Recombinant Human Matrilin-2 Protein

• Reactivity: Hu
• Applications: Binding Activity

Recombinant Human Matrilin-2 Protein Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. Immobilized rat tail Collagen I at 10 µg/mL (100 µL/well) can bind rhMatrilin-2 with a linear range of 16-1,000 ng/mL.
• Source: Mouse myeloma cell line, NS0-derived human Matrilin-2 protein
  Arg24-Arg937, with a C-terminal 6-His tag
• Accession #: AAH10444
• N-terminal Sequence: Arg24
• Protein/Peptide Type: Recombinant Proteins
• Gene: MATN2
• Purity: >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Theoretical MW: 103 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: >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• 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-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 (VWA) containing proteins. It is expressed in many tissues and functions as a bridging component between other matrix proteins (1 - 4). The human 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, 6). Alternate splicing generates Isoform 2 (with an 18 aa deletion near the C-terminus), Isoform 3 (with a deletion of the fourth EGF-like repeat), and Isoform 4 (with a deletion of the first VWA and first EGF-like repeat). Human Matrilin-2 shares 87% and 84% aa sequence identity with mouse and canine Matrilin-2, respectively, and 27%, 22%, and 33% aa sequence identity with human Matrilin-1, -3, and -4, respectively. Matrilin-2 forms a variety of disulfide-linked oligomers via its coiled-coil domain (4, 7, 8, 9). It can assemble into homotrimers or heterotrimers with Matrilin-1 and/or Matrilin-4 (4, 7, 8) but has not been detected in heterotrimers containing Matrilin-3 (8). The VWA domains are thought to mediate Matrilin-Matrilin interactions as well as interactions with other matrix proteins such as Fibronectin, Collagen I, Fibrillin-2, and Laminin-1/Nidogen-1 complexes (7). 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 (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. Piecha, D. et al. (1999) J. Biol. Chem. 274:13353.
5. Muratoglu, S. et al. (2000) Cytogenet. Cell Genet. 90:323.
6. Deak, F. et al. (1997) J. Biol. Chem. 272:9268.
7. Piecha, D. et al. (2002) Biochem. J. 367:715.
8. Frank, S. et al. (2002) J. Biol. Chem. 277:19071.
9. Pan, O.H. and K. Beck (1998) J. Biol. Chem. 273:14205.
10. Mates, L. et al. (2004) Matrix Biol. 23:195.

Publications for Matrilin-2 (3044-MN)(2)

Publications using 3044-MN

• E The, Q Yao, P Zhang, Y Zhai, L Ao, DA Fullerton, X Meng Mechanistic Roles of Matrilin-2 and Klotho in Modulating the Inflammatory Activity of Human Aortic Valve Cells Cells, 2020;9(2):. 2020 [PMID: 32046115] (Cell Culture, Human)
• F Li, R Song, L Ao, TB Reece, JC Cleveland, N Dong, DA Fullerton, X Meng ADAMTS5 Deficiency in Calcified Aortic Valves Is Associated With Elevated Pro-Osteogenic Activity in Valvular Interstitial Cells Arterioscler. Thromb. Vasc. Biol., 2017;0(0):. 2017 [PMID: 28546218] (Bioassay, Human)

Bioinformatics

• Gene Symbol: MATN2
• Uniprot:
  • AAH10444()