Recombinant Human gAdiponectin/gAcrp30 Protein, CF

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

Recombinant Human gAdiponectin/gAcrp30 Protein, CF Summary

• Details of Functionality: Bioassay data are not available.
• Source: Mouse myeloma cell line, NS0-derived human gAdiponectin/gAcrp30 protein
  Ala108-Asn244, with a C-terminal 6-His tag
• Accession #: Q15848
• N-terminal Sequence: Ala108
• Protein/Peptide Type: Recombinant Proteins
• Gene: ADIPOQ
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Endotoxin Note: <0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 16.7 kDa (monomer).
  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: 19-20 kDa, reducing conditions

Packaging, Storage & Formulations

• Storage:
  • 4 months from date of receipt, 2 to 8 °C as supplied.
• Buffer: Supplied as a 0.2 μm filtered solution in PBS.
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human gAdiponectin/gAcrp30 Protein, CF

• gAcrp30
• gAdiponectin
• gAdipoQ
• gApM1

Background

Adiponectin, alternatively named Adipocyte Complement-Related Protein of 30 kDa (Acrp30), shares structural similarity with complement factor C1q and is a member of the family of defense collagens (1‑7). It is secreted exclusively by differentiated adipocytes and circulates at high concentrations (in μg/mL range). Adiponectin has a modular structure comprising an N-terminal collagenous domain with multiple collagen triple helix repeats, followed by a C-terminal C1q-like globular domain. The globular domain has similar folding topology with tumor necrosis factor-alpha and assembles into homotrimers. Higher order oligomeric adiponectins (hexamers and higher molecular weight forms) are also formed via interactions between the collagenous stalk. A truncated form of Adiponectin containing only the globular domain (gAdiponectin or gAcrp30) can be generated by proteolytic cleavage (5). The gAdiponectin as well as all oligomeric forms of the full length Adiponectin are detected in serum. Different isoforms of Adiponectin have been shown to activate different signal transduction pathways (8‑11). Conflicting biological activities have been reported for the various isoforms.

Two seven membrane-spanning Adiponectin receptors, designated AdipoR1 and AdipoR2 have been identified (12). AdipoR1 is expressed predominantly in muscle and functions as a high‑affinity receptor for gAdiponectin, but a very low‑affinity receptor for the full length Adiponectin. AdipoR2 binds both the full length and globulin domain with intermediate affinity and is expressed primarily in liver.

Adiponectin is an anti-diabetic and anti-atherogenic hormone that plays important roles in the regulation of lipid and glucose metabolism (1‑7). Similarly to full length Adiponectin, recombinant gAdiponectin from R&D Systems has been shown to inhibit proliferation of mouse M1 myeloid cells (13). The globular domain of human Adiponectin shares 89% aa sequence identity with the mouse homologue.

1. Scherer, P.E. et al. (1995) J. Biol. Chem. 270:26746.
2. Hu, E. et al. (1996) J. Biol. Chem. 271:10697.
3. Maeda, K. et al. (1996) Biochem. Biophys. Res. Commun. 221:286.
4. Tsao, T-S. et al. (2002) J. Biol. Chem. 277:29359.
5. Fruebis, J. et al. (2001) Proc. Natl. Acad. Sci. USA 98:2005.
6. Berg, A.H. et al. (2001) Nature Med. 7:947.
7. Pajvani, U.T. et al. (2003) J. Biol. Chem. 278:9073.
8. Tomas, E. et al. (2002) Proc. Natl. Acad. Sci. USA 99:16309.
9. Tsao, T.S. et al. (2003) J. Biol. Chem., Sept. 30 [Epub ahead of print].
10. Wang, Y. et al. (2002) J. Biol. Chem. 277:19521.
11. Sato, C. et al. (2001) J. Biol. Chem. 276:28849.
12. Yamauchi, T. et al. (2003) Nature 423:762.
13. Yokota, T. et al. (2000) Blood 96:1723.

Publications for gAdiponectin/gAcrp30 (1688-AC)(3)

Publications using 1688-AC

• S Kim, Y Lee, JW Kim, YJ Son, MJ Ma, JH Um, ND Kim, SH Min, DI Kim, BB Kim Discovery of a novel potent peptide agonist to adiponectin receptor 1 PLoS ONE, 2018-06-18;13(6):e0199256. 2018-06-18 [PMID: 29912982] (Bioassay, Mouse)
• Han R, Lai R, Ding Q, Wang Z, Luo X, Zhang Y, Cui G, He J, Liu W, Chen Y Apolipoprotein A-I stimulates AMP-activated protein kinase and improves glucose metabolism. Diabetologia, 2007-07-18;50(9):1960-8. 2007-07-18 [PMID: 17639303] (Bioassay, Mouse)
• Rovin BH, Song H Chemokine induction by the adipocyte-derived cytokine adiponectin. Clin. Immunol., 2006-02-28;120(1):99-105. 2006-02-28 [PMID: 16503200] (Bioassay, Human)

Bioinformatics

• Gene Symbol: ADIPOQ
• Uniprot:
  • Q15848()