Reactivity | MuSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Details of Functionality | Measured by the ability of the immobilized protein to support the adhesion of A172 human glioblastoma cells (ATCC: CRL-1620). When 5 x 104 cells/well are added to Recombinant Mouse Cadherin‑4/R‑Cadherin coated plates, cell adhesion is enhanced in a dose dependent manner after 90 minutes at 37 °C. The ED50 for this effect is 0.4-2.0 μg/mL. |
Source | Mouse myeloma cell line, NS0-derived mouse Cadherin-4/R-Cadherin protein Met1-Ala731 with a C-terminal 6-His tag |
Accession # | |
N-terminal Sequence | His21 & Asp167 |
Protein/Peptide Type | Recombinant Proteins |
Gene | Cdh4 |
Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Endotoxin Note | <0.01 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 78.5 & 62.5 kDa. 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 | 99 & 84 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 PBS. |
Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Reconstitution Instructions | Reconstitute at 400 μg/mL in PBS. |
Cadherin‑4, also known as R‑Cadherin, is a 120‑140 kDa type I transmembrane protein belonging to the 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). Mouse Cadherin‑4 is synthesized with a 20 amino acid (aa) signal peptide and a 146 aa N‑terminal propeptide. The mature cell surface‑expressed protein consists of a 565 amino acid (aa) extracellular domain (ECD) that contains five Cadherin repeats, a 22 aa transmembrane segment, and a 160 aa cytoplasmic domain (3, 4). Within the propeptide and ECD, mouse Cadherin‑4 shares 92% and 98% aa sequence identity with human and rat Cadherin‑4, respectively. Cadherin‑4 is expressed in epithelial cells, vascular smooth muscle cells, glial and neuronal cells, pancreatic beta ‑cells, thyroid follicular cells, and bone marrow Lin‑ hematopoietic stem cells (4 ‑ 10). It interacts in cis to form homodimers as well as heterodimers with N‑Cadherin which function as adhesion multimers in trans-configuration (3, 11, 12). It is down‑regulated in invasive breast cancer but up‑regulated in rhabdomyosarcoma and has been shown to exert both positive and negative effects on cell migration and tumor cell invasiveness (5, 13, 14). Cadherin‑4 is involved in a variety of homing processes including guidance of the optic nerve and pioneer axons in early brain development, branching and guidance of the retinal vasculature, and targeting of hematopoietic stem cells to sites of ischemia (7, 10, 15, 16). Cadherin‑4 additionally binds to KLRG1, an inhibitory receptor expressed on NK cells (17).
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