Recombinant Mouse gAdiponectin/gAcrp30 Protein, CF

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

Recombinant Mouse gAdiponectin/gAcrp30 Protein, CF Summary

• Details of Functionality: Measured by its ability to induce TIMP-1 secretion by mouse macrophages. Kumada, M. et al. (2004) Circulation 109:2046. The ED₅₀ for this effect is 5-20 µg/mL.
• Source: Mouse myeloma cell line, NS0-derived mouse gAdiponectin/gAcrp30 protein
  Ala111-Asn247 & Tyr112-Asn247, both with a C-terminal 6-His tag
• Accession #: Q60994
• N-terminal Sequence: Ala111 & Tyr112
• Protein/Peptide Type: Recombinant Proteins
• Gene: Adipoq
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Endotoxin Note: <1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• 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: 18-24 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 opening.
  • 3 months, -20 to -70 °C under sterile conditions after opening.
• Buffer: Supplied as a 0.2 μm filtered solution in PBS.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Notes

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

Alternate Names for Recombinant Mouse 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 137 amino acid (aa) residue globular domain of mouse Adiponectin shares 89% aa sequence identity with the human 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 (1119-AC)(3)

Publications using 1119-AC

• Koch C, Lowe C, Legler K, Benzler J, Boucsein A, Bottiger G, Grattan D, Williams L, Tups A Central adiponectin acutely improves glucose tolerance in male mice. Endocrinology, 2014;155(5):1806-16. 2014 [PMID: 24564394] (In Vivo, Mouse)
• Wen JP, Lv WS, Yang J, Nie AF, Cheng XB, Yang Y, Ge Y, Li XY, Ning G Globular adiponectin inhibits GnRH secretion from GT1-7 hypothalamic GnRH neurons by induction of hyperpolarization of membrane potential. Biochem. Biophys. Res. Commun., 2008;371(4):756-61. 2008 [PMID: 18466765] (Bioassay, Mouse)
• Fenton JI, Birmingham JM, Hursting SD, Hord NG Adiponectin blocks multiple signaling cascades associated with leptin-induced cell proliferation in Apc Min/+ colon epithelial cells. Int. J. Cancer, 2008;122(11):2437-45. 2008 [PMID: 18338750] (Bioassay, Mouse)

Bioinformatics

• Gene Symbol: Adipoq
• Uniprot:
  • Q60994(Mouse)