Recombinant Mouse Matrilin-2 Protein

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Product Details

Summary
Reactivity MuSpecies Glossary
Applications Binding Activity

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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.
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.

Applications/Dilutions

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.
SDS-PAGE
120 kDa, reducing conditions

Packaging, Storage & Formulations

Storage
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.
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.

Notes

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

Background

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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