Recombinant Human gAdiponectin/gAcrp30 Protein, CF

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R&D Systems Recombinant Proteins and Enzymes
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Product Details
Citations (3)

Recombinant Human gAdiponectin/gAcrp30 Protein, CF Summary

Product Specifications

>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.01 EU per 1 μg of the protein by the LAL method.
Bioassay data are not available.
Mouse myeloma cell line, NS0-derived human gAdiponectin/gAcrp30 protein
Ala108-Asn244, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Predicted Molecular Mass
16.7 kDa (monomer)
19-20 kDa, reducing conditions

Product Datasheets

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Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.


Formulation Supplied as a 0.2 μm filtered solution in PBS.
Shipping The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage:
  • 4 months from date of receipt, 2 to 8 °C as supplied.
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Background: gAdiponectin/gAcrp30

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.
Entrez Gene IDs
9370 (Human); 11450 (Mouse); 246253 (Rat)
Alternate Names
gAcrp30; gAdiponectin; gAdipoQ; gApM1

Citations for Recombinant Human gAdiponectin/gAcrp30 Protein, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

3 Citations: Showing 1 - 3
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  1. Discovery of a novel potent peptide agonist to adiponectin receptor 1
    Authors: S Kim, Y Lee, JW Kim, YJ Son, MJ Ma, JH Um, ND Kim, SH Min, DI Kim, BB Kim
    PLoS ONE, 2018;13(6):e0199256.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  2. Apolipoprotein A-I stimulates AMP-activated protein kinase and improves glucose metabolism.
    Authors: Han R, Lai R, Ding Q, Wang Z, Luo X, Zhang Y, Cui G, He J, Liu W, Chen Y
    Diabetologia, 2007;50(9):1960-8.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  3. Chemokine induction by the adipocyte-derived cytokine adiponectin.
    Authors: Rovin BH, Song H
    Clin. Immunol., 2006;120(1):99-105.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay


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