Recombinant Human Chondroadherin (Catalog # 8218-CH) inducesadhesion of ATDC5 mouse chondrogenic cells. The ED50 for this effect is 0.4-2.4 μg/mL.
2 μg/lane of Recombinant Human Chondroadherin was resolved with SDS-PAGE underreducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Bluestaining, showing bands at 33-38 kDa.
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
38 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
33-38 kDa, reducing conditions
Publications
Read Publication using 8218-CH in the following applications:
12 months from date of receipt, ≤ -20 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, ≤ -20 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 500 μg/mL in PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Chondroadherin His-tag Protein, CF
CHAD
chondroadherin proteoglycan
Chondroadherin
SLRR4A
SLRR4ACartilage leucine-rich protein
Background
Chondroadherin
(CHAD), also known as SLRR4A, is a 38-kDa secreted protein belonging to the small
leucine-rich proteoglycans (SLRPs) that help regulate the assembly and function
of the ECM (1). CHAD is highly expressed
in cartilaginous tissues, with lower expression levels found in bone, tendon,
and eye (2-4). Mature human CHAD consists of a 337 amino acid (aa) protein that contains
eleven leucine-rich repeats (LRRs) including nine tandem leucine-rich repeats
as well as N-terminal and C-terminal leucine-rich domains flanked by
cysteine-rich regions (5). CHAD
interacts with collagen II and mediates signaling between chondrocytes and the
ECM by binding to the alpha 2 beta 1 integrin, heparan sulphate, and to cell surface
proteoglycans like syndecans (5-9). In addition, CHAD interacts with both N-
and C-terminal globular domains of type VI collagen (10). Human CHAD shares 95% and 94% aa sequence identity with mouse and rat CHAD, respectively.
Neame, P.J. et al. (1994) J. Biol. Chem. 269:21547.
Larson, T. et al. (1991) J. Biol. Chem. 266:20428.
Mizuno, M. et al. (1996) Calcif. Tissue Int. 59:163.
Johnson, J.M. et al. (2006) Mol. Vis. 12:1057.
Månsson, B. et al. (2001) J. Biol. Chem. 276:32883.
Paracuellos, P. et al. (2017) Matrix Biol. 63:106.
Batista, M. et al. (2014) Matrix Biol. 38:84.
Camper, L. et al. (1997) J. Cell Biol. 138:1159.
Haglund, L. et al. (2013) J. Biol. Chem. 288:995.
Wiberg, C. et al. (2002) J. Biol. Chem. 277:49120.
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