Recombinant Mouse gAdiponectin/gAcrp30 Protein, CF

Name: Recombinant Mouse gAdiponectin/gAcrp30 Protein, CF
Brand: R&D Systems
SKU: 1119-AC

R&D Systems, Inc. a Bio-Techne Brand

Catalog # 1119-AC

Citations (3)

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Key Product Details

Source:	NS0
Accession #:	Q60994
Applications:	Bioactivity

View Full Technical Details for Recombinant Mouse gAdiponectin/gAcrp30 Protein, CF

Product Specifications for Recombinant Mouse gAdiponectin/gAcrp30 Protein, CF

Source	Mouse myeloma cell line, NS0-derived mouse gAdiponectin/gAcrp30 protein Ala111-Asn247 & Tyr112-Asn247, both with a C-terminal 6-His tag
Purity	>95%, 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.
N-terminal sequence Analysis	Ala111 & Tyr112
Predicted Molecular Mass	16.7 kDa (monomer)
SDS-PAGE	18-24 kDa, reducing conditions
Activity	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.

Formulation, Preparation and Storage

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.

1119-AC

Formulation	Supplied as a 0.2 μm filtered solution in PBS.
Shipping	The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.

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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 137 amino acid (aa) residue globular domain of mouse Adiponectin shares 89% aa sequence identity with the human homologue.

Item	Value
References	Scherer, P.E. et al. (1995) J. Biol. Chem. 270:26746. Hu, E. et al. (1996) J. Biol. Chem. 271:10697. Maeda, K. et al. (1996) Biochem. Biophys. Res. Commun. 221:286. Tsao, T-S. et al. (2002) J. Biol. Chem. 277:29359. Fruebis, J. et al. (2001) Proc. Natl. Acad. Sci. USA 98:2005. Berg, A.H. et al. (2001) Nature Med. 7:947. Pajvani, U.T. et al. (2003) J. Biol. Chem. 278:9073. Tomas, E. et al. (2002) Proc. Natl. Acad. Sci. USA 99:16309. Tsao, T.S. et al. (2003) J. Biol. Chem. Sept. 30 [Epub ahead of print]. Wang, Y. et al. (2002) J. Biol. Chem. 277:19521. Sato, C. et al. (2001) J. Biol. Chem. 276:28849. Yamauchi, T. et al. (2003) Nature 423:762. Yokota, T. et al. (2000) Blood 96:1723.
Entrez Gene IDs	9370 (Human); 11450 (Mouse); 246253 (Rat)
Alternate Names	gAcrp30, gAdipoQ, gAdiponectin, gApM1

Citations for Recombinant Mouse gAdiponectin/gAcrp30 Protein, CF (3)

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Citations are publications that use Bio-Techne products. Selected citations for Recombinant Mouse gAdiponectin/gAcrp30 Protein, CF include:

Species: Mouse
Sample Types: In Vivo
Applications: In Vivo

Koch C et al. (2014), Central adiponectin acutely improves glucose tolerance in male mice. Endocrinology, 155(5):1806-16.
PMID: 24564394
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay

Fenton JI et al. (2008), Adiponectin blocks multiple signaling cascades associated with leptin-induced cell proliferation in Apc Min/+ colon epithelial cells. Int. J. Cancer, 122(11):2437-45.
PMID: 18338750
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay

Wen JP et al. (2008), Globular adiponectin inhibits GnRH secretion from GT1-7 hypothalamic GnRH neurons by induction of hyperpolarization of membrane potential. Biochem. Biophys. Res. Commun., 371(4):756-61.
PMID: 18466765

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