Recombinant Human Matrilin-3 Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Binding Activity
Format
Carrier-Free

Order Details

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 #
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

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
Publications
Read Publications using
3017-MN in the following applications:

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

  • B14.5b
  • CI-B14.5b
  • complex I subunit B14.5b
  • Complex I-B14.5b
  • EDM5
  • HLC-1NADH dehydrogenase (ubiquinone) 1, subcomplex unknown, 2 (14.5kD, B14.5b)
  • HOA
  • Human lung cancer oncogene 1 protein
  • Matrilin3
  • Matrilin-3
  • NADH dehydrogenase (ubiquinone) 1, subcomplex unknown, 2, 14.5kDa
  • NADH dehydrogenase [ubiquinone] 1 subunit C2
  • NADHDH2
  • NADH-ubiquinone oxidoreductase subunit B14.5b
  • NDUFC2

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.

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Publications for NDUFC2 (3017-MN)(3)

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Bioinformatics

Gene Symbol NDUFC2
Uniprot