-right asymmetry. N-cadherin is also thought to provide a mechanism for transendothelial migration of cancer cells thus promoting metastasis.

InVivoMAb anti-human N-cadherin (CD325) Specifications

Isotype	Mouse IgG1, κ
Recommended Isotype Control(s)	InVivoMAb mouse IgG1 isotype control, unknown specificity(BE0083)
Recommended InVivoPure Dilution Buffer	InVivoPure pH 7.0 Dilution Buffer(IP0070)
Immunogen	Recombinant human N-cadherin extracellular domain
Reported Applications	Western blot Immunofluorescence Flow cytometry
Endotoxin	<2EU/mg (<0.002EU/μg) Determined by LAL gel clotting assay
Purity	>95% Determined by SDS-PAGE
Formulation	PBS, pH 7.0 Contains no stabilizers or preservatives
Sterility	0.2 μM filtered
Production	Purified from tissue culture supernatant in an animal free facility
Purification	Protein G
Storage	The antibody solution should be stored undiluted at 4°C, and protected from prolonged exposure to light. Do not freeze.
RRID	AB_10950101
Molecular Weight	150 kDa

References provided by Bioz:

Disclaimer: These articles are provided by Bioz, an automated third-party article search engine. Given Bioz’s automation, these articles may not reflect the reported applications listed for this product. For an extensive up-to-date article list directly tailored to the reported applications listed for this product please see the Bio X Cell Application References by clicking the green button above.

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InVivoMAb anti-human N-cadherin (CD325) (Clone: 8C11)

Cai, X., et al. (2014). "Autonomous stimulation of cancer cell plasticity by the human NKG2D lymphocyte receptor coexpressed with its ligands on cancer cells." PLoS One 9(10): e108942. PubMed

The stimulatory NKG2D receptor on lymphocytes promotes tumor immune surveillance by targeting ligands selectively induced on cancer cells. Progressing tumors counteract by employing tactics to disable lymphocyte NKG2D. This negative dynamic is escalated as some human cancer cells co-opt expression of NKG2D, thereby complementing the presence of its ligands for autonomous stimulation of oncogenic signaling. Clinical association data imply relationships between cancer cell NKG2D and metastatic disease. Here we show that NKG2D promotes cancer cell plasticity by induction of phenotypic, molecular, and functional signatures diagnostic of the epithelial-mesenchymal transition, and of stem-like traits via induction of Sox9, a key transcriptional regulator of breast stem cell maintenance. These findings obtained with model breast tumor lines and xenotransplants were recapitulated by ex vivo cancer cells from primary invasive breast carcinomas. Thus, NKG2D may have the capacity to drive high malignancy traits underlying metastatic disease.

Karayannis, T., et al. (2014). "Cntnap4 differentially contributes to GABAergic and dopaminergic synaptic transmission." Nature 511(7508): 236-240. PubMed

Although considerable evidence suggests that the chemical synapse is a lynchpin underlying affective disorders, how molecular insults differentially affect specific synaptic connections remains poorly understood. For instance, Neurexin 1a and 2 (NRXN1 and NRXN2) and CNTNAP2 (also known as CASPR2), all members of the neurexin superfamily of transmembrane molecules, have been implicated in neuropsychiatric disorders. However, their loss leads to deficits that have been best characterized with regard to their effect on excitatory cells. Notably, other disease-associated genes such as BDNF and ERBB4 implicate specific interneuron synapses in psychiatric disorders. Consistent with this, cortical interneuron dysfunction has been linked to epilepsy, schizophrenia and autism. Using a microarray screen that focused upon synapse-associated molecules, we identified Cntnap4 (contactin associated protein-like 4, also known as Caspr4) as highly enriched in developing murine interneurons. In this study we show that Cntnap4 is localized presynaptically and its loss leads to a reduction in the output of cortical parvalbumin (PV)-positive GABAergic (gamma-aminobutyric acid producing) basket cells. Paradoxically, the loss of Cntnap4 augments midbrain dopaminergic release in the nucleus accumbens. In Cntnap4 mutant mice, synaptic defects in these disease-relevant neuronal populations are mirrored by sensory-motor gating and grooming endophenotypes; these symptoms could be pharmacologically reversed, providing promise for therapeutic intervention in psychiatric disorders.

