Adiponectin Human, Trimeric form HEK293

Cat. No.	Size	Price
RD172091100	0.1 mg

Technical Data

Type

Recombinant protein

Amino Acid Sequence

ETTTQGPGVLLPLPKGAATGWMAGIPGHPGHNGAPGRDGRDGTPGEKGEKGDPGLIGPKGDIGETGVPGAEGPRGFPGIQGRKGEPGEGAYVYRSAFSVGLETYVTIPNMPIRFTKIFYNQQNHYDGSTGKFHCNIPGLYYFAYHITVYMKDVKVSLFKKDKAMLFTYDQYQENNVDQASGSVLLHLEVGDQVWLQVYGEGERNGLYADNDNDSTFTGFLLYHDTNDYKDDDDK

Source

HEK293

Purity

Purity as determined by densitometric image analysis: >95%

SDS-PAGE Gel

12% SDS-PAGE separation of Human Adiponectin, Trimeric form
1. M.W. marker – 14, 21, 31, 45, 66, 97 kDa
2. reduced and heated sample, 5μg/lane
3. non-reduced and non-heated sample, 5μg/lane

Biological Activity

The biological activity of Adiponectin is measured by its ability to inhibit proliferation of mouse 3T3 fibroblasts stimulated by PDGF. The ED50 for the effect is typically 5-15 μg/mL.

Endotoxin

< 0.1 EU/ug

Formulation

Filtered (0.4 μm) and lyophilized from 0.5 mg/ml solution in phosphate buffered saline pH 7.5

Reconstitution

Add deionized water to prepare a working stock solution of approximately 0.5 mg/mL and let the lyophilized pellet dissolve completely.

Applications

Western blotting, ELISA, Cell culture and/or animal studies

Shipping

At ambient temperature. Upon receipt, store the product at the temperature recommended below.

Storage/Expiration

Store the lyophilized protein at -80 °C. Lyophilized protein remains stable until the expiry date when stored at -80 °C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at -80 °C for long term storage. Reconstituted protein can be stored at 4 °C for a week.

Quality Control Test

BCA to determine quantity of the protein.

SDS PAGE to determine purity of the protein.

GFC to determine purity of the protein.

LAL to determine quantity of endotoxin.

Summary

Research topic

Chronic renal failure, Coronary artery disease, Diabetology - Other Relevant Products, Energy metabolism and body weight regulation

Summary

Adiponectin, also referred to as Acrp30, AdipoQ and GBP-28, is a recently discovered 244 aminoacid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells. The protein belongs to the soluble defence collagen superfamily; it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. Adiponectin forms homotrimers, which are the building blocks for higher order complexes found circulating in serum. Together, these complexes make up approximately 0.01% of total serum protein. Adiponectin receptors AdipoR1 and AdipoR2 have been recently cloned; AdipoR1 is abundantly expressed in skeletal muscle, whereas AdipoR2 is predominantly expressed in the liver. Paradoxically, adipose tissue-expressed adiponectin levels are inversely related to the degree of adiposity. Adiponectin concentrations correlate negatively with glucose, insulin, triglyceride concentrations, liver fat content and body mass index and positively with high-density lipoprotein-cholesterol levels, hepatic insulin sensitivity and insulin-stimulated glucose disposal. Adiponectin has been shown to increase insulin sensitivity and decrease plasma glucose by increasing tissue fat oxidation. Of particular interest is that low adiponectin serum levels predict type 2 diabetes independent of other risk factors. Adiponectin also inhibits the inflammatory processes of atherosclerosis suppressing the expression of adhesion and cytokine molecules in vascular endothelial cells and macrophages, respectively. This adipokine plays a role as a scaffold of newly formed collagen in myocardial remodelling after ischaemic injury and also stimulates angiogenesis by promoting cross-talk between AMP-activated protein kinase and Akt signalling in endothelial cells. Low serum adiponectin levels are found in patients with coronary artery disease. Moreover, high circulating levels of adiponectin are associated with decreased risk of myocardial infarction, independent of other factors. Altogether, adiponectin has the potential to become a clinically relevant parameter to be measured routinely in subjects at risk for type 2 diabetes, atherosclerosis and the metabolic syndrome.

Product References (3)

References

Demolombe V, de Brevern AG, Felicori L, NGuyen C, Machado de Avila RA, Valera L, Jardin-Watelet B, Lavigne G, Lebreton A, Molina F, Moreau V. PEPOP 2.0: new approaches to mimic non-continuous epitopes. BMC Bioinformatics. 2019 Jul 11;20(1):387. doi: 10.1186/s12859-019-2867-5. PubMed PMID: 31296178. PubMed CentralPMCID: PMC6625012. See more on PubMed
Barb D, Neuwirth A, Mantzoros CS, Balk SP. Adiponectin signals in prostate cancer cells through Akt to activate the mammalian target of rapamycin pathway. Endocr Relat Cancer. 2007 Dec;14(4):995-1005. doi: 10.1677/ERC-06-0091. PubMed PMID: 18045951. See more on PubMed
Haugen F, Drevon CA. Activation of nuclear factor-kappaB by high molecular weight and globular adiponectin. Endocrinology. 2007 Nov;148(11):5478-86. doi: 10.1210/en.2007-0370. Epub 2007 Aug 16. PubMed PMID: 17702846. See more on PubMed

