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Merck

A1960

Aggrecan from bovine articular cartilage

lyophilized powder

Synonyme(s) :

Aggrecan Protein

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About This Item

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

Nom du produit

Aggrecan from bovine articular cartilage, lyophilized powder

biological source

bovine articular cartilage

form

lyophilized powder

packaging

glass bottle of 1 mg

technique(s)

cell culture | mammalian: suitable

impurities

salt, essentially free

color

white

solubility

H2O: 2 mg/mL

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

Quality Level

Gene Information

cow ... AGC1(280985)

Application

Aggrecan is a critical component for cartilage structure and the function of joints. Its synthesis and degradation are being studied for their roles in cartilage deterioration during joint injury disease and aging.

Biochem/physiol Actions

This molecule produces a rigid, reversibly deformable gel that resists compression. It combines with hyaluronic acid to form very large macromolecular complexes that have an increased hydrohynamic volume and a significant increase (30-40%) in the relative viscosity of the solution.

Disclaimer

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

Other Notes

Aggrecan is a major structural proteoglycan of the cartilage extracellular matrix. It is a large proteoglycan, with a molecular weight greater than 2,500 kDa composed of approximately 100-150 glycosaminoglycan chains attached to a core protein. The majority of these glycosaminoglycan chains are chondroitin/dermatan sulfate. Aggrecan contains three globular domains, G1, G2, and G3, which are involved in aggregation and hylauronan binding, cell adhesion and chondrycte apoptosis.

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.

Classe de stockage

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

L Cao et al.
Experimental cell research, 246(2), 527-537 (1999-02-02)
A major feature of cartilage deterioration during joint injury and disease is aggrecan degradation and the loss of proteoglycan. Most of the degraded fragments are released into the circulatory system except the G1 domain which accumulates locally in the synovial
N Ishiguro et al.
Arthritis and rheumatism, 42(1), 129-136 (1999-01-27)
To determine the relationship between matrix metalloproteinases (MMPs), their inhibitors, and the turnover of matrix molecules in articular cartilage from patients with osteoarthritis (OA). Synovial fluid samples were collected from the knees of 54 patients with OA. Radiographic evaluations and
T E Hardingham et al.
European journal of clinical chemistry and clinical biochemistry : journal of the Forum of European Clinical Chemistry Societies, 32(4), 249-257 (1994-04-01)
Aggrecan, the large aggregating proteoglycan from cartilage contains chondroitin sulphate and keratan sulphate attached to a multidomain protein core. It aggregates by binding to hyaluronan and this is further stabilised by a separate globular link protein. There are two structurally
C J Billington et al.
The Biochemical journal, 336 ( Pt 1), 207-212 (1998-11-10)
The breakdown of aggrecan in cartilage is, in part, mediated by an enzyme named aggrecanase that cleaves within the interglobular domain of the molecule between a glutamic residue and an alanine residue. Although the enzyme cleavage site has been identified
L Cao et al.
Matrix biology : journal of the International Society for Matrix Biology, 17(5), 379-392 (1998-11-20)
The proteoglycan aggrecan is a major component of cartilage, and degradation of aggrecan is associated with aging and a number of pathological conditions. To investigate the effects of the accumulation of G1 domain from degraded aggrecan, we overexpressed the G1

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