Nozaki, K., et al. (2014). "DDX3X induces primary EGFR-TKI resistance based on intratumor heterogeneity in lung cancer cells harboring EGFR-activating mutations." PLoS One 9(10): e111019. PubMed

The specific mechanisms how lung cancer cells harboring epidermal growth factor receptor (EGFR) activating mutations can survive treatment with EGFR-tyrosine kinase inhibitors (TKIs) until they eventually acquire treatment-resistance genetic mutations are unclear. The phenotypic diversity of cancer cells caused by genetic or epigenetic alterations (intratumor heterogeneity) confers treatment failure and may foster tumor evolution through Darwinian selection. Recently, we found DDX3X as the protein that was preferentially expressed in murine melanoma with cancer stem cell (CSC)-like phenotypes by proteome analysis. In this study, we transfected PC9, human lung cancer cells harboring EGFR exon19 deletion, with cDNA encoding DDX3X and found that DDX3X, an ATP-dependent RNA helicase, induced CSC-like phenotypes and the epithelial-mesenchymal transition (EMT) accompanied with loss of sensitivity to EGFR-TKI. DDX3X expression was associated with upregulation of Sox2 and increase of cancer cells exhibiting CSC-like phenotypes, such as anchorage-independent proliferation, strong expression of CD44, and aldehyde dehydrogenase (ALDH). The EMT with switching from E-cadherin to N-cadherin was also facilitated by DDX3X. Either ligand-independent or ligand-induced EGFR phosphorylation was inhibited in lung cancer cells that strongly expressed DDX3X. Lack of EGFR signal addiction resulted in resistance to EGFR-TKI. Moreover, we found a small nonadherent subpopulation that strongly expressed DDX3X accompanied by the same stem cell-like properties and the EMT in parental PC9 cells. The unique subpopulation lacked EGFR signaling and was highly resistant to EGFR-TKI. In conclusion, our data indicate that DDX3X may play a critical role for inducing phenotypic diversity, and that treatment targeting DDX3X may overcome primary resistance to EGFR-TKI resulting from intratumor heterogeneity.

Abba, M., et al. (2013). "Unraveling the role of FOXQ1 in colorectal cancer metastasis." Mol Cancer Res 11(9): 1017-1028. PubMed

Malignant cell transformation, invasion, and metastasis are dependent on the coordinated rewiring of gene expression. A major component in the scaffold of these reprogramming events is one in which epithelial cells lose intercellular connections and polarity to adopt a more motile mesenchymal phenotype, which is largely supported by a robust transcriptional machinery consisting mostly of developmental transcription factors. This study demonstrates that the winged helix transcription factor, FOXQ1, contributes to this rewiring process, in part by directly modulating the transcription of TWIST1, itself a key mediator of metastasis that transcriptionally regulates the expression of important molecules involved in epithelial-to-mesenchymal transition. Forced expression and RNA-mediated silencing of FOXQ1 led to enhanced and suppressed mRNA and protein levels of TWIST1, respectively. Mechanistically, FOXQ1 enhanced the reporter activity of TWIST1 and directly interacted with its promoter. Furthermore, enhanced expression of FOXQ1 resulted in increased migration and invasion in colorectal cancer cell lines, whereas knockdown studies showed the opposite effect. Moreover, using the in vivo chicken chorioallantoic membrane metastasis assay model, FOXQ1 significantly enhanced distant metastasis with minimal effects on tumor growth. IMPLICATIONS: These findings reveal FOXQ1 as a modulator of TWIST1-mediated metastatic phenotypes and support its potential as a biomarker of metastasis.

Cui, Y. and S. Yamada (2013). "N-cadherin dependent collective cell invasion of prostate cancer cells is regulated by the N-terminus of alpha-catenin." PLoS One 8(1): e55069. PubMed

Cancer cell invasion is the critical first step of metastasis, yet, little is known about how cancer cells invade and initiate metastasis in a complex extracellular matrix. Using a cell line from bone metastasis of prostate cancer (PC3), we analyzed how prostate cancer cells migrate in a physiologically relevant 3D Matrigel. We found that PC3 cells migrated more efficiently as multi-cellular clusters than isolated single cells, suggesting that the presence of cell-cell adhesion improves 3D cell migration. Perturbation of N-cadherin function by transfection of either the N-cadherin cytoplasmic domain or shRNA specific to N-cadherin abolished collective cell migration. Interestingly, PC3 cells do not express alpha-catenin, an actin binding protein in the cadherin complex. When the full-length alpha-catenin was re-introduced, the phenotype of PC3 cells reverted back to a more epithelial phenotype with a decreased cell migration rate in 3D Matrigel. Interestingly, we found that the N-terminal half of alpha-catenin was sufficient to suppress invasive phenotype. Taken together, these data suggest that the formation of N-cadherin junctions promotes 3D cell migration of prostate cancer cells, and this is partly due to an aberrant regulation of the N-cadherin complex in the absence of alpha-catenin.

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