Recombinant Mouse Matrilin-3 Protein, CF Summary
Ala35-Arg481 & Arg39-Arg481, both with a C-terminal 6-His tag
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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 100 μg/mL in sterile PBS.|
|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.
Matrilin-3 is a 50 - 60 kDa extracellular matrix protein that belongs to the superfamily of von Willebrand factor A (VWA) containing proteins. It is primarily expressed in cartilage and functions as a bridging component between proteins of the collagenous matrix (1 - 3). The mouse Matrilin-3 cDNA encodes a 481 amino acid (aa) precursor with a 27 aa signal sequence, an N-terminal VWA domain, four tandem EGF-like repeats, and a C-terminal coiled-coil domain (4). The Matrilins differ in the number of VWA domains (one or two) and EGF-like repeats (one, three, four, or ten) they contain. Mouse Matrilin-3 shares 82% aa sequence identity with human Matrilin-3. Within the first VWA domain, mouse Matrilin-3 shares approximately 51% aa sequence identity with mouse Matrilin-1, -2, and -4. The coiled-coil domain of Matrilin-3 mediates disulfide-linked homo-oligomerization, with tetramer formation being the most dominant (5 - 7). It can also assemble into hetero-oligomers with Matrilin-1 (5 - 7). Matrilin-3 is more plentiful than Matrilin-1 in the proliferative zone of the growth plate, whereas the reverse is true in the maturation zone (5). Matrilin-3 interacts directly with Collagen IX and COMP (8, 9). In the absence of Collagen IX, the expression of Matrilin-3 is unchanged, although it is retained inside chondrocytes and is not incorporated into the matrix (9). Intracellular retention of Matrilin-3 also occurs with particular point mutations in the VWA domain that results in multiple epiphyseal dysplasia (11 - 13). In contrast, a point mutation in the first EGF-like repeat which has been linked to hand osteoarthritis does not prevent Matrilin-3 secretion (13). Matrilin-3 knockout mice do not display any obvious abnormalities, suggesting that other molecules may compensate for the lack of Matrilin-3 (10).
- Wagener, R. et al. (2005) FEBS Lett. 579:3323.
- Deak, F. et al. (1999) Matrix Biol. 18:55.
- Whittaker, C.A. and R.O. Hynes (2002) Mol. Biol. Cell 13:3369.
- Wagener, R. et al. (1997) FEBS Lett. 413:129.
- Zhang, Y. and Q. Chen (2000) J. Biol. Chem. 275:32628.
- Klatt, A.R. et al. (2000) J. Biol. Chem. 275:3999.
- Frank, S. et al. (2002) J. Biol. Chem. 277:19071.
- Mann, H.H. et al. (2004) J. Biol. Chem. 279:25294.
- Budde, B. et al. (2005) Mol. Cell. Biol. 25:10465.
- Ko, Y. et al. (2004) Mol. Cell. Biol. 24:1691.
- Jackson, G.C. et al. (2004) J. Med. Genet. 41:52.
- Cotterill, S.L. et al. (2005) Hum. Mutat. 26:557.
- Otten, C. et al. (2005) J. Med. Genet. 42:774.
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