Human Cadherin-11 APC-conjugated Antibody Summary
-17, rhE-Cadherin, rhN-Cadherin, rhP-Cadherin, or rhVE-Cadherin is observed.
Phe23-Thr617
Accession # AAA35622
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
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Detection of Cadherin‑11 in PC‑3 Human Cell Line by Flow Cytometry. PC-3 human prostate cancer cell line was stained with Mouse Anti-Human Cadherin-11 APC-conjugated Monoclonal Antibody (Catalog # FAB17901A, filled histogram) or isotype control antibody (Catalog # IC003A, open histogram). Cells were stained in a buffer containing Ca2+and Mg2+. View our protocol for Staining Membrane-associated Proteins.
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Preparation and Storage
- 12 months from date of receipt, 2 to 8 °C as supplied.
Background: Cadherin-11
Cadherin-11, also known as OB-Cadherin, is a 120 kDa member of the classical Cadherin family of calcium-dependent homophilic adhesion proteins. Cadherins are involved in multiple processes including embryonic development, cell migration, and maintenance of epithelial integrity (1). Cadherin-11 is expressed in embryonic mesodermal tissues and contributes to the morphogenesis of the nervous and skeletal systems (2-4). It is expressed on osteoblasts in the adult where it promotes the differentiation of both osteoblasts and chondrocytes (5). Cadherin-11 is up‑regulated on breast cancer and prostate cancer cells which preferentially metastasize to bone (6, 7). It facilitates this metastasis via homophilic adhesion to bone marrow stroma and osteoblast-expressed Cadherin-11 (6‑8). In the synovium, Cadherin‑11 supports adhesion between synoviocytes but promotes cell invasion in synovitis and rheumatoid arthritis (9, 10). Its up‑regulation in the vasculature following injury contributes to intimal hyperplasia by inducing smooth muscle cell migration and proliferation (11). In the nervous system, Cadherin-11 interacts with FGF R1 to promote neurite extension from spinal cord explants (12). Mature human Cadherin‑11 consists of a 564 amino acid (aa) extracellular domain (ECD) with five tandem Cadherin repeats, a 23 aa transmembrane segment, and a 156 aa cytoplasmic domain (13, 14). Within the ECD, human Cadherin-11 shares 97% and 98% aa sequence identity with mouse and rat Cadherin‑11, respectively. An 80 kDa portion of the Cadherin‑11 ECD can be shed by proteolytic cleavage, and this fragment competes with the full length molecule for cell adhesion (3, 15). Alternate splicing of human Cadherin-11 generates an 85 kDa isoform with substituted transmembrane and cytoplasmic regions (14, 15).
- Pokutta, S. and W.I. Weis (2007) Annu. Rev. Cell Dev. Biol. 23:237.
- Kimura, Y. et al. (1995) Dev. Biol. 169:347.
- McCusker, C. et al. (2009) Mol. Biol. Cell 20:78.
- Clendenon, S.G. et al. (2009) Dev. Dyn. 238:1909.
- Kii, I. et al. (2004) J. Bone Mineral Res. 19:1840.
- Tamura, D. et al. (2008) Int. J. Oncol. 33:17.
- Chu, K. et al. (2008) Mol. Cancer Res. 6:1259.
- Huang, C.-F. et al. (2010) Cancer Res. 70:4580.
- Valencia, X. et al. (2004) J. Exp. Med. 200:1673.
- Kiener, H.P. et al. (2009) Arthritis Rheum. 60:1305.
- Monahan, T.S. et al. (2007) J. Vasc. Surg. 45:581.
- Boscher, C. and R.-M. Mege (2008) Cell. Signal. 20:1061.
- Tanihara, H. et al. (1994) Cell Adhes. Commun. 2:15.
- Okazaki, M. et al. (1994) J. Biol. Chem. 269:12092.
- Kawaguchi, J. et al. (1999) J. Bone Mineral Res. 14:764.
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