Recombinant Human Matrilin-3 Protein, CF

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R&D Systems Recombinant Proteins and Enzymes
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Recombinant Human Matrilin-3 Protein, CF Summary

Product Specifications

>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.01 EU per 1 μg of the protein by the LAL method.
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.
Mouse myeloma cell line, NS0-derived human Matrilin-3 protein
Asp29-Arg486, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Predicted Molecular Mass
50.6 kDa
57 kDa, reducing conditions

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Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.


Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 100 μg/mL in sterile PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.
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Background: Matrilin-3

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.
Entrez Gene IDs
4148 (Human); 17182 (Mouse)
Alternate Names
DIPOA; EDM5; HOA; matrilin 3; Matrilin3; Matrilin-3; NDUFC2; OADIP; OS2

Citations for Recombinant Human Matrilin-3 Protein, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

4 Citations: Showing 1 - 4
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  1. Matrilin-3 alleviates extracellular matrix degradation of nucleus pulposus cells via induction of IL-1 receptor antagonist
    Authors: XD Lu, YR Liu, ZY Zhang
    Eur Rev Med Pharmacol Sci, 2020;24(10):5231-5241.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  2. Matrilin-3 inhibits chondrocyte hypertrophy as a bone morphogenetic protein-2 antagonist.
    Authors: Yang X, Trehan S, Guan Y, Sun C, Moore D, Jayasuriya C, Chen Q
    J Biol Chem, 2014;289(50):34768-79.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Bioassay
  3. Identification of a central role for complement in osteoarthritis.
    Authors: Wang Q, Rozelle AL, Lepus CM
    Nat. Med., 2011;17(12):1674-9.
    Species: Human
    Sample Types: Tissue Homogenates
    Applications: Bioassay
  4. 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.
    Authors: 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
    J. Biol. Chem., 2007;282(15):11101-9.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Enzyme Assay Substrate


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