Recombinant Human Aggrecan G1-IGD-G2 Domains Protein, CF Summary
Product Specifications
Val20-Gly675, with a C-terminal 10-His tag
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
1220-PG
| Formulation | Lyophilized from a 0.2 μm filtered solution in Tris and NaCl. |
| Reconstitution | For hyaluronan-binding assay, reconstitute at 100 μg/mL in PBS. For use as a metalloprotease substrate, reconstitute at 250 μg/mL in 50 mM Tris, 10 mM CaCl2, 150 mM NaCl and 0.05% Brij-35, pH 7.5. |
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Reconstitution Calculator
Background: Aggrecan
Aggrecan, also known as aggrecan 1, chondroitin sulfate proteoglycan, and large aggregating proteoglycan, is encoded by the AGC1 gene with gene aliases of SEDK; CSPG1; MSK16; CSPGCP. As the key component of the cartilage extracellular matrix, aggrecan hydrates the collagen network and provides cartilage with its properties of compressibility and elasticity. Maintenance of aggrecan content is therefore critical to the function of the tissue and aggrecan degradation is an important factor in the erosion of articular cartilage in arthritic diseases (2). The deduced amino acid sequence of human aggrecan core protein consists of 2415 resides and predicts a signal peptide and domains of G1, IGD, G2, KS, CS-1, CS-2 and G3 (3). Two globular domains, G1 and G2, comprise the N-terminus of the proteoglycan and also contain link domains. The third globular domain, G3, corresponds to the C-terminus. The keratan sulfate (KS) and the chondroitin sulfate (CS) attachment domains are between G2 and G3. With KS and CS attached to the 250 kDa core protein, aggrecan monomers exist as a 1,000 to 2,000 kDa molecule. In addition, aggrecan monomers interact with hyaluronan through their G1 domain, resulting in larger aggregates containing 10 to 100 aggrecan monomers on a hyaluronan backbone (2).
Aggrecan can be cleaved by MMPs and ADAMTSs at the Asn360-Phe361 and Glu392-Ala393 bond in the IGD (residues are numbered based on Accession # NP_037359), respectively (2). Inhibition of ADATMS4 and ADAMTS5 cleavage prevents aggrecan degradation in osteoarthritic cartilage, while mice with aggrecan resistant to MMP cleavage do not accumulate aggrean and develop normally (2,4). Consisting of the G1, IGD and G2 domains, recombinant human Aggrecan can be used as a protein substrate for MMPs and ADAMTSs and in binding assays involving hyaluronan.
- Doege. K.J. et al. (1991) J. Biol. Chem. 266:894.
- Malfait, A.-M. et al. (2002) J. Biol. Chem. 277:22201.
- Caterson, B. et al. (2000) Matrix Biol. 19:333.
- Little, C.B. et al. (2005) Mol. Cel. Biol. 25:3388.
Citations for Recombinant Human Aggrecan G1-IGD-G2 Domains Protein, CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
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Citations: Showing 1 - 7
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Parvalbumin interneuron-derived tissue-type plasminogen activator shapes perineuronal net structure
Authors: M Lépine, S Douceau, G Devienne, P Prunotto, S Lenoir, C Regnauld, E Pouettre, J Piquet, L Lebouvier, Y Hommet, E Maubert, V Agin, B Lambolez, B Cauli, C Ali, D Vivien
Bmc Biology, 2022-10-05;20(1):218.
Species: Human
Sample Types: Protein
Applications: Bioassay -
Highly sensitive quantification of bacterial chondroitin in a culture based on ELISA techniques
Authors: K Suzuki, H Kaseyama-T, S Ito
Journal of microbiological methods, 2022-09-16;0(0):106579.
Species: Bacteria - Escherichia coli
Sample Types: Protein
Applications: Surface Plasmon Resonance (SPR -
Hyaluronan synthase 2, a target of miR-200c, promotes carbon tetrachloride-induced acute and chronic liver inflammation via regulation of CCL3 and CCL4
Authors: SM Kim, GY Song, A Shim, JH Lee, CB Eom, C Liu, YM Yang, E Seki
Experimental & Molecular Medicine, 2022-06-03;0(0):.
Species: Mouse
Sample Types: Whole Tissue
Applications: Bioassay -
Cleavage of proteoglycans, plasma proteins and the platelet-derived growth factor receptor in the hemorrhagic process induced by snake venom metalloproteinases
Authors: AF Asega, MC Menezes, D Trevisan-S, D Cajado-Car, L Bertholim, AK Oliveira, A Zelanis, SMT Serrano
Sci Rep, 2020-07-31;10(1):12912.
Species: Human, Snake
Sample Types: Protein, Recombinant Protein
Applications: Bioassay -
MEK inhibition suppresses K-Ras wild-type cholangiocarcinoma in vitro and in vivo via inhibiting cell proliferation and modulating tumor microenvironment
Authors: P Wang, X Song, K Utpatel, R Shang, YM Yang, M Xu, J Zhang, L Che, J Gordan, A Cigliano, E Seki, M Evert, DF Calvisi, X Hu, X Chen
Cell Death Dis, 2019-02-11;10(2):120.
Species: Mouse
Sample Types: Whole Tissue
Applications: IHC-P -
The serine proteinase hepsin is an activator of pro-matrix metalloproteinases: molecular mechanisms and implications for extracellular matrix turnover
Authors: DJ Wilkinson, A Desilets, H Lin, S Charlton, M Del Carmen, A Falconer, C Bullock, YC Hsu, K Birchall, A Hawkins, P Thompson, WR Ferrell, J Lockhart, R Plevin, Y Zhang, E Blain, SW Lin, R Leduc, JM Milner, AD Rowan
Sci Rep, 2017-12-01;7(1):16693.
Species: Human
Sample Types: Recombinant Protein
Applications: Enzyme Assay -
Identification of a novel HtrA1-susceptible cleavage site in human aggrecan: evidence for the involvement of HtrA1 in aggrecan proteolysis in vivo.
Authors: Chamberland A, Wang E, Jones AR, Collins-Racie LA, LaVallie ER, Huang Y, Liu L, Morris EA, Flannery CR, Yang Z
J. Biol. Chem., 2009-08-05;284(40):27352-9.
Applications: Enzyme Assay
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