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D8428

Sigma-Aldrich

Decorin from bovine articular cartilage

salt-free, lyophilized powder

Sinónimos:

Decorin protein

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About This Item

MDL number:
MFCD00283027
UNSPSC Code:
12352202
NACRES:
NA.75

biological source

bovine articular cartilage

Quality Level

200

form

salt-free, lyophilized powder

mol wt

~100 kDa

packaging

glass bottle of 0.5 mg

technique(s)

cell culture | mammalian: suitable

solubility

PBS: ≥2.00 mg/mL, clear, colorless to yellow

UniProt accession no.

P21793

storage temp.

−20°C

Gene Information

cow ... DCN(280760)

Categorías relacionadas

General description

Decoran is a small proteoglycan composed of a chondroitin/dermatan sulfate glycosaminoglycans attached to a 40 kDa core protein. It is found primarily in the extracellular matrix of articular cartilage. Decorin interacts with collagen types I and II via its core protein wherein it delays fibrillogenesis. Decorin also interacts with fibronectin, thrombospondin and TGF-β isoforms, and the EGF-receptor.
Decorin from bovine articular cartilage is a proteoglycan that belongs to the small leucine-rich repeat proteoglycans and proteins (SLRPs) family. Decorin is present in almost all tissues. It has a protein core composed of leucine-rich repeats (LRRs), flanked by two cysteine-rich regions.

Application

Decorin from bovine articular cartilage has been used in solid phase binding assay (ELISA), binding assays, binding inhibition assay, parasite binding assays, scaffold fabrication, quartz crystal microbalance assay, inhibition of CSA (chondroitin sulphate A) binding assay and glycans and glycan biotinylation.

Biochem/physiol Actions

Decorin plays an important role in guiding the proper assembly of collagen during fibrillogenesis. Deficiency in decorin results in altered tissue structure and function. It controls growth factors like EGF and TGF-β. Decorin blocks aggregation of fibrils into fibers and fibrillogenesis in cell-free constructs of polymerized type I collagen.

Other Notes

Decorin is an approx. 100 kDa proteoglycan consisting of a 40 kDa core protein and one chondroitin or dermatan sulfate glycosaminoglycan chain. From 0.2 μm filtered solution prior to lyophilization.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Certificados de análisis (COA)

Lot/Batch Number
019M4179V
11180819
078M4093V
11170815
057M4102V

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Differential induction of functional IgG using the Plasmodium falciparum placental malaria vaccine candidate VAR2CSA.
Pinto V V, et al.
PLoS ONE, 6(3), e17942-e17942 (2011)
Crystal structure of the dimeric protein core of decorin, the archetypal small leucine-rich repeat proteoglycan.
Scott P G, et al.
Proceedings of the National Academy of Sciences of the USA, 101(44), 15633-15638 (2004)
Daniela G Seidler et al.
IUBMB life, 60(11), 729-733 (2008-09-19)
A molecular network of extracellular matrix molecules determines the tissue architecture and accounts for mechanical properties like compressibility or stretch resistance. It is widely accepted that the elements of the cellular microenvironment are important regulators of the cellular behavior in
Xiaolei Wang et al.
Scientific reports, 7(1), 9672-9672 (2017-08-31)
Choroidal neovascularization(CNV) is the most severe complication in Age-related macular degeneration(AMD) and the most common cause of irreversible blindness in the elderly in developed world. The aim of this study was to identify the effect of transforming growth factor-β(TGF-β) and
Engineering of fibrillar decorin matrices for a tissue-engineered trachea.
Hinderer S, et al.
Biomaterials, 33(21), 5259-5266 (2012)
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Artículos

Glycosaminoglycans and Proteoglycans

There are five identified glycosaminoglycan chains (see Figure 1): Hyaluronan is not sulfated, but the other glycosaminoglycan chains contain sulfate substituents at various positions of the chain.

Glycosaminoglycan Sulfation and Signaling

Glycosaminoglycans are large linear polysaccharides constructed of repeating disaccharide units.

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