Recombinant Mouse Osteocrin Protein, CF Summary
Val28-Gly130, 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 250 μg/mL in 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.
Osteocrin, also known as Musclin, is a secreted protein that is primarily expressed in bone and muscle. It is synthesized as a proprotein (11 kDa) that undergoes proteolytic processing to generate a mature 50 amino acid C-terminal active peptide (1). It was found to modulate osteoblast differentation and to regulate glucose metabolism in muscles (2). Mouse Osteocrin proprotein shares 77% and 78% amino acid sequence identity with the rat and human protein, respectively. Secretion of Osteocrin has been shown to be increased with exercise and is associated with metabolically beneficial formation of brown fat (3). Osteocrin has also been attributed to increases in exercise endurance through promotion of mitochondrial biosynthesis (4). Based on similarities with NPs (natriuretic peptides), Osteocrin was found to interact with NP clearance receptor NPR-C. This interaction is thought to modulate the availability of NPs, importantly increasing CNP which has been shown to stimulate endochondral ossification and elongate bones (5). In primates, Osteocrin may have evolved to regulate neuronal structure and function (6).
- Nishizawa, H. et al. (2004) Journal of Biological Chemistry, 279:19391.
- Thomas, G. et al. (2003) Journal of Biological Chemistry, 278:50563.
- Jeramic N. et al. (2017) J Cell Physiol 232:61.
- Subbatino, E. et al. (2015) Proc. Acad. Natl. Sci. U. S. A. 112:16042.
- Kanai, Y. et al. (2017) J of Clin Invest 127: 4136
- Ataman, B. et al. (2016) Nature 539:242.
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