Recombinant Mouse Matrilin-3 Protein, CF

• Reactivity: Mu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Mouse Matrilin-3 Protein, CF Summary

• Details of Functionality: Measured by its ability to induce adhesion of ATDC5 mouse chondrogenic cells. rmMatrilin-3, immobilized at 10 µg/mL (100 µL/well), induces 50-70% adhesion of ATDC-5 cells.
• Source: Mouse myeloma cell line, NS0-derived mouse Matrilin-3 protein
  Ala35-Arg481 & Arg39-Arg481, both with a C-terminal 6-His tag
• Accession #: Q6IR12
• N-terminal Sequence: Ala35 & Arg39
• Protein/Peptide Type: Recombinant Proteins
• Purity: >90%, 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

• Dilutions:
  • Bioactivity
• Theoretical MW: 49 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: 54-56 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.
• Purity: >90%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Reconstitution Instructions: Reconstitute at 100 μg/mL in sterile PBS.

Notes

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

Alternate Names for Recombinant Mouse Matrilin-3 Protein, CF

• DIPOA
• EDM5
• HOA
• matrilin 3
• Matrilin3
• Matrilin-3
• NDUFC2
• OADIP
• OS2

Background

Matrilin-3 is a 50 - 60 kDa extracellular matrix protein that belongs to the superfamily of von Willebrand factor A (VWA) containing proteins. It is primarily expressed in cartilage and functions as a bridging component between proteins of the collagenous matrix (1 - 3). The mouse Matrilin-3 cDNA encodes a 481 amino acid (aa) precursor with a 27 aa signal sequence, an N-terminal VWA domain, four tandem EGF-like repeats, and a C-terminal coiled-coil domain (4). The Matrilins differ in the number of VWA domains (one or two) and EGF-like repeats (one, three, four, or ten) they contain. Mouse Matrilin-3 shares 82% aa sequence identity with human Matrilin-3. Within the first VWA domain, mouse Matrilin-3 shares approximately 51% aa sequence identity with mouse Matrilin-1, -2, and -4. The coiled-coil domain of Matrilin-3 mediates disulfide-linked homo-oligomerization, with tetramer formation being the most dominant (5 - 7). It can also assemble into hetero-oligomers with Matrilin-1 (5 - 7). Matrilin-3 is more plentiful than Matrilin-1 in the proliferative zone of the growth plate, whereas the reverse is true in the maturation zone (5). Matrilin-3 interacts directly with Collagen IX and COMP (8, 9). In the absence of Collagen IX, the expression of Matrilin-3 is unchanged, although it is retained inside chondrocytes and is not incorporated into the matrix (9). Intracellular retention of Matrilin-3 also occurs with particular point mutations in the VWA domain that results in multiple epiphyseal dysplasia (11 - 13). In contrast, a point mutation in the first EGF-like repeat which has been linked to hand osteoarthritis does not prevent Matrilin-3 secretion (13). Matrilin-3 knockout mice do not display any obvious abnormalities, suggesting that other molecules may compensate for the lack of Matrilin-3 (10).

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. Wagener, R. et al. (1997) FEBS Lett. 413:129.
5. Zhang, Y. and Q. Chen (2000) J. Biol. Chem. 275:32628.
6. Klatt, A.R. et al. (2000) J. Biol. Chem. 275:3999.
7. Frank, S. et al. (2002) J. Biol. Chem. 277:19071.
8. Mann, H.H. et al. (2004) J. Biol. Chem. 279:25294.
9. Budde, B. et al. (2005) Mol. Cell. Biol. 25:10465.
10. Ko, Y. et al. (2004) Mol. Cell. Biol. 24:1691.
11. Jackson, G.C. et al. (2004) J. Med. Genet. 41:52.
12. Cotterill, S.L. et al. (2005) Hum. Mutat. 26:557.
13. Otten, C. et al. (2005) J. Med. Genet. 42:774.

Bioinformatics

• Uniprot:
  • Q6IR12()