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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 (165) and Decorin Kits (64) and many more products for this protein.
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Human Decorin Protein expressed in Human Cells - ABIN2002301
Li, Pennisi, Yaccoby: Role of decorin in the antimyeloma effects of osteoblasts. in Blood 2008
Show all 5 references for ABIN2002301
Human Decorin Protein expressed in Wheat germ - ABIN1351201
Khan, Girish, Lala, Di Guglielmo, Lala: Decorin is a novel VEGFR-2-binding antagonist for the human extravillous trophoblast. in Molecular endocrinology (Baltimore, Md.) 2011
Show all 4 references for ABIN1351201
Human Decorin Protein expressed in HEK-293 Cells - ABIN2180962
Santra, Reed, Iozzo: Decorin binds to a narrow region of the epidermal growth factor (EGF) receptor, partially overlapping but distinct from the EGF-binding epitope. in The Journal of biological chemistry 2002
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 Proteins) while bone grafts had the highest expression of DCN.
Defective Proteolytic Processing of Fibrillar Procollagens and Prodecorin Due to Biallelic BMP1 (show BMP1 Proteins) Mutations Results in a Severe, Progressive Form of Osteogenesis Imperfecta (show COL1A2 Proteins).
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]
findings indicate that decorin may indirectly act as an antagonist to MM cell survival and that the interplay between MM and decorin may be an important target to explore in manipulating the tumor niche to inhibit tumorigenesis
decorin expression and immunoreactivity in normal and malignant human colorectal tissue
Our results reveal the molecular details of the periostin (show POSTN Proteins)-decorin complex in both phyllodes tumor tissues and breast cancer cells; this interaction may represent a novel target for anti-cancer therapy
A role for decorin and p-Smad-2 (show SMAD2 Proteins) in the pathophysiology of fetal membranes and adverse pregnancy outcomes.
decorin plays crucial roles in non-small-cell lung cancer against carcinogenesis and progression.
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 Proteins).
Data show that biglycan (show BGN Proteins), collagen type I, collagen type II, decorin, and versican (show Vcan Proteins) 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 Proteins) suppresses the synthesis of biglycan (show BGN Proteins) 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 Proteins) and is required for proper in vivo autophagy.
Importance of biglycan (show BGN Proteins) 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 Proteins). Adventitial decorin in normal aorta may protect against the development of AAA (show AAAS Proteins)
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 Proteins)-dependent manner, and fetal membrane stabilization at later stages of gestation without changes in TGFbeta (show TGFB1 Proteins) levels.
A decorin-deficient matrix affects skin chondroitin/dermatan sulfate levels and keratinocyte function.
Decorin deficiency promotes hepatic carcinogenesis.
LDL electrostatic interactions with decorin and biglycan (show BGN Proteins) 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