• Purity

  >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

• Endotoxin Level

  <1.0 EU per 1 μg of the protein by the LAL method.  

• Activity

  Measured by its ability to induce TIMP-1 secretion by mouse macrophages. Kumada, M.     et al. (2004) Circulation     109:2046. The ED    ₅₀ for this effect is 5-20 μg/mL.

• Source

  Mouse myeloma cell line, NS0-derived Glu18-Asn247, with a C-terminal 6-His tag

• Accession #

• N-terminal Sequence    
  Analysis

  Glu18

• Structure / Form

  Oligomer

• Predicted Molecular Mass

  25.8 kDa

• SDS-PAGE

  28-38 kDa, under reducing conditions

Background: Adiponectin/Acrp30

Adiponectin, also known as Acrp30, is an adipocyte-derived protein with wide ranging paracrine and endocrine effects on metabolism and inflammation. It promotes adipocyte differentiation, fatty acid catabolism, and insulin sensitivity, and is negatively correlated with obesity, type 2 diabetes, and atherogenesis. In this context, adiponectin is an anti-inflammatory agent, but it exerts pro-inflammatory effects in nonmetabolic disorders such as rheumatoid arthritis and inflammatory bowel disease (1-3). Adiponectin interacts with the receptors AdipoR1 and AdipoR2, calreticulin, and Cadherin-13/T-Cadherin, as well as with several growth factors (4-7). Mature mouse adiponectin consists of a 66 amino acid (aa) N-terminal collagenous region and a 137 aa C-terminal C1q-like globular domain which can be cleaved by a leukocyte-derived elastase (8-10). Mature mouse adiponectin shares 83% and 91% amino acid (aa) sequence identity with human and rat adiponectin, respectively. Adiponectin associates into trimers that may assemble into medium molecular weight (MMW) hexamers and then into >300 kDa high molecular weight (HMW) oligomers (11-13). The glycosylation of four hydroxylated lysine residues in the collagenous domain is required for the intracellular formation of HMW complexes (14). The various multimeric forms of adiponectin exhibit distinct tissue specific and gender specific profiles and activities (13, 15).

• References:

1. Lara-Castro, C. et al. (2007) Curr. Opin. Lipidol. 18:263.

2. Tilg, H. and A.R. Moschen (2006) Nat. Rev. Immunol. 6:772.

3. Fantuzzi, G. (2008) J. Allergy Clin. Immunol. 121:326.

4. Yamauchi, T. et al. (2007) Nat. Med. 13:332.

5. Takemura, Y. et al. (2007) J. Clin. Invest. 117:375.

6. Hug, C. et al. (2004) Proc. Natl. Acad. Sci. 101:10308.

7. Wang, Y. et al. (2005) J. Biol. Chem. 280:18341.

8. Scherer, P.E. et al. (1995) J. Biol. Chem. 270:26746.

9. Hu, E. et al. (1996) J. Biol. Chem. 271:10697.

10. Waki, H. et al. (2005) Endocrinology 146:790.

11. Waki, H. et al. (2003) J. Biol. Chem. 278:40352.

12. Tsao, T.S. et al. (2003) J. Biol. Chem. 278:50810.

13. Wang, Y. et al. (2008) Biochem. J. 409:623.

14. Wang, H. et al. (2006) J. Biol. Chem. 281:16391.

15. Pajvani, U.B. et al. (2003) J. Biol. Chem. 278:9073.

• Entrez Gene IDs:

  9370 (Human); 11450 (Mouse); 246253 (Rat)

• Alternate Names:

  ACDC; Acrp30; ACRP30ADPN; adipocyte, C1Q and collagen domain containing; Adiponectin; adiponectin, C1Q and collagen domain containing; AdipoQ; ADIPQTL1; ApM1; apM-1; APM1APM-1; C1q and collagen domain-containing protein; GBP28; GBP28apM1; Gelatin-binding protein