Recombinant Mouse Cadherin-11 Fc Chimera Protein, CF Summary
Product Specifications
Optimal dilutions should be determined by each laboratory for each application.
| Mouse Cadherin-11 (Met1 - Thr617) Accession # P55288 |
IEGRMDP | Mouse IgG2A (Glu98 - Lys330) |
| N-terminus | C-terminus | |
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
6627-CA
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
| Reconstitution | Reconstitute at 100 μg/mL in PBS. |
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Reconstitution Calculator
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 ‑ 5). It is expressed on osteoblasts in the adult where it promotes the differentiation of both osteoblasts and chondrocytes (6). Cadherin-11 is up‑regulated on breast cancer and prostate cancer cells which preferentially metastasize to bone (7, 8). It facilitates this metastasis via homophilic adhesion to bone marrow stroma and osteoblast-expressed Cadherin-11 (7 ‑ 9). In the synovium, Cadherin-11 supports adhesion between synoviocytes but promotes cell invasion in synovitis and rheumatoid arthritis (10, 11). Its up‑regulation in the vasculature following injury contributes to intimal hyperplasia by inducing smooth muscle cell migration and proliferation (12). In the nervous system, Cadherin-11 interacts with FGF R1 to promote neurite extension from spinal cord explants (13). Mature mouse 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 (2, 3, 14). Within the ECD, mouse Cadherin-11 shares 97% and 98% aa sequence identity with human 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 (4, 15).
- Pokutta, S. and W.I. Weis (2007) Annu. Rev. Cell Dev. Biol. 23:237.
- Kimura, Y. et al. (1995) Dev. Biol. 169:347.
- Hoffmann, I. and R. Balling (1995) Dev. Biol. 169:337.
- 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.
- Okazaki, M. et al. (1994) J. Biol. Chem. 269:12092.
- Kawaguchi, J. et al. (1999) J. Bone Mineral Res. 14:764.
Citation for Recombinant Mouse Cadherin-11 Fc Chimera Protein, CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
1 Citation: Showing 1 - 1
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Secretomics reveals gelatinase substrates at the blood-brain barrier that are implicated in astroglial barrier function
Authors: Burmeister, M;Fraunenstein, A;Kahms, M;Arends, L;Gerwien, H;Deshpande, T;Kuhlmann, T;Gross, CC;Naik, VN;Wiendl, H;Klingauf, J;Meissner, F;Sorokin, L;
Science advances
Species: Mouse
Sample Types: Recombinant Protein
Applications: Bioassay
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