Recombinant Mouse Matrilin-2 Protein


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Recombinant Mouse Matrilin-2 Protein Summary

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.
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
>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.


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.
120 kDa, reducing conditions

Packaging, Storage & Formulations

Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
>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.


This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse Matrilin-2 Protein

  • MATN2
  • matrilin 2
  • Matrilin2
  • Matrilin-2


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).

  1. Wagener, R. et al. (2005) FEBS Lett. 579:3323.
  2. Deak, F. et al. (1999) Matrix Biol. 18:55.
  3. Whittaker, C.A. and R.O. Hynes (2002) Mol. Biol. Cell 13:3369.
  4. Piecha, D. et al. (1999) J. Biol. Chem. 274:13353.
  5. Deak, F. et al. (1997) J. Biol. Chem. 272:9268.
  6. Piecha, D. et al. (2002) Biochem. J. 367:715.
  7. Frank, S. et al. (2002) J. Biol. Chem. 277:19071.
  8. Pan, O.H. and K. Beck (1998) J. Biol. Chem. 273:14205.
  9. Mates, L. et al. (2004) Matrix Biol. 23:195.

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