Aggrecan Antibody [M12J8] | Primary Antibodies

Application: Reactivity: Human

Usage Information

Dilution
WB1:1000-1:10000

Application
WB

Reactivity
Human

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
261 kDa 600 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Datasheet & SDS

Biological Description

Specificity
Aggrecan Antibody [M12J8] detects endogenous levels of total Aggrecan protein.

Clone
M12J8

Synonym(s)
ACAN, AGC1, AGCAN, aggrecan, Aggrecan core protein, Aggrecan core protein 2, CSPCP, CSPG1, CSPGCP, large aggregating proteoglycan, MSK16, PGCA, SEDK, SSOAOD

Background
Aggrecan, encoded by ACAN, is a large chondroitin sulfate proteoglycan of the lectican family that is highly expressed in growth plate and articular cartilage and forms a major non‑collagenous structural component of the cartilage extracellular matrix together with type II collagen. The core protein contains three globular domains (G1, G2, G3) separated by extended regions bearing dense arrays of chondroitin sulfate and keratan sulfate chains; the N‑terminal G1 domain, which shares structural motifs with link protein, binds hyaluronan and link protein to form large ternary aggregates, the central G2 domain is homologous to G1/link repeats and contributes to product processing, and the C‑terminal G3 domain regulates glycosaminoglycan modification, secretion, and interactions with other matrix molecules. The glycosaminoglycan‑rich domain between G2 and G3 carries multiple chondroitin sulfate and keratan sulfate chains that create a highly negatively charged, bottlebrush‑like polyelectrolyte, and aggrecan–hyaluronan aggregates embedded in the collagen network form a hydrated gel that imbibes water, generates swelling pressure, and provides the osmotic and mechanical properties required for cartilage to resist compressive loads during joint use. Through hyaluronan‑dependent aggregation and interactions of its G3 domain with ECM partners such as tenascins, fibulins, and fibrillin, aggrecan organizes the pericellular and territorial matrix and contributes to chondrocyte–matrix and chondrocyte–chondrocyte interactions that influence chondroskeletal morphogenesis in development and maintenance of articular cartilage architecture in maturity. In the central nervous system, aggrecan is present in perineuronal nets where it binds hyaluronan, link protein, and tenascins to form condensed ECM structures around neurons, and in this context it regulates the organization of neural extracellular space and contributes to control of developmental plasticity and responses to injury. ACAN mutations that alter core protein structure or glycosaminoglycan attachment associate with short stature, skeletal dysplasia, and abnormal joint and spine development, consistent with a central role of aggrecan in growth plate function and cartilage patterning. In osteoarthritis and related degenerative joint diseases, aggrecan loss from cartilage is an early and prominent event, and cleavage of the core protein by aggrecanases such as ADAMTS‑4 and ADAMTS‑5, and by matrix metalloproteinases, generates defined fragments that diffuse from the tissue and reduce proteoglycan content, leading to diminished load‑bearing capacity and altered cartilage biomechanics.

Background

Aggrecan, encoded by ACAN, is a large chondroitin sulfate proteoglycan of the lectican family that is highly expressed in growth plate and articular cartilage and forms a major non‑collagenous structural component of the cartilage extracellular matrix together with type II collagen. The core protein contains three globular domains (G1, G2, G3) separated by extended regions bearing dense arrays of chondroitin sulfate and keratan sulfate chains; the N‑terminal G1 domain, which shares structural motifs with link protein, binds hyaluronan and link protein to form large ternary aggregates, the central G2 domain is homologous to G1/link repeats and contributes to product processing, and the C‑terminal G3 domain regulates glycosaminoglycan modification, secretion, and interactions with other matrix molecules. The glycosaminoglycan‑rich domain between G2 and G3 carries multiple chondroitin sulfate and keratan sulfate chains that create a highly negatively charged, bottlebrush‑like polyelectrolyte, and aggrecan–hyaluronan aggregates embedded in the collagen network form a hydrated gel that imbibes water, generates swelling pressure, and provides the osmotic and mechanical properties required for cartilage to resist compressive loads during joint use. Through hyaluronan‑dependent aggregation and interactions of its G3 domain with ECM partners such as tenascins, fibulins, and fibrillin, aggrecan organizes the pericellular and territorial matrix and contributes to chondrocyte–matrix and chondrocyte–chondrocyte interactions that influence chondroskeletal morphogenesis in development and maintenance of articular cartilage architecture in maturity. In the central nervous system, aggrecan is present in perineuronal nets where it binds hyaluronan, link protein, and tenascins to form condensed ECM structures around neurons, and in this context it regulates the organization of neural extracellular space and contributes to control of developmental plasticity and responses to injury. ACAN mutations that alter core protein structure or glycosaminoglycan attachment associate with short stature, skeletal dysplasia, and abnormal joint and spine development, consistent with a central role of aggrecan in growth plate function and cartilage patterning. In osteoarthritis and related degenerative joint diseases, aggrecan loss from cartilage is an early and prominent event, and cleavage of the core protein by aggrecanases such as ADAMTS‑4 and ADAMTS‑5, and by matrix metalloproteinases, generates defined fragments that diffuse from the tissue and reduce proteoglycan content, leading to diminished load‑bearing capacity and altered cartilage biomechanics.

References
https://pubmed.ncbi.nlm.nih.gov/11942407/ https://pubmed.ncbi.nlm.nih.gov/26914753/

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%