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 Adiponectin/Acrp30 protein Glu18-Asn247, with a C-terminal 6-His tag
>90%, 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
Dilutions
Bioactivity
Theoretical MW
25.8 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
28-38 kDa, under reducing conditions
Publications
Read Publications using 5095-AC in the following applications:
6 months from date of receipt, 2 to 8 °C as supplied.
Buffer
Supplied as a 0.2 μm filtered solution in PBS.
Purity
>90%, 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 Adiponectin/Acrp30 Protein, CF
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
Background
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).
Lara-Castro, C. et al. (2007) Curr. Opin. Lipidol. 18:263.
Tilg, H. and A.R. Moschen (2006) Nat. Rev. Immunol. 6:772.
Fantuzzi, G. (2008) J. Allergy Clin. Immunol. 121:326.
Yamauchi, T. et al. (2007) Nat. Med. 13:332.
Takemura, Y. et al. (2007) J. Clin. Invest. 117:375.
Hug, C. et al. (2004) Proc. Natl. Acad. Sci. 101:10308.
Wang, Y. et al. (2005) J. Biol. Chem. 280:18341.
Scherer, P.E. et al. (1995) J. Biol. Chem. 270:26746.
Hu, E. et al. (1996) J. Biol. Chem. 271:10697.
Waki, H. et al. (2005) Endocrinology 146:790.
Waki, H. et al. (2003) J. Biol. Chem. 278:40352.
Tsao, T.S. et al. (2003) J. Biol. Chem. 278:50810.
Wang, Y. et al. (2008) Biochem. J. 409:623.
Wang, H. et al. (2006) J. Biol. Chem. 281:16391.
Pajvani, U.B. et al. (2003) J. Biol. Chem. 278:9073.
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