| Reactivity | MuSpecies Glossary |
| Applications | Binding Activity |
| Details of Functionality | Measured by its binding ability in a functional ELISA. Immobilized Collagen I at 10 µg/mL (100 µL/well) will bind Recombinant Mouse Matrilin‑2 with a linear range of 8-1,000 ng/mL. |
| Source | Mouse myeloma cell line, NS0-derived mouse Matrilin-2 protein Arg24-Arg956 & Met40-Arg956, both with a C-terminal 6-His tag |
| Accession # | |
| N-terminal Sequence | Arg24 & Met40 |
| Protein/Peptide Type | Recombinant Proteins |
| Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
| Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
| Dilutions |
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| Theoretical MW | 104.9 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 | 120 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 with BSA as a carrier protein. |
| Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
| Reconstitution Instructions | Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin. |
Matrilin-2 is an extracellular matrix protein that belongs to the superfamily of von Willebrand factor A domain (VWA) containing proteins. It is expressed in many tissues and functions as a bridging component between other matrix molecules (1, 2, 3, 4). The mouse Matrilin-2 cDNA encodes a 956 amino acid (aa) precursor with a 23 aa signal sequence, two VWA domains separated by ten tandem EGF-like repeats, and a C-terminal coiled coil domain (5). Mouse Matrilin-2 shares 84%-87% aa sequence identity with human, rat, and canine Matrilin-2, and 26%, 21%, and 34% aa sequence identity with mouse Matrilin-1, -3, and -4, respectively. Matrilin-2 forms a variety of disulfide-linked oligomers via its coiled coil domain (4, 6-8). It can assemble into homotrimers or heterotrimers with Matrilin-1 and/or Matrilin-4 (4, 6, 7) but has not been detected in heterotrimers containing Matrilin-3 (7). The VWA domains are thought to mediate Matrilin-Matrilin interactions as well as interactions with other matrix proteins such as Fibronectin, Collagen I, Fibrilin-2, and Laminin-1/Nidogen-1 complexes (6). Matrilin-2 knockout mice do not display any obvious abnormalities, suggesting that the expression of other molecules can compensate for the lack of Matrilin-2 (9).
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