Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Activity
Measured by the ability of the immobilized protein to support the adhesion of Caki‑2 human clear cell carcinoma epithelial cells. When 5 x 10 4 cells/well are added to Recombinant Human Cadherin-6 Fc Chimera coated plates (5 µg/mL with 100 µL/well), >30% of cells will adhere after 30 minutes at 37° C.
Optimal concentration depends on cell type as well as the application or research objectives.Source
Mouse myeloma cell line, NS0-derived
Human Cadherin-6
(Thr22 - Ala615 & Ser54 - Ala615)
Accession # P55285IEGRMD Human IgG1
(Pro100 - Lys330)6-His tag N-terminus C-terminus Accession #
N-terminal Sequence
AnalysisThr22 & Ser54
Structure / Form
Disulfide-linked homodimer
Predicted Molecular Mass
93.7 kDa (pro), 90 kDa (mature)
SDS-PAGE
120-140 kDa, reducing conditions
2715-CA |
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Formulation Lyophilized from a 0.2 μm filtered solution in PBS. | ||
Reconstitution Reconstitute at 100 μg/mL in sterile 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.
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Background: Cadherin-6/KCAD
Cadherin-6, also known as KCAD or K-Cadherin, is a 110 - 120 kDa type I transmembrane glycoprotein belonging to the classical Cadherin superfamily of calcium-dependent adhesion molecules. Cadherins are involved in multiple processes including embryonic development, cell migration, and maintenance of epithelial integrity (1, 2). Human Cadherin-6 is synthesized with an 18 amino acid (aa) signal peptide and a 35 aa N-terminal propeptide. The mature cell surface-expressed protein consists of a 562 amino acid (aa) extracellular domain (ECD) that contains five tandem Cadherin repeats, a 21 aa transmembrane segment, and a 154 aa cytoplasmic domain (3). Within the ECD, human Cadherin-6 shares 96% and 98% aa sequence identity with mouse and rat Cadherin-10, respectively. Alternate splicing of the human Cadherin-6 mRNA generates additional isoforms with deletions in the extracellular region or a substituted and truncated cytoplasmic domain (4). It interacts homotypically as well as heterotypically with Cadherin-9 and more weakly with Cadherins-7, -10, and -14 (5, 6). Cadherin-6 is expressed primarily in the kidney and brain, both during development and in the adult (3, 7 - 9). It is enriched in renal proximal tubule epithelial cells and their precursors at sites of cell-cell contact as well as on basolateral membranes (8, 10, 11). In the nervous system, Cadherin-6 is neuronally expressed in discrete regions of the neural plate, neural crest cells that give rise to peripheral nerves, and the brain (7, 12). Cadherin-6 is additionally expressed in the developing retina, osteoclasts and their progenitors, ovarian epithelium, and endometrium during the follicular phase of the menstrual cycle (4, 13 ‑ 15). It is also expressed in carcinomas of the kidney, ovary, and liver (3, 10, 11, 14).
References:
Pokutta, S. and W.I. Weis (2007) Annu. Rev. Cell Dev. Biol. 23:237.
Gumbiner, B.M. (2005) Nat. Rev. Mol. Cell Biol. 6:622.
Shimoyama, Y. et al. (1995) Cancer Res. 55:2206.
Mbalaviele, G. et al. (1998) J. Cell Biol. 141:1467.
Shimoyama, Y. et al. (2000) Biochem. J. 349:159.
Shimoyama, Y. et al. (1999) J. Biol. Chem. 274:11987.
Inoue, T. et al. (1998) Dev. Dyn. 211:338.
Xiang Y.-Y. et al. (1994) Cancer Res. 54:3034.
Cho, E.A. et al. (1998) Development 125:803.
Paul, R. et al. (1997) Cancer Res. 57:2741.
Shimazui, T. et al. (2000) Eur. Urol. 38:331.
Inoue, T. et al. (1997) Dev. Biol. 183:183.
Ruan, G. et al. (2006) Mech. Dev. 123:881.
Sellar, G.C. et al. (2001) Cancer Res. 61:6977.
Getsios, S. et al. (1998) Dev. Dyn. 211:238.
Entrez Gene IDs:
1004 (Human)
Alternate Names:
cadherin 6, type 2, K-cadherin (fetal kidney); cadherin, fetal kidney; Cadherin6; Cadherin-6; CDH6; KCAD; K-cadherin (fetal kidney); K-Cadherin
