Reactivity | MuSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Details of Functionality | Measured by the ability of the immobilized protein to support the adhesion of human neutrophils. When 2 x 105 cells/well are added to CXADR-coated plates (10 µg/mL, 100 µL/well), approximately 40‑60% of the cells will adhere after 20 minutes at 37° C. |
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Source | Mouse myeloma cell line, NS0-derived mouse CXADR protein
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Accession # | |||||||
N-terminal Sequence | Leu20 |
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Structure / Form | Disulfide-linked homodimer |
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Protein/Peptide Type | Recombinant Proteins |
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Gene | Cxadr |
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Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
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Endotoxin Note | <0.01 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 51.2 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 | 61-65 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 100 μg/mL in sterile PBS. |
CXADR (coxsackie and adenovirus receptor), also known as CAR, is a 46 kDa type I transmembrane glycoprotein that belongs to the CTX family of the Ig superfamily (1 - 3). CXADR has received attention as a receptor that facilitates gene transfer mediated by most adenoviruses (1, 2). It is also an adhesion molecule within junctional complexes, notably between epithelial cells lining body cavities and within myocardial intercalated discs (1, 2, 4). CXADR is essential for normal cardiac development in the mouse (7). It is expressed throughout brain neuroepithelium during development, but mainly in ependymal cells in the adult (4 - 6). The 365 amino acid (aa) mouse CXADR contains a 19 aa signal sequence, a 218 aa extracellular domain (ECD) with a V-type (D1) and a C2-type (D2) Ig-like domain, a 21 aa transmembrane segment and a 107 aa intracellular domain. D1 is thought to be responsible for homodimer formation in trans within tight junctions (2). The fiber knob of adenoviruses attaches at a similar site, and evidence suggests that disruption of tight junctions facilitates virus binding (1, 2). A PDZ binding motif at the C-terminus interacts with several cytoplasmic junctional proteins (1). The ECD of mouse CXADR shares 97%, 90%, 89%, 89% and 88% aa sequence identity with the corresponding regions of rat, human, bovine, porcine and canine CXADR, respectively. An alternately spliced isoform (CXADR2) that diverges in the C-terminal 15 aa shows the same expression pattern, but may show different subcellular localization (4, 8). Transcription of other splice variants has been detected, but not their translation. A secreted form identified in serum and pleural fluid can block viral infection (9).
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