Recombinant Human Matrilin-3 Protein, CF

• Reactivity: Hu
• Applications: Binding Activity
• Format: Carrier-Free

Recombinant Human Matrilin-3 Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. Immobilized rhCOMP at 2 µg/mL (100 µL/well) can bind rhMatrilin-3 with a linear range of 1.5-100 ng/mL.
• Source: Mouse myeloma cell line, NS0-derived human Matrilin-3 protein
  Asp29-Arg486, with a C-terminal 6-His tag
• Accession #: O15232
• N-terminal Sequence: Asp29
• Protein/Peptide Type: Recombinant Proteins
• Gene: NDUFC2
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Endotoxin Note: <0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Binding Activity
• Theoretical MW: 50.6 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: 57 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: >95%, 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 Human 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 human Matrilin-3 cDNA encodes a 486 amino acid (aa) precursor with a 28 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. Human Matrilin-3 shares 82% aa sequence identity with mouse Matrilin-3. Within the first VWA domain, human Matrilin-3 shares approximately 55% aa sequence identity with human 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). Matrilin-3 also associates with smaller cartilage fibrils independent of Collagen IX (9). Matrilin-3 knockout mice do not display any obvious abnormalities, suggesting that other molecules may compensate for the lack of Matrilin-3 (10). In contrast, intracellular retention of Matrilin-3 with particular point mutations in the VWA domain results in multiple epiphyseal dysplasia (11 - 13). A point mutation in the first EGF-like repeat which has been linked to hand osteoarthritis does not prevent Matrilin-3 secretion (13).

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. Belluoccio, D. et al. (1998) Genomics 53:391.
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.

Publications for MATN3 (3017-MN)(4)

Publications using 3017-MN

• XD Lu, YR Liu, ZY Zhang Matrilin-3 alleviates extracellular matrix degradation of nucleus pulposus cells via induction of IL-1 receptor antagonist Eur Rev Med Pharmacol Sci, 2020-05-01;24(10):5231-5241. 2020-05-01 [PMID: 32495856] (Bioassay, Human)
• Yang X, Trehan S, Guan Y, Sun C, Moore D, Jayasuriya C, Chen Q Matrilin-3 inhibits chondrocyte hypertrophy as a bone morphogenetic protein-2 antagonist. J Biol Chem, 2014-10-20;289(50):34768-79. 2014-10-20 [PMID: 25331953] (Bioassay, Human)
• Wang Q, Rozelle AL, Lepus CM Identification of a central role for complement in osteoarthritis. Nat. Med., 2011-11-06;17(12):1674-9. 2011-11-06 [PMID: 22057346] (Bioassay, Human)
• Hills R, Mazzarella R, Fok K, Liu M, Nemirovskiy O, Leone J, Zack MD, Arner EC, Viswanathan M, Abujoub A, Muruganandam A, Sexton DJ, Bassill GJ, Sato AK, Malfait AM, Tortorella MD Identification of an ADAMTS-4 cleavage motif using phage display leads to the development of fluorogenic peptide substrates and reveals matrilin-3 as a novel substrate. J. Biol. Chem., 2007-02-20;282(15):11101-9. 2007-02-20 [PMID: 17311924] (Enzyme Assay Substrate, Human)

Bioinformatics

• Gene Symbol: NDUFC2
• Uniprot:
  • O15232()