Recombinant Human Fibromodulin/FMOD Protein, CF

When Bovine Collagen-I is immobilized at 10 μg/mL, 100 μL/well, Recombinant Human Fibromodulin/FMOD (Catalog # 9840-FM) binds with anED50 of 1-6 μg/mL.

2 μg/lane of Recombinant Human Fibromodulin/FMOD Protein (Catalog # 9840-FM) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 41-55 kDa.

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human Fibromodulin/FMOD Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA.

  When Bovine Collagen I is coated at 10 µg/mL (100 μL/well), Recombinant Human Fibromodulin/FMOD (Catalog # 9840-FM) binds with an ED₅₀ of 0.250-2.25 µg/mL.

• Source: Mouse myeloma cell line, NS0-derived human Fibromodulin/FMOD protein
  Asp75-Ile376, with an N-terminal 10-His tag
• Accession #: Q06828
• N-terminal Sequence: His
• Protein/Peptide Type: Recombinant Proteins
• Purity: >95%, 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

• Dilutions:
  • Bioactivity
• Theoretical MW: 36 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: 41-55 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 Trehalose.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining
• Reconstitution Instructions: Reconstitute at 200 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Fibromodulin/FMOD Protein, CF

• Collagen-binding 59 kDa protein
• fibromodulin proteoglycan
• Fibromodulin
• FM
• FMOD
• Keratan sulfate proteoglycan fibromodulin
• SLRR2E
• SLRR2EKSPG fibromodulin

Background

Fibromodulin (FMOD) is a secreted, 60-70 kDa class II member of the small leucine-rich proteoglycan (SLRP) family of matrix proteins. It is expressed by a variety of cell types, including keratinocytes, fibroblasts and chrondrocytes, and is known to bind to type I and XII collagen, plus TGF-beta (1, 2). FMOD is posited to displace lumican binding to collagen, generating 3D collagen fibrils from simple lumican-induced collagen dimers (3). Mature human FMOD is 358 amino acids (aa) in length (aa 19-376). It contains a sulfated N-terminal complement C1q binding domain (aa 19-98) and 12 Leu-rich repeats (LRRs) (aa 98-376), with the LRR5-7 and LRR11 responsible for collagen type I binding (2 - 4). Fibromodulin contains varying amounts of keratan sulfate, and undergoes significant tyrosine sulfation (5). Over aa 76-376, human Fibromodulin shares 96% aa identity with mouse and rat Fibromodulin. Recent study has shown that FMOD can induce glioma cell migration and invasion by promoting actin cytoskeleton remodeling (6).

1. Velez-Delvalle, C. et al. (2008) Biochem. Biophys. Res. Commun. 371:420.
2. Kalamajski, S. et al. (2007) J. Biol. Chem. 282:26740.
3. Kalamajski, S. et al. (2009) J. Biol. Chem. 284:534.
4. Sjoberg, A. et al. (2005) J. Biol. Chem. 280:32301.
5. Onnerfjord, P. et al. (2004) J. Biol. Chem. 279:26.
6. Mondal, B. et al. (2017) Oncogene 36:71.

Publications for Fibromodulin/FMOD (9840-FM)(1)

Publication using 9840-FM

• Kolb, J;Tsata, V;John, N;Kim, K;Möckel, C;Rosso, G;Kurbel, V;Parmar, A;Sharma, G;Karandasheva, K;Abuhattum, S;Lyraki, O;Beck, T;Müller, P;Schlü beta ler, R;Frischknecht, R;Wehner, A;Krombholz, N;Steigenberger, B;Beis, D;Takeoka, A;Blümcke, I;Möllmert, S;Singh, K;Guck, J;Kobow, K;Wehner, D; Small leucine-rich proteoglycans inhibit CNS regeneration by modifying the structural and mechanical properties of the lesion environment Nature communications 2023-10-26 [PMID: 37884489] (Bioassay, Mouse)

Bioinformatics

• Uniprot:
  • Q06828()