Recombinant Human Fibromodulin/FMOD Protein, CF Summary
Product Specifications
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.
Asp75-Ile376, with an N-terminal 10-His tag
Analysis
Product Datasheets
Carrier Free
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.
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.
9840-FM
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
Reconstitution | Reconstitute at 200 μg/mL in 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.
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Scientific Data

When Bovine Collagen I is coated at 10 µg/mL (100 μL/well), Recombinant Human Fibromodulin/FMOD Protein (Catalog # 9840-FM) binds with an ED50 of 0.250-2.25 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.
Reconstitution Calculator
Background: Fibromodulin/FMOD
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).
- Velez-Delvalle, C. et al. (2008) Biochem. Biophys. Res. Commun. 371:420.
- Kalamajski, S. et al. (2007) J. Biol. Chem. 282:26740.
- Kalamajski, S. et al. (2009) J. Biol. Chem. 284:534.
- Sjoberg, A. et al. (2005) J. Biol. Chem. 280:32301.
- Onnerfjord, P. et al. (2004) J. Biol. Chem. 279:26.
- Mondal, B. et al. (2017) Oncogene 36:71.
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