Reactivity | HuSpecies Glossary |
Applications | Binding Activity |
Details of Functionality | Measured by its binding ability in a functional ELISA. Immobilized rat tail Collagen I at 10 µg/mL (100 µL/well) can bind rhMatrilin-2 with a linear range of 16-1,000 ng/mL. |
Source | Mouse myeloma cell line, NS0-derived human Matrilin-2 protein Arg24-Arg937, with a C-terminal 6-His tag |
Accession # | |
N-terminal Sequence | Arg24 |
Protein/Peptide Type | Recombinant Proteins |
Gene | MATN2 |
Purity | >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
Theoretical MW | 103 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 | >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions | Reconstitute at 100 μg/mL in sterile PBS. |
Matrilin-2 is an extracellular matrix protein that belongs to the superfamily of von Willebrand factor A (VWA) containing proteins. It is expressed in many tissues and functions as a bridging component between other matrix proteins (1 - 4). The human 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, 6). Alternate splicing generates Isoform 2 (with an 18 aa deletion near the C-terminus), Isoform 3 (with a deletion of the fourth EGF-like repeat), and Isoform 4 (with a deletion of the first VWA and first EGF-like repeat). Human Matrilin-2 shares 87% and 84% aa sequence identity with mouse and canine Matrilin-2, respectively, and 27%, 22%, and 33% aa sequence identity with human Matrilin-1, -3, and -4, respectively. Matrilin-2 forms a variety of disulfide-linked oligomers via its coiled-coil domain (4, 7, 8, 9). It can assemble into homotrimers or heterotrimers with Matrilin-1 and/or Matrilin-4 (4, 7, 8) but has not been detected in heterotrimers containing Matrilin-3 (8). The VWA domains are thought to mediate Matrilin-Matrilin interactions as well as interactions with other matrix proteins such as Fibronectin, Collagen I, Fibrillin-2, and Laminin-1/Nidogen-1 complexes (7). 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 (10).
PTMs for Matrilin-2 (3044-MN)Learn more about PTMs related to Matrilin-2 (3044-MN).
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