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The protein encoded by DCN is a small cellular or pericellular matrix proteoglycan that is closely related in structure to biglycan protein. Additionally we are shipping Decorin Antibodies (181) and Decorin Proteins (28) and many more products for this protein.
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Human Decorin ELISA Kit for Sandwich ELISA - ABIN625287
Kanzleiter, Rath, Görgens, Jensen, Tangen, Kolnes, Kolnes, Lee, Eckel, Schürmann, Eckardt: The myokine decorin is regulated by contraction and involved in muscle hypertrophy. in Biochemical and biophysical research communications 2014
Show all 3 references for ABIN625287
Mouse (Murine) Decorin ELISA Kit for Sandwich ELISA - ABIN1672791
Danielson, Fazzio, Cohen, Cannizzaro, Eichstetter, Iozzo: The human decorin gene: intron-exon organization, discovery of two alternatively spliced exons in the 5' untranslated region, and mapping of the gene to chromosome 12q23. in Genomics 1993
Show all 2 references for ABIN1672791
analysis of decorin and lumican (show LUM ELISA Kits) expression in fibroblasts correlated with palmoplantar collagen bundle size
via gain-of-function analyses, DCN overexpression could inhibit renal cell carcinoma (RCC (show XRCC1 ELISA Kits)) cell proliferation and metastasis in vitro and vivo. At the mechanism level, we found that an ectopic expression of DCN significantly upregulated P21 (show CDKN1A ELISA Kits) and E-cadherin (show CDH1 ELISA Kits) expression. Altogether, these results revealed that DCN is a tumor suppressor in RCC (show XRCC1 ELISA Kits), and it could serve as a potential therapeutic target in patients with RCC (show XRCC1 ELISA Kits).
Internal mammary artery tissue from active smokers contains decreased amounts of type 1 collagen and decorin.
A synthetic peptide corresponding to this decorin region dose-dependently inhibited the response to myostatin (show MSTN ELISA Kits) in cardiomyocytes
increased blood DCN levels could be a candidate biomarker for PE.
An emerging concept that multiple proteases, especially those produced by inflammatory cells, are capable of cleaving DCN suggests that native DCN could be inactivated in a number of pathological inflammatory conditions
Decorin plays a key role in the maintenance of the order in the normal corneal extracellular matrix.
Compared with bone graft and marrow cavity contents, sticking scars had the highest expression of BMP-2 (show BMP2 ELISA Kits) while bone grafts had the highest expression of DCN.
Defective Proteolytic Processing of Fibrillar Procollagens and Prodecorin Due to Biallelic BMP1 (show BMP1 ELISA Kits) Mutations Results in a Severe, Progressive Form of Osteogenesis Imperfecta (show COL1A2 ELISA Kits).
Data show that decorin is not only associated with angiogenesis, but it plays a causal role in this process. Also, depending on the molecular microenvironment where angiogenesis is induced, decorin can either promote or inhibit angiogenesis. [review]
The inclusion of decorin proteoglycan during fibrillogenesis of type I collagen increases the modulus and tensile strength of resulting collagen gels.
These findings reveal a novel role of DCN as an antagonistic ligand for VEGFR-2 (show KDR ELISA Kits).
Data show that biglycan (show BGN ELISA Kits), collagen type I, collagen type II, decorin, and versican (show Vcan ELISA Kits) were significantly affected by vibration duration, frequency, and amplitude.
Results suggest that decorin contributes to the formation and stabilization of collagen fibres in the perimysium that support muscle fibres assembled with myogenesis.
decorin is a dimer in solution
decorin-induced fibroblast cytoskeletal and signalling changes result in an increased cell migration; potential role in the remodelling process
Transduced bovine decorin synthesized de novo by rat arterial smooth muscle cells increases type I collagen synthesis and enhances contraction of collagen gels.
The results indicate that CTGF (show CTGF ELISA Kits) suppresses the synthesis of biglycan (show BGN ELISA Kits) but newly induced that of decorin in the cells when the cell density is low.
a novel collagen binding domain in decorin acts cooperatively with leucine-rich repeat 4 to mask the alpha2beta1 integrin-binding site on collagen, an important sequence for the phagocytosis of collagen fibrils
analysis of decorin from different bovine tissues
Systemic delivery of an oncolytic adenovirus expressing decorin for the treatment of breast cancer bone metastases reduced tumor burden and inhibited bone destruction.
Decorin is an autophagy-inducible proteoglycan (show Vcan ELISA Kits) and is required for proper in vivo autophagy.
Importance of biglycan (show BGN ELISA Kits) and decorin as targets for the manipulation of fetal membrane extracellular matrix stability in the context of inflammation.
The results suggest that decorin plays a dual role in AAA (show AAAS ELISA Kits). Adventitial decorin in normal aorta may protect against the development of AAA (show AAAS ELISA Kits)
Development of congenital stromal dystrophy is dependent on export and extracellular deposition of truncated decorin.
decorin may modulate follicular cycling and morphogenesis
We found that decorin is abundantly secreted and deposited in normal connective tissue but its expression is consistently decreased in the tumor microenvironment.
Decorin signaling supported fetal membrane remodeling at early stages of gestation in a TGFbeta (show TGFB1 ELISA Kits)-dependent manner, and fetal membrane stabilization at later stages of gestation without changes in TGFbeta (show TGFB1 ELISA Kits) levels.
A decorin-deficient matrix affects skin chondroitin/dermatan sulfate levels and keratinocyte function.
LDL electrostatic interactions with decorin and biglycan (show BGN ELISA Kits) in the aortic valve leaflets and vascular wall is a major source of LDL retention.
The expression of the DCN gene increased from gestational day 26 to 90 in both Yorkshire and Meishan pig placenta.
The protein encoded by this gene is a small cellular or pericellular matrix proteoglycan that is closely related in structure to biglycan protein. The encoded protein and biglycan are thought to be the result of a gene duplication. This protein is a component of connective tissue, binds to type I collagen fibrils, and plays a role in matrix assembly. It contains one attached glycosaminoglycan chain. This protein is capable of suppressing the growth of various tumor cell lines. There are multiple alternatively spliced transcript variants known for this gene. This gene is a candidate gene for Marfan syndrome.
, bone proteoglycan II
, decorin proteoglycan
, dermatan sulphate proteoglycans II
, proteoglycan core protein
, small leucine-rich protein 1B
, dermatan sulfate proteoglycan-II (decorin)
, dermatan sulfate proteoglycan II