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The small leucine rich proteoglycan (show Vcan ELISA Kits) fibromodulin is overexpressed in human prostate epithelial cancer cell lines in culture and human prostate cancer tissue.
The data suggest a fibromodulin-modulated collagen cross-linking mechanism where fibromodulin binds to a specific part of the collagen domain and also forms a complex with lysyl oxidase (show LOX ELISA Kits), targeting the enzyme toward specific cross-linking sites.
fibromodulin is involved in the inflammatory processes that characterize atherosclerotic plaque vulnerability
The results suggest that regions within FMOD is associated with ACL (show ACLY ELISA Kits) injury susceptibility and that genetic sequence variability within genes encoding proteoglycans may potentially modulate the ligament fibril properties.
Melanocyte-secreted factor FMOD is a key regulator of angiogenesis.
Hepatic fibromodulin activates hepatic stellate cells and promotes collagen I deposition, which leads to liver fibrosis.
lumican (show LUM ELISA Kits) and fibromodulin display different behaviors and that lumican (show LUM ELISA Kits) may promote regeneration of the TMJ after degeneration and deformation induced by IL-1 beta (show IL1B ELISA Kits).
study shows (1) a detailed description of ectopic ossification (EO) formed by Bgn (show BGN ELISA Kits), Fmod or combined depletion, (2) the role of exercise in modulating EO and (3) that Bgn (show BGN ELISA Kits) and Fmod are critical in controlling motor function.
Fibromodulin is shown for the first time to be naturally processed and presented as a tumor-associated antigen in primary chronic lymphocytic leukemia cells, enabling the expansion of autologous tumor-specific T cells.
Fibromodulin has a role in progression of B-cell chronic lymphocytic leukemia and mantle cell lymphoma
Some nine tyrosine residues in the fibromodulin N-terminal domain are O-sulfated (show SULF1 ELISA Kits), a posttranslational modification often involved in protein interactions. Taken together, this study suggests a novel, regulatory function for tyrosine sulfation in Fibromodulin, which controls the interaction with collagen type I.
There are discrete populations of fibromodulin within articular cartilage, which may have differing impacts upon tissue processes.
MMP-13 (show MMP13 ELISA Kits) treatment of fresh articular cartilage results in cleaved fibromodulin fragments
fibromodulin and decorin (show DCN ELISA Kits) have similarities and differences that may represent the biochemical basis of redundancy in small leucine-rich proteoglycan (show Vcan ELISA Kits) function
tyrosine sulfate-rich domains of the LRR proteins fibromodulin and osteoadherin (show OMD ELISA Kits) bind motifs of basic clusters in a variety of heparin-binding proteins, including bioactive factors
Suggest a more complex role for collagen in plaque stability than previously anticipated in fibromodulin-deficient/ApoE (show APOE ELISA Kits)-null atherosclerotic mice.
The differential effects of Fmod deficiency on bones and teeth appear to diverge in adult mice.
Fibromodulin suppresses nuclear factor-kappaB activity by inducing the delayed degradation of IKBA (show NFKBIA ELISA Kits) via a JNK (show MAPK8 ELISA Kits)-dependent pathway coupled to fibroblast apoptosis.
FMOD presence is critical for proper temporospatial coordination of wound healing events and normal TGF-beta (show TGFB1 ELISA Kits) bioactivity.
fibromodulin plays important roles in the regulation of region-specific fibrillogenesis required for the integration of the corneal and scleral matrices and sulcus development required for establishment of the visual axis
Biglycan (show BGN ELISA Kits) and fibromodulin are novel key players in regulating chondrogenesis and extracellular matrix turnover during temoporomandibular joint osteoarthritis pathology.
deficiency combined with lumican (show LUM ELISA Kits) deficiency manifest several clinical features or Ehlers-Danlos syndrome
Dual functions may be related to the different forms of Fmod found in bone versus teeth.
Fibromodulin is a member of a family of small interstitial proteoglycans, containing a central region composed of leucine-rich repeats with 4 keratan sulfate chains flanked by disulfide-bonded terminal domains. It may participate in the assembly of the extracellular matrix as it interacts with type I and type II collagen fibrils and inhibits fibrillogenesis in vitro. It may also regulate TGF-beta activities by sequestering TGF-beta into the extracellular matrix.
, KSPG fibromodulin
, collagen-binding 59 kDa protein
, keratan sulfate proteoglycan fibromodulin