United States set
Menu Shopping cart $0 Search
Manufactured by BioVendor

Human Aggrecan (PG) ELISA

  • Regulatory status:RUO
  • Type:Sandwich ELISA, HRP-labelled antibody
  • Other names:PG, ACAN, Aggrecan core protein, Cartilage-specific proteoglycan core protein, CSPCP, Chondroitin sulfate proteoglycan core protein 1, Chondroitin sulfate proteoglycan 1, AGC1, AGCAN, CSPG1, CSPGCP, MSK16, SEDK, SSOAOD
  • Species:Human
Cat. No. Size Price

RIS001R 96 wells (1 kit) $552,35
PubMed Product Details
Technical Data


Sandwich ELISA, HRP-labelled antibody


The RIS001R Human Aggrecan (PG) ELISA Immunoenzymetric assay for the measurement of human aggrecan (PG) in synovial fluid, serum and cell culture supernatant. It is intended for research use only.


Serum, Synovial fluid, Cell culture supernatant

Sample Requirements

50 µl/well


On blue ice packs. Upon receipt, store the product at the temperature recommended below.


Store the complete kit at 2–8°C. Under these conditions, the kit is stable until the expiration date (see label on the box).

Calibration Curve

Calibration Range

10–250 ng/ml

Limit of Detection

0.9 ng/ml



  • RUO
  • calibration range 10-250 ng/ml
  • limit of detection 0.9 ng/ml
  • assay for the measurement of human aggrecan (PG) in synovial fluid, serum and cell culture supernatant
  • lyophilized controls

Research topic

Bone and cartilage metabolism, Extracellular matrix


Aggrecan (PG) is the predominant proteoglycan species in articular cartilage. It is composed of a core protein of 210 kDa to which over 100 chondroitin sulfate chains, about 20-50 keratan sulfate chains and O-linked as well as N-linked oligosaccharides are covently attached. The core protein contains three distinct globular domains (G1-G3). G1 is at the amino terminus, separated by a short extended segment from G2, while G3 is at the carboxy terminal end. The G1 amino terminal region can interact noncovalently with hyaluronic acid (HA) and has then be termed the hyaluronic acid binding region (HABR). A link protein interact with both the G1 region and the HA to stabilize this interaction. PG is produced by chondrocytes, and its production is regulated by cytokines and growth factors such as IL1β, TNFα, IGF1 or TGFβ. In extracellular matrix, as many as 200 aggrecan molecules can bind to one single HA molecule to form an aggregate (MW: 5.107 to 5.108). An imbalance in the synthesis and degradation of the matrix components is a common feature of both osteoarthritis and rheumatoid arthritis. The loss of PG and other matrix components from the cartilage leads to destruction of the tissue, causing complete deterioration of the articular surface. Several recent publications suggest that the PG and PG fragments released in synovial fluid and serum during the degradation process might serve as markers of the metabolic changes in diseased cartilage. Cell culture is a commonly used procedure for the study of cartilage metabolism. The measurement of PG and other matrix components in culture supernatants and cellular contents can assist analysis of the effects of cytokines, growth factors, drugs and potential chondroprotective substances on the cartilage homeostasy. Biovendor has developped a ELISA for the measurement of human aggrecan to aid the study of this important cartilage constituent. The PG-ELISA is convenient, highly specific, and allow accurate measurement of PG in synovial fluid, serum and culture supernatant This assay is a new interesting tool for the exploration of the cartilage metabolism.

Summary References (9)

References to Aggrecan

  • Bassleer C, Henrotin Y, Franchimont P. Insulin-Like Growth factor 1 and Glycosaminoglycan-Peptide Complex: Their Effects on Differentiated Human Chondrocytes Cultivated in Clusters. Litera Rheumatologica. 1991;13; 33-44
  • Bassleer C, Henrotin Y, Franchimont P. Effects of a Glycosaminoglycan-Peptide Complex and Interleukin 1 on Differentiated Human Chondrocytes Cultivated in Clusters. Litera Rheumatologica. 1991;13; 21-31
  • Franchimont P, Bassleer C. Effects of hormones and local growth factors on articular chondrocyte metabolism. J Rheumatol Suppl. 1991 Feb;27:68-70
  • Franchimont P, Bassleer C, Henrotin Y. Effects of hormones and drugs on cartilage repair. J Rheumatol Suppl. 1989 Aug;18:5-9
  • Heinegard D, Oldberg A. Structure and biology of cartilage and bone matrix noncollagenous macromolecules. FASEB J. 1989 Jul;3 (9):2042-51
  • Lohmander LS, Lark MW, Dahlberg L, Walakovits LA, Roos H. Cartilage matrix metabolism in osteoarthritis: markers in synovial fluid, serum, and urine. Clin Biochem. 1992 Jun;25 (3):167-74
  • Poole AR, Ionescu M, Swan A, Dieppe PA. Changes in cartilage metabolism in arthritis are reflected by altered serum and synovial fluid levels of the cartilage proteoglycan aggrecan. Implications for pathogenesis. J Clin Invest. 1994 Jul;94 (1):25-33
  • Saxne T, Heinegard D. Synovial fluid analysis of two groups of proteoglycan epitopes distinguishes early and late cartilage lesions. Arthritis Rheum. 1992 Apr;35 (4):385-90
  • Saxne T, Heinegard D, Wollheim FA. Cartilage proteoglycans in synovial fluid and serum in patients with inflammatory joint disease. Relation to systemic treatment. Arthritis Rheum. 1987 Sep;30 (9):972-9
Related Products Docs