When Recombinant Human NPRC/NPR-3 Fc Chimera (Catalog # 10233-NR) is immobilized at 2 μg/mL, Recombinant Human Osteocrin (Catalog # 9669-ON) binds with an ED50 of 2‑20 ng/mL.
Measured by its binding ability in a functional ELISA. When
Recombinant Human NPRC/NPR3 Fc Chimera
(Catalog #
10233-NR)
is
immobilized at 2 μg/mL
(100 μL/well), the concentration of Recombinant Human Osteocrin
that produces 50% of the optimal binding response is 2-20 ng/mL.
Source
E. coli-derived human Osteocrin protein Val28-Gly133, with a C-terminal 6-His tag
>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
13 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
18 kDa, reducing conditions
Publications
Read Publication using 9669-ON in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °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 250 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 Osteocrin Protein, CF
Musclin
Osteocrin
OSTN
Background
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 acids (5 kDa) C-terminal peptide (1).
It was found to modulate osteoblast differentiation and to regulate glucose
metabolism in muscles (2). Human Osteocrin proprotein shares 77% and 78% amino
acid sequence identity with the rat and mouse protein, respectively. Secretion
of Osteocrin has been shown to be increased with exercise and is associated
with metabolically beneficial formation of brown fat (3). Osterocrin 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) J Bio Chem 279:19391.
Thomas, G. et al. (2003) J Bio Chem 278:50563.
Jeramic, N. et al. (2017) J Cell Physiol 232:61.
Subbatino, E. et al. (2015) Proc Natl Acad Sci U S A 112:16042.
Kanai, Y. et al. (2017) J of Clin Invest 127:4136.
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