| Species : |
Mouse |
| Source : |
Mouse myeloma cell line |
| Tag : |
His |
| Protein Length : |
21-349 aa |
| Description : |
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 extracellular matrix (ECM). CHAD is highly expressed in cartilaginous tissues, with lower expression levels found in bone, tendon, and eye. Mature mouse CHAD is a 338 amino acid (aa) protein that contains twelve leucine-rich repeats (LRRs) including ten tandem leucine-rich repeats as well as N-terminal and C-terminal leucine-rich domains flanked by cysteine-rich regions. 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. In addition, CHAD also interacts with both N- and C-terminal globular domains of type VI collagen. Mouse CHAD shares 95% and 98% aa sequence identity with human and rat CHAD, respectively. |
| Form : |
Lyophilized from a 0.2 μm filtered solution in PBS. |
| Bio-activity : |
Measured by its ability to induce adhesion of ATDC5 mouse chondrogenic cells. The ED50 for this effect is 0.08-048 μg/mL |
| Molecular Mass : |
38 kDa |
| Endotoxin : |
< 0.10 EU/μg of the protein by the LAL method. |
| Purity : |
> 95% by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie Blue Staining. |
| Storage : |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, ≤ -20 centigrade as supplied.
1 month, 2 to 8 centigrade under sterile conditions after reconstitution.
3 months, ≤ -20 centigrade under sterile conditions after reconstitution. |
| Shipping : |
The product is shipped at ambient temperature. |
| Reconstitution : |
Reconstitute at 500 μg/mL in PBS. |
| N-terminal Sequence Analysis : |
No results obtained. Protein identity confirmed via Mass Spectrometry. |
| Reference : |
1. Neame, P.J. et al. (1994) J. Biol. Chem. 269:21547.
2. Larson, T. et al. (1991) J. Biol. Chem. 266:20428.
3. Mizuno, M. et al. (1996) Calcif. Tissue Int. 59:163. |
