| Reactivity | HuSpecies Glossary |
| Applications | Bioactivity |
| Format | Carrier-Free |
| Details of Functionality | Measured by the ability of the immobilized protein to support the adhesion of C2C12 mouse myoblast cells stimulated for 36 hours with 10% equine serum. When 3 x 104 cells/well are added to rhM-CAD/Fc Chimera coated plates (6 µg/mL, 100 µL/well), approximately 35-60% will adhere after 1 hour 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 M-Cadherin/Cadherin-15 protein
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| Accession # | |||||||
| N-terminal Sequence | Val22 |
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| Structure / Form | Disulfide-linked homodimer |
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| Protein/Peptide Type | Recombinant Proteins |
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| Gene | CDH15 |
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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 | 90.5 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 | 122 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 MES, 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. |
M-Cadherin (M-CAD or Cadherin-15) is a 124 kDa type I transmembrane glycoprotein of the Cadherin superfamily of calcium-dependent homotypic adhesion molecules (1 - 4). Like other classical Cadherins, the 814 amino acid (aa) human M-CAD contains a signal sequence (21 aa), a propeptide (29 aa), an extracellular domain with five Cadherin domain repeats (ECD, 556 aa), a transmembrane segment (20 aa) and a cytoplasmic domain (188 aa) (1). A splice variant that diverges within the third Cadherin repeat has been sequenced. The Cadherin repeats are responsible for cell-cell adhesion by homophilic binding on opposing cells (1 - 4). Intracellularly, M-CAD binds beta -catenin or plakoglobin ( gamma -catenin), which in turn bind alpha -catenin (4). M-CAD also binds p120 catenin (5). Connection of Cadherin/catenin complexes to the actin cytoskeleton is in question, but is possible through a linker (6). Connection to microtubules has been shown (7). M-CAD is present during early stages of skeletal muscle development and is thought to align myoblasts for fusion (8). It is also present in muscle satellite cells and participates in muscle regeneration (9). M-CAD is also expressed in the granule cell layer of the cerebellar glomerulus (10). Deletion of mouse M-CAD has little effect in vivo, most likely due to compensation by N-Cadherin (11). However, M-CAD upregulation and adhesion between myoblasts during induction of differentiation in vitro is required for their fusion (8, 12, 13). M-CAD activity is later downregulated by sequestering to caveoli, p120 catenin/RhoA-induced ubiquitination and/or cleavage by calpain-3. This terminates fusion and allows sarcomere formation (5, 12, 13). Human M-CAD ECD shows 88% aa identity with mouse, rat or bovine, and 85% aa identity with canine M-CAD ECD. M-CAD is an outlier among classical Cadherins, with 40% aa identity or less in the ECD (4).
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