Recombinant Mouse Matrilin-4 Protein, CF

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Product Details

Summary
Reactivity MuSpecies Glossary
Applications Binding Activity
Format
Carrier-Free

Order Details

Recombinant Mouse Matrilin-4 Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. Immobilized rhCOMP/his (2 µg/mL, 100 µL/well) can bind rmMatrilin-4 with a linear range of 3-200 ng/mL.
Source
Mouse myeloma cell line, NS0-derived mouse Matrilin-4 protein
Gln22-Lys624, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
No results obtained: Gln22 predicted
Protein/Peptide Type
Recombinant Proteins
Gene
Matn4
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
  • Binding Activity
Theoretical MW
67.2 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
75 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-4 Protein, CF

  • FLJ14417
  • MATN4
  • matrilin 4
  • Matrilin4
  • Matrilin-4

Background

Matrilin-4 is a 73 kDa secreted glycoprotein that is a member of the matrilin family of the von Willebrand Factor-A (vWA) domain-containing superfamily (1). Matrilins are modular extracellular matrix proteins that serve as adaptors and linkers for other matrix proteins. Matrilin-4, like Matrilin-2, has a broad distribution in both cartilage and in loose connective tissue such as dermis, lung and kidney, while matrilins 1 and 3 are limited to cartilage. Matrilin-4 is present in nervous tissue and is abundant in the brain (2, 3). Mature mouse Matrilin-4 shares 98%, 90%, 89% and 66% amino acid (aa) identity with rat, human, canine and chicken Matrilin-4, respectively. The 624 aa mouse Matrilin-4 contains a 22 aa signal sequence, two potential glycosylation sites, and four cysteine-rich EGF-like domains placed between two vWA domains. A short isoform lacks the N-terminal vWA domain (aa 28 - 217). A C-terminal alpha -helix/coiled-coil region (aa 590 - 623) by which multimers are formed is often proteolytically removed so that Matrilin-4 is found as a mixture of monomers with homo- or hetero- dimers and trimers. Matrilin-4 forms multimers with Matrilins 1 and 2 but not with Matrilin-3 (3, 4). The N-terminal vWA domains of Matrilins associate with collagen IV microfibrils via the proteoglycans biglycan and decorin, linking the fibrils with other matrix constituents aggrecan and collagen II (5, 6). Matrilins also show calcium-dependent binding to the cartilage oligomeric matrix protein (COMP); this interaction is of high affinity for oligomeric Matrilin-4 and somewhat lower affinity for monomeric Matrilin-4 (6). Functions and distributions of Matrilins overlap enough so that knockouts of Matrilins 1, 2 and 3 lack obvious phenotypes (1).

  1. Wagener, R. et al. (2005) FEBS Lett. 579:3323.
  2. Klatt, A.R. et al. (2002) Matrix Biol. 21:289.
  3. Klatt, A.R. et al. (2001) J. Biol. Chem. 276:17267.
  4. Frank, S. et al. (2002) J. Biol. Chem. 277:19071.
  5. Wiberg, C. et al. (2003) J. Biol. Chem. 278:37698.
  6. Mann, H.H. et al. (2004) J. Biol. Chem. 279:25294.
  7. Frank, S. et al. (2002) J. Biol. Chem. 277:19071.

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Bioinformatics

Gene Symbol Matn4
Uniprot