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TNMD encodes a protein that is related to chondromodulin-I, which is a cartilage-specific glycoprotein that functions to stimulate chondrocyte growth and to inhibit tube formation of endothelial cells. Additionally we are shipping Tenomodulin Antibodies (54) and Tenomodulin Proteins (7) and many more products for this protein.
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Human TNMD ELISA Kit for Sandwich ELISA - ABIN852804
Bolton, Montastier, Carayol, Bonnel, Mir, Marques, Astrup, Saris, Iacovoni, Villa-Vialaneix, Valsesia, Langin, Viguerie: Molecular Biomarkers for Weight Control in Obese Individuals Subjected to a Multiphase Dietary Intervention. in The Journal of clinical endocrinology and metabolism 2017
our study demonstrates that Tnmd is required for proper tendon tissue adaptation to endurance running and aids in better understanding of the structural-functional relationships of tendon tissues.
TNMD is upregulated in adipose tissue of insulin-resistant versus insulin-sensitive individuals. TNMD expression increases in human preadipocytes during differentiation, whereas silencing TNMD blocks adipogenesis.
results suggest that Tnmd acts on the maturation or maintenance of the PDL by positively regulating cell adhesion via its BRICHOS domain
Report differential expression and cellular localization of novel isoforms of the tendon biomarker tenomodulin and suggest possible roles in tenocyte proliferation and tendon injury.
According to these results the sequence variation of TNMD is not associated with alzheimer disease, but might modify the effect of APOE (show APOE ELISA Kits) epsilon4-allele in women.
Tenomodulin is expressed abundantly in the elastin (show ELN ELISA Kits)-rich subendothelial outer layer of the normal chordae tendineae cordis.
TNMD could be a novel candidate gene for age-related macular degeneration.
Human adipose tissue TNMD gene expression is highly affected by obesity, adipose tissue location, and weight loss, indicating that TNMD may play a role in adipose tissue function.
Tnmd is required for prevention of adipocyte accumulation and fibrovascular scar formation during early tendon healing.
The results of enhanced tenogenic differentiation and neotendon formation indicated that Tnmd may serve not only as a tenogenic marker but also as a positive regulator of MSCs tenogenic differentiation, which might be applied to MSCs-mediated tendon regeneration.
In vitro comparison of tenogenic differentiation potentials among bone marrow derived stem cells (BMSCs), adipose derived stem cells (ASCs), dermal fibroblasts (DFs (show FST ELISA Kits)) and tenocytes (TCs) of the same Tnmd transgenic mice. BMSCs exhibited the best tenogenic potential than other three cell types.
Upon high-fat diet feeding, transgenic mice overexpressing Tnmd develop increased epididymal white adipose tissue (eWAT) mass, and preadipocytes derived from Tnmd transgenic mice display greater proliferation, consistent with elevated adipogenesis.
Loss of Tnmd affects significantly the self-renewal and senescence properties, but not the multipotential of tendon stem cells.
In our study of MM development, the laminar structure regulating TeM also prevents vascular invasion during the formation of compartment of the MM.
Results suggest that tenomodulin (Tnmd) is a regulator of tenocyte proliferation and is involved in collagen fibril maturation but do not confirm an in vivo involvement of Tnmd in angiogenesis.
The expression domains of ChM-I (show LECT1 ELISA Kits) and TeM during vertebrate development incorporate the typical avascular regions of the mesenchymal tissues.
This gene encodes a protein that is related to chondromodulin-I, which is a cartilage-specific glycoprotein that functions to stimulate chondrocyte growth and to inhibit tube formation of endothelial cells. This protein is also an angiogenesis inhibitor. Genetic variation in this gene is associated with a risk for type 2 diabetes, central obesity and serum levels of systemic immune mediators in a body size-dependent manner. This gene is also a candidate gene for age-related macular degeneration, though a direct link has yet to be demonstrated.
, BRICHOS domain containing 4
, chondromodulin-1-like protein
, chondromodulin-I-like protein