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B8041

Sigma-Aldrich

Biglycan from bovine articular cartilage

essentially salt-free, lyophilized powder

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About This Item

Numéro MDL:
MFCD00676525
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.75

Source biologique

bovine articular cartilage

Niveau de qualité

200

Forme

essentially salt-free, lyophilized powder

Poids mol.

200-350 kDa

Conditionnement

glass bottle of 0.5 mg

Technique(s)

cell culture | mammalian: suitable

Solubilité

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

Numéro d'accès UniProt

P21809

Conditions d'expédition

dry ice

Température de stockage

−20°C

Informations sur le gène

cow ... BGN(280733)

Description générale

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

Actions biochimiques/physiologiques

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.

Composants

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

Attention

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

Notes préparatoires

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.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

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
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
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
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
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