Recombinant Human Chondroadherin His-tag Protein, CF Summary
Ala22-Thr350, with a C-terminal 6-His tag
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.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 500 μg/mL in PBS.|
|Shipping||The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||
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.
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.
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- 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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