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anti-Mouse (Murine) Fibromodulin Antikörper:
anti-Rat (Rattus) Fibromodulin Antikörper:
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Human Polyclonal Fibromodulin Primary Antibody für WB - ABIN4311712
Herchenhan, Uhlenbrock, Eliasson, Weis, Eyre, Kadler, Magnusson, Kjaer: Lysyl Oxidase Activity Is Required for Ordered Collagen Fibrillogenesis by Tendon Cells. in The Journal of biological chemistry 2015
Human Polyclonal Fibromodulin Primary Antibody für WB - ABIN515774
Yang, Culshaw, Liu, Lu, French, Clements, Corcoran: Canine tissue-specific expression of multiple small leucine rich proteoglycans. in Veterinary journal (London, England : 1997) 2012
The extracellular matrix proteoglycan fibromodulin is upregulated in clinical and experimental heart failure and affects cardiac remodeling.
FMOD affected the expressions of the Cav1.1 and Cav3.1 genes. FMOD regulates calcium channel activity. The mRNA expressions of Cav1.1 and Cav3.1 increased during muscle regeneration.
Studies in knockout, obese, and diabetic mouse models helped characterize the operation of a novel FMOD-based regulatory circuit that controls myoblast switching from a myogenic to a lipid accumulation fate. FMOD regulation of myoblasts is an essential part of the myogenic program, and it offers opportunities for the development of therapeutics for the treatment of different muscle diseases
impact of FMOD deficiency on the development of experimental skin fibrosis is limited
Fibromodulin can be a unique effector of dense collagen matrix assembly in tumor stroma and, without affecting other major matrix components or the cellular composition, can function as a main agent in tumor barrier function
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, targeting the enzyme toward specific cross-linking sites.
Suggest a more complex role for collagen in plaque stability than previously anticipated in fibromodulin-deficient/ApoE-null atherosclerotic mice.
The expression of decreased in the medial, basolateral, and central amygdala regions after chronic immobilization stress in mice.
Hepatic fibromodulin activates hepatic stellate cells and promotes collagen I deposition, which leads to liver fibrosis.
The differential effects of Fmod deficiency on bones and teeth appear to diverge in adult mice.
critical for temporomandibular joint subchondral bone integrity
Fibromodulin suppresses nuclear factor-kappaB activity by inducing the delayed degradation of IKBA via a JNK-dependent pathway coupled to fibroblast apoptosis.
FMOD presence is critical for proper temporospatial coordination of wound healing events and normal TGF-beta 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 and fibromodulin are novel key players in regulating chondrogenesis and extracellular matrix turnover during temoporomandibular joint osteoarthritis pathology.
deficiency combined with lumican deficiency manifest several clinical features or Ehlers-Danlos syndrome
promote formation of a dense stroma and elevated intersitial fluid pressure, thus modulated fluid balance in thyroid cancer.
Dual functions may be related to the different forms of Fmod found in bone versus teeth.
Homologous sequence in lumican and fibromodulin leucine-rich repeat 5-7 competes for collagen binding.
Some nine tyrosine residues in the fibromodulin N-terminal domain are O-sulfated, 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 treatment of fresh articular cartilage results in cleaved fibromodulin fragments
fibromodulin and decorin have similarities and differences that may represent the biochemical basis of redundancy in small leucine-rich proteoglycan function
tyrosine sulfate-rich domains of the LRR proteins fibromodulin and osteoadherin bind motifs of basic clusters in a variety of heparin-binding proteins, including bioactive factors
The results of luciferase reporter assay and methylation-specific PCR (MSP) demonstrated that GDNF facilitated the demethylation of the FMOD promoter.
crystal structures at ~2.2A resolution of human fibromodulin and chondroadherin.
we found that secreted FMOD as an important regulator of glioma cell migration downstream of TGF-beta1 pathway and forms a potential basis for therapeutic intervention in GBM.
The small leucine rich proteoglycan fibromodulin is overexpressed in human prostate epithelial cancer cell lines in culture and human prostate cancer tissue.
expression levels distinguish chronic lymphocytic leukemia B cells from normal B lymphocytes
fibromodulin is involved in the inflammatory processes that characterize atherosclerotic plaque vulnerability
The results suggest that regions within FMOD is associated with ACL 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.
Associations between higher fibomodulin gene expression and risk factors in chronic lymphocytic leukemia.
lumican and fibromodulin display different behaviors and that lumican may promote regeneration of the TMJ after degeneration and deformation induced by IL-1 beta.
study shows (1) a detailed description of ectopic ossification (EO) formed by Bgn, Fmod or combined depletion, (2) the role of exercise in modulating EO and (3) that Bgn 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
fibromodulin activates the classical pathway of complement by directly binding C1q
complement control protein 6-8 is able to interact with DNA and necrotic cells, but in contrast the His-384 allotype binds these ligands more strongly than the Tyr-384 variant
The collagen-binding Glu-353 and Lys-355 residues in fibromodulin are exposed on the exterior of the beta-sheet-loop structure of the leucine-rich repeat, which resembles the location of interacting residues in other leucine-rich repeat proteins.
Fibromodulin gene is constantly expressed in human epidermal keratinocytes.
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