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B8041

Sigma-Aldrich

Biglycan from bovine articular cartilage

essentially salt-free, lyophilized powder

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About This Item

MDL number:
MFCD00676525
UNSPSC Code:
12352202
NACRES:
NA.75

biological source

bovine articular cartilage

Quality Level

200

form

essentially salt-free, lyophilized powder

mol wt

200-350 kDa

packaging

glass bottle of 0.5 mg

technique(s)

cell culture | mammalian: suitable

solubility

water: soluble ≥2.00 mg/mL, clear, colorless

UniProt accession no.

P21809

shipped in

dry ice

storage temp.

−20°C

Gene Information

cow ... BGN(280733)

General description

proteoglycan consisting of a 45 kDa core protein and two chrondroitin/dermatan sulfate glycosaminoglycan chains

Biochem/physiol Actions

Biglycan interacts with collagen type I and II, fibronectin and TGF-ß. In a low ionic strength (less than 3 mM phosphate) buffer, Biglycan binds more strongly to collagen type I. At higher ionic strengths, Biglycan will instead increase the inhibition effect of TGF-ß on osteoclast proliferation at a concentration of 4-20 mg/mL. It also functions to prevent the attachment of CHO cells to fibronectin, with a 50% inhibition at 17-21 mg/mL. As an extracellular component, Biglycan binds TGF-β 1, facilitates bone mineralization and supports osteoblast differentiation thru BMP-4 binding.

Components

Biglycan is a 200-350 kDa proteoglycan consisting of a 45 kDa core protein and two chondroitin/dermatan sulfate glycosaminoglycan chains.

Caution

Store this product at -20°C. Stored as supplied, this powder shows little decomposition in 3 years when stored properly.

Preparation Note

This product is extracted from articular cartilage, chematographically purified, dialyzed against water, and 0.2 μm filtered prior to lyophilization. Once lyophilized, this powder is essentially salt-free. The product is soluble in water at 2 mg/mL.

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)

Certificates of Analysis (COA)

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P J Roughley et al.
Matrix biology : journal of the International Society for Matrix Biology, 14(1), 51-59 (1994-01-01)
In chondrocytes isolated directly from human articular cartilage, without subsequent culture, biglycan mRNA levels decreased with the age of the donor, whereas those for decorin increased. In cultured chondrocytes in the presence of FCS, mRNA levels for biglycan remained similar
G Pogány et al.
Archives of biochemistry and biophysics, 313(1), 102-111 (1994-08-15)
Binding of proteoglycans to type I collagen in vitro was assessed using radiolabeled decorin, biglycan, and large proteoglycans and acid-extracted bovine tendon collagen. Decorin, biglycan, and large proteoglycans were all bound to collagen fibrils in phosphate-buffered saline (PBS) containing 3
E Schönherr et al.
The Journal of biological chemistry, 270(6), 2776-2783 (1995-02-10)
The small proteoglycan decorin is known to interact with type I collagen fibrils, thereby influencing the kinetics of fibril formation and the distance between adjacent collagen fibrils. The structurally related proteoglycan biglycan has been proposed not to bind to fibrillar
Xiao-Dong Chen et al.
FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 18(9), 948-958 (2004-06-03)
Biglycan (bgn) is a small leucine-rich proteoglycan enriched in extracellular matrices of skeletal tissues. Bgn-deficient mice develop age-related osteopenia with a phenotype that resembles osteoporosis and premature arthritis. In the present study, we have examined the differentiation of bgn-deficient osteoblasts
Mauricio Moreno et al.
The EMBO journal, 24(7), 1397-1405 (2005-03-19)
The BMP4 signaling pathway plays key roles during early embryonic development and for maintenance of adult homeostasis. In the extracellular space, BMP4 activity is regulated by a group of interacting molecules including the BMP antagonist Chordin, the metalloproteinase Tolloid and

Articles

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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