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Sigma-Aldrich

Aggrecan from bovine articular cartilage

lyophilized powder

Synonym(s):

Aggrecan Protein

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About This Item

MDL number:
MFCD00676441
UNSPSC Code:
12352202
NACRES:
NA.75

biological source

bovine articular cartilage

Quality Level

200

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.

P13608

shipped in

wet ice

storage temp.

−20°C

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.

Components

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.

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 Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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H Hedlund et al.
The Journal of biological chemistry, 274(9), 5777-5781 (1999-02-20)
Aggrecan, the predominant large proteoglycan of cartilage, is a multidomain macromolecule with each domain contributing specific functional properties. One of the domains contains the majority of the keratan sulfate (KS) chain substituents and a protein segment with a proline-rich hexapeptide
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
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
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