Recombinant Human CTRP5/C1qTNF5 Protein, CF

Recombinant Human CTRP5/C1qTNF5 Induces Phosphorylation of AMPK in C2C12 Differentiated Myocytes. C2C12 differentiated myocytes were treated with Recombinant Human CTRP5/C1qTNF5 (Catalog # 9510‑TN) for 1 hour prior to Western blot analysis

• Reactivity: Hu
• Applications: Binding Activity, Bioactivity
• Format: Carrier-Free

Recombinant Human CTRP5/C1qTNF5 Protein, CF Summary

• Details of Functionality: Measured by its ability to induce phospho AMPK activation in C2C12 mouse differentiated myocytes. 300 ng/mL of Recombinant Human CTRP5/C1qTNF5 induces phosphorylation of AMPK. Measured by its binding ability in a functional ELISA. When Recombinant Human MFRP (Catalog # 1915-MF) is immobilized at 2 μg/mL, 100 μL/well, the concentration of Recombinant Human CTRP5/C1qTNF5 that produces 50% of the optimal binding response is 0.3-1.8 μg/mL.
• Source: Mouse myeloma cell line, NS0-derived human CTRP5/C1qTNF5 protein
  Ser16-Ala243, with Gln44Arg substitution and a C-terminal 6-His tag
• Accession #: Q9BXJ0
• N-terminal Sequence: Ser16
• Protein/Peptide Type: Recombinant Proteins
• Purity: >85%, 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:
  • Binding Activity2
  • Bioactivity
• Theoretical MW: 25 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: 26-32 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 HEPES and NaCl.
• Purity: >85%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 200 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 CTRP5/C1qTNF5 Protein, CF

• C1q and tumor necrosis factor related protein 5
• C1qTNF5
• Complement C1q Tumor Necrosis Factor-Related Protein 5 Precursor Variant 3
• CTRP5
• CTRP5LORDDKFZp586B0621
• LORD 6
• Myonectin 3

Background

CTRP5, also known as C1qTNF5, belongs to the highly conserved family of Acrp30/Adiponectin paralogs known as C1q and TNF‑related protein family (1). All family members share a modular organization comprising an N‑terminal signal peptide, a short variable region with conserved cysteine residues, a collagenous domain for coiled coil structure, and a C‑terminal globular domain (2, 3). CTRP proteins are predicted to have trimeric structures that can assemble into higher order molecular forms (1). Human and mouse CTRP5 share 94% amino acid sequence identity. CTRP5 is highly expressed in the eye, testis and adipose tissue (4). A mutation (S163R) in C1qTNF5 impairs secretion and is associated with early-onset long anterior zonules (LAZ) and late-onset retinal degeneration (L-ORD) (5). In both mouse and human, the 3' untranslated region of the MFRP transcript contains the complete open reading frame of C1qTNF5, suggesting that these genes are dicistronic. MFRP and C1qTNF5 have been shown to directly interact in the retinal pigment epithelium and are likely functionally related (6). Like other C1qTNF family members, C1qTNF5 shares similarities to adiponectin in structure and function and has been shown to stimulate glucose uptake and increase fatty acid oxidation through activation of AMPK in skeletal muscle (3). Conversely, administration of rhC1qTNF5 was shown to attenuate insulin-induced Akt activation in adipocytes and skeletal muscle (7).

1. Wong, G.W. et al. (2004) Proc. Natl. Acad. Sci. U. S. A. 101:10302.
2. Thanasupawat, T. et al. (2015) Front. Endocrinol. (Lausanne) 6:127.
3. Park, S.Y. et al. (2009) J. Biol. Chem. 284:27780.
4. Schäffler A. and Buechler C. (2012) Trends Endocrinol. Metab. 23:194.
5. Tu X. and Palczewski K. (2014) J. Struct. Biol. 186:86.
6. Mandal M.N. et al. (2006) Invest. Ophthalmol. Vis. Sci. 47:5505.
7. Lei X. et al. (2016) Am. J. Physiol. Endocrinol. Metab. 310:E1036.

Bioinformatics

• Uniprot:
  • Q9BXJ0()