Recombinant Human CTRP3/C1qTNF3/CORS26 Protein, CF

When Recombinant Human CTRP3/C1qTNF3/CORS26 (Catalog #9398-TN) is immobilized at 4 µg/mL, Recombinant Human CD36/SR-B3 Fc Chimera (Catalog # 1955-CD) binds with an ED50 of 1.5-7.5 μg/mL.

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human CTRP3/C1qTNF3/CORS26 Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinan Human CTRP3/C1qTNF3/CORS26 is immobilized at 4 µg/mL (100 µL/well), the concentration of Recombinant Human CD36/SR-B3 Fc Chimera (Catalog # 1955-CD) that produces 50% of the optimal binding response is 1.5-7.5 μg/mL.
• Source: Mouse myeloma cell line, NS0-derived human CTRP3/C1qTNF3/CORS26 protein
  Gln23-Lys246
• Accession #: Q9BXJ4-1
• N-terminal Sequence: No results obtained. Gln23 inferred from enzymetic pyroglutamate treatment revealing Asp24
• Structure / Form: Disulfide-linked homo-oligomer
• Protein/Peptide Type: Recombinant Proteins
• Purity: >90%, 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: 24 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: 25-37 kDa, reducing conditions

Packaging, Storage & Formulations

• Storage: 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: >90%, 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 CTRP3/C1qTNF3/CORS26 Protein, CF

• C1ATNF3
• C1q and tumor necrosis factor related protein 3
• C1qTNF3
• Cartducin
• cartonectin
• collagenous repeat-containing sequence of 26-kDa
• complement C1q tumor necrosis factor-related protein 3
• complement-c1q tumor necrosis factor-related protein 3
• Corcs
• Cors
• CORS26
• Cors-26
• CTRP3
• CTRP32310005P21Rik
• FLJ37576
• Secretory protein CORS26

Background

CORS-26 (collagenous repeat-containing sequence of 26 kDa protein) also known as C1qTNF3 (complement C1q TNF-related protein 3/CTRP3), cartonectin, cartducin, is a 30-32 kDa, secreted member of the C1q and TNF-related (CTRP) superfamily of molecules (1). The mature protein is 224 aa in length. It contains an N-terminal collagen-like domain followed by a C-terminal globular region. Human CORS26 shares 99% aa sequence identity with the mouse CORS26 (2). Like other CTRP members, CORS26 has a trimeric structure and can assemble into hexameric or higher order molecular forms (3). It is expressed by a variety of cells, including adipocytes, cartilage, fibroblasts, monocytes and proliferating chondrocytes (4). The inflammatory effects of LPS, TLR-4 and fatty acids have been shown to be inhibited by CORS26 in adipocytes and monocytes (5). In mouse models, CORS26 has been shown to lower glucose levels and decrease gluconeogenic gene expression (6). Inhibition of 3T3-L1 pre-adipocyte differentiation to adipocytes is associated with CORS26 treatment, demonstrating potential anti-obesity effects (7). Treatment with CORS26 results in the proliferation of skeletal muscle C2C12 cells and inhibition of C2C12 myotube differentiation, mediated by the ERK pathway (8). Due to the variety of functions in metabolism and inflammation, CORS26 is a potential new target of type 2 diabetes treatment.

1. Wong, G.W. et al. (2004) Proc. Natl. Acad. Sci. U.S.A. 101:10302.
2. Schaffler A. et al. (2003). Biochim Biophys Acta.1630:123.
3. Suzuki S. et al. (2007) FEBS Lett. 581: 809.
4. Weigert J. et al. (2005) FEBS Lett. 579: 5565.
5. Kopp, A. et al. (2010) Endocrinology. 151:5267.
6. Peterson J. M. et al. (2010) J Biol Chem. 285:39691.
7. Nishimoto, H. et al. (2017) Cell Bio Int. 41:197.
8. Otani M. et al. (2015) Mol Cell Biochem. 409:271.

Bioinformatics

• Uniprot:
  • Q9BXJ4-1()