Summary References (17)

References to Adiponectin

Lam KS, Xu A. Adiponectin: protection of the endothelium. Curr Diab Rep. 2005, 5, 254–259.
Ding X, Saxena NK, Lin S, Xu A, Srinivasan S, Anania FA. The roles of leptin and adiponectin: a novel paradigm in adipocytokine regulation of liver fibrosis and stellate cell biology. Am J Pathol. 2005, 166, 1655–1669.
Xu A, Chan KW, Hoo RL, Wang Y, Tan KC, Zhang J, Chen B, Lam MC, Tse C, Cooper GJ, Lam KS. Testosterone selectively reduces the high molecular weight form of adiponectin by inhibiting its secretion from adipocytes. J Biol Chem. 2005, 280, 18073–18080.
Wang Y, Lam KS, Xu JY, Lu G, Xu LY, Cooper GJ, Xu A. Adiponectin inhibits cell proliferation by interacting with several growth factors in an oligomerization-dependent manner. J Biol Chem. 2005, 280, 18341–18347.
Ouchi N, Kobayashi H, Kihara S, Kumada M, Sato K, Inoue T, Funahashi T, Walsh K. Adiponectin stimulates angiogenesis by promoting cross-talk between AMP-activated protein kinase and Akt signaling in endothelial cells. J Biol Chem. 2004, 279, 1304–1309.
Ishikawa Y, Akasaka Y, Ishii T, Yoda-Murakami M, Choi-Miura NH, Tomita M, Ito K, Zhang L, Akishima Y, Ishihara M, Muramatsu M, Taniyama M. Changes in the distribution pattern of gelatinbinding protein of 28 kDa (adiponectin) in myocardial remodelling after ischaemic injury. Histopathology. 2003, 42, 43–52.
Diez JJ, Iglesias P. The role of the novel adipocyte-derived hormone adiponectin in human disease. Eur J Endocrinol. 2003, 148, 293–300.
Waki H, Yamauchi T, Kamon J, Ito Y, Uchida S, Kita S, Hara K, Hada Y, Vasseur F, Froguel P, Kimura S, Nagai R, Kadowaki T. Impaired multimerization of human adiponectin mutants associated with diabetes. Molecular structure and multimer formation of adiponectin. J Biol Chem. 2003, 278, 40352–40363.
Yamauchi T, Kamon J, Ito Y, Tsuchida A, Yokomizo T, Kita S, Sugiyama T, Miyagishi M, Hara K, Tsunoda M, Murakami K, Ohteki T, Uchida S, Takekawa S, Waki H, Tsuno NH, Shibata Y, Terauchi Y, Froguel P, Tobe K, Koyasu S, Taira K, Kitamura T, Shimizu T, Nagai R, Kadowaki T. Cloning of adiponectin receptors that mediate antidiabetic metabolic effects. Nature. 2003, 423, 762–769.
Yamauchi T, Kamon J, Waki H, Imai Y, Shimozawa N, Hioki K, Uchida S, Ito Y, Takakuwa K, Matsui J, Takata M, Eto K, Terauchi Y, Komeda K, Tsunoda M, Murakami K, Ohnishi Y, Naitoh T, Yamamura K, Ueyama Y, Froguel P, Kimura S, Nagai R, Kadowaki T. Globular adiponectin protected ob/ob mice from diabetes and ApoE-deficient mice from atherosclerosis. J Biol Chem. 2003, 278, 2461–2468.
Daimon M, Oizumi T, Saitoh T, Kameda W, Hirata A, Yamaguchi H, Ohnuma H, Igarashi M, Tominaga M, Kato T. Decreased serum levels of adiponectin are a risk factor for the progression to type 2 diabetes in the Japanese Population: the Funagata study. Diabetes Care. 2003 Jul;26(7):2015–20.
Pajvani UB, Du X, Combs TP, Berg AH, Rajala MW, Schulthess T, Engel J, Brownlee M, Scherer PE. Structure-function studies of the adipocyte-secreted hormone Acrp30/adiponectin. Implications for metabolic regulation and bioactivity. J Biol Chem. 2003, 278, 9073–9085.
Spranger J, Kroke A, Mohlig M, Bergmann MM, Ristow M, Boeing H, Pfeiffer AF. Adiponectin and protection against type 2 diabetes mellitus. Lancet. 2003, 361, 226–228.
Kondo H, Shimomura I, Matsukawa Y, Kumada M, Takahashi M, Matsuda M, Ouchi N, Kihara S, Kawamoto T, Sumitsuji S, Funahashi T, Matsuzawa Y. Association of adiponectin mutation with type 2 diabetes: a candidate gene for the insulin resistance syndrome. Diabetes. 2002, 51, 2325–2328.
Wang Y, Xu A, Knight C, Xu LY, Cooper GJ. Hydroxylation and glycosylation of the four conserved lysine residues in the collagenous domain of adiponectin. Potential role in the modulation of its insulin-sensitizing activity. J Biol Chem. 2002, 277, 19521–19529.
Tsao TS, Lodish HF, Fruebis J. ACRP30, a new hormone controlling fat and glucose metabolism. Eur J Pharmacol. 2002, 440, 213–21.
Das K, Lin Y, Widen E, Zhang

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