| Reactivity | HuSpecies Glossary |
| Applications | Bioactivity |
| Format | Carrier-Free |
| Details of Functionality | Measured by the ability of the immobilized protein to support the adhesion of Caki‑2 human clear cell carcinoma epithelial cells. When 5 x 104 cells/well are added to Recombinant Human Pro-Cadherin‑12 Fc Chimera coated plates (5 µg/mL with 100 µL/well), approximately >30% will adhere after 30 minutes at 37 °C. Optimal concentration depends on cell type as well as the application or research objectives. |
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| Source | Mouse myeloma cell line, NS0-derived human Cadherin-12 protein
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| N-terminal Sequence | No results obtained: Gln24 predicted |
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| Structure / Form | Disulfide-linked homodimer |
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| Protein/Peptide Type | Recombinant Proteins |
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| Gene | CDH12 |
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| Purity | >90%, by SDS-PAGE under reducing conditions and visualized by silver stain |
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| Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
| Dilutions |
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| Theoretical MW | 92.5 kDa (monomer). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
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| SDS-PAGE | 115 kDa, reducing conditions |
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| Publications |
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| Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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| Buffer | Lyophilized from a 0.2 μm filtered solution in Tris-Citrate, NaCl and CaCl2. |
| Purity | >90%, by SDS-PAGE under reducing conditions and visualized by silver stain |
| Reconstitution Instructions | Reconstitute at 100 μg/mL in sterile PBS. |
The cadherin superfamily is a large family of membrane-associated glycoproteins that engage in homotypic, calcium-dependent, cell-cell adhesion events. The superfamily can be divided into at least four subfamilies based on its member’s extracellular (EC) regions and cytoplasmic domains (1, 2). These include classical cadherins, desmosomal cadherins, protocadherins, and cadherin-like molecules that contain a variable number of EC and transmembrane (TM) domains (1). Cadherin-12, also known as brain‑cadherin and N-cadherin 2, is a 150 kDa classical cadherin. Classical family molecules are modular in their extracellular region, mediating calcium‑dependent cell-cell adhesion through their five EC Ca++-binding repeats (2). Cadherin-12 can be further identified as a type II classical cadherin, due to the absence of a His-Ala-Val motif in its most N-terminal cadherin repeat (3). Human Cadherin-12 is synthesized as a 794 amino acid (aa) type I transmembrane preproprotein that contains a 23 aa signal peptide, a 31 aa prosequence, a 555 aa extracellular region, a 28 aa transmembrane segment, and a 157 aa cytoplasmic domain (4, 5). The five EC cadherin domains are approximately 110 aa in length and generate two beta -sheets that are oriented like bread in a sandwich. Human Cadherin‑12 EC region is 96% aa identical to mouse Cadherin-12 EC region. Cadherin-12 is expressed specifically in CNS neurons. The bulk of its expression is postnatal, and it is proposed to be involved in synaptogenesis (4). As a classic cadherin, Cadherin-12 will form homodimers and promote intercellular adhesion with itself and, possibly, cadherins-8 and -14 (6).
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