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Adiponectin Human HEK293

  • Regulatory status:RUO
  • Type:Recombinant protein
  • Source:HEK293
  • Other names:Adipocyte C1q and collagen domain-containing protein, Adipocyte complement-related 30 kDa protein, ACRP30, Adipose most abundant gene transcript 1 protein, apM-1, Gelatin-binding protein, ADIPOQ, ACDC, APM1, GBP28
  • Species:Human
Cat. No. Size Price
1 - 4 pcs / 5 - 9 pcs / 10+ pcs


RD172023100 0.1 mg $618 / $549 / On request
PubMed Product Details
Technical Data

Type

Recombinant protein

Description

Total 234 AA. MW 25.5 kDa (calculated). UniProtKB acc.no. Q15848 (Glu19 – Asn244). C-Terminal tag (8 extra AA).

Amino Acid Sequence

ETTTQGPGVLLPLPKGACTGWMAGIPGHPGHNGAPGRDGRDGTPGEKGEKGDPGLIGPKGDIGETGVPGAEGPRGFPGIQGRKGEPGEGAYVYRSAFSVGLETYVTIPNMPIRFTKIFYNQQNHYDGSTGKFHCNIPGLYYFAYHITVYMKDVKVSLFKKDKAMLFTYDQYQENNVDQASGSVLLHLEVGDQVWLQVYGEGERNGLYADNDNDSTFTGFLLYHDTNDYKDDDDK

Glu 1 to Gln 5 were confirmed by N-terminal sequencing

Source

HEK293

Purity

˃ 90 % by SDS-PAGE

SDS-PAGE Gel

12% SDS-PAGE separation of Human A diponectin

  1. M.w. marker – 14, 21, 31, 45, 66, 97 kDa
  2. reduced and heated sample, 2.5μg/lane
  3. non-reduced and non-heated sample, 2.5μg/lane

Endotoxin

< 1.0 EU/μg

Formulation

Filtered (0.4 μm) and lyophilized from 0.5 mg/mL solution in phosphate buffered saline, pH 7.4

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

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. Endotoxin level determination.

Note

This product is intended for research use only.

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 (17)

References

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  • Pisto P, Ukkola O, Santaniemi M, Kesäniemi YA. Plasma adiponectin--an independent indicator of liver fat accumulation. Metabolism. 2011 Nov;60(11):1515-20. doi: 10.1016/j.metabol.2011.03.009. Epub 2011 May 11. PubMed PMID: 21565369. See more on PubMed
  • Kitajima K, Miura S, Yamauchi T, Uehara Y, Kiya Y, Rye KA, Kadowaki T, Saku K. Possibility of increasing cholesterol efflux by adiponectin and its receptors through the ATP binding cassette transporter A1 in HEK293T cells. Biochem Biophys Res Commun. 2011 Jul 29;411(2):305-11. doi: 10.1016/j.bbrc.2011.06.131. Epub 2011 Jun 28. PubMed PMID: 21740892. See more on PubMed
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  • Conde J, Gomez R, Bianco G, Scotece M, Lear P, Dieguez C, Gomez-Reino J, Lago F, Gualillo O. Expanding the adipokine network in cartilage: identification and regulation of novel factors in human and murine chondrocytes. Ann Rheum Dis. 2011 Mar;70(3):551-9. doi: 10.1136/ard.2010.132399. Epub 2011 Jan 7. PubMed PMID: 21216818. See more on PubMed
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  • Murdolo G, Hammarstedt A, Schmelz M, Jansson PA, Smith U. Acute hyperinsulinemia differentially regulates interstitial and circulating adiponectin oligomeric pattern in lean and insulin-resistant, obese individuals. J Clin Endocrinol Metab. 2009 Nov;94(11):4508-16. doi: 10.1210/jc.2009-0431. Epub 2009 Oct 9. PubMed PMID: 19820029. See more on PubMed
  • Sell H, Laurencikiene J, Taube A, Eckardt K, Cramer A, Horrighs A, Arner P, Eckel J. Chemerin is a novel adipocyte-derived factor inducing insulin resistance in primary human skeletal muscle cells. Diabetes. 2009 Dec;58(12):2731-40. doi: 10.2337/db09-0277. Epub 2009 Aug 31. PubMed PMID: 19720798. PubMed CentralPMCID: PMC2780878. See more on PubMed
  • Folco EJ, Rocha VZ, López-Ilasaca M, Libby P. Adiponectin inhibits pro-inflammatory signaling in human macrophages independent of interleukin-10. J Biol Chem. 2009 Sep 18;284(38):25569-75. doi: 10.1074/jbc.M109.019786. Epub 2009 Jul 18. PubMed PMID: 19617629. PubMed CentralPMCID: PMC2757958. See more on PubMed
  • Greenstein AS, Khavandi K, Withers SB, Sonoyama K, Clancy O, Jeziorska M, Laing I, Yates AP, Pemberton PW, Malik RA, Heagerty AM. Local inflammation and hypoxia abolish the protective anticontractile properties of perivascular fat in obese patients. Circulation. 2009 Mar 31;119(12):1661-70. doi: 10.1161/CIRCULATIONAHA.108.821181. Epub 2009 Mar 16. PubMed PMID: 19289637. See more on PubMed
  • Rodriguez PC, Ernstoff MS, Hernandez C, Atkins M, Zabaleta J, Sierra R, Ochoa AC. Arginase I-producing myeloid-derived suppressor cells in renal cell carcinoma are a subpopulation of activated granulocytes. Cancer Res. 2009 Feb 15;69(4):1553-60. doi: 10.1158/0008-5472.CAN-08-1921. Epub 2009 Feb 5. PubMed PMID: 19201693. PubMed CentralPMCID: PMC2900845. See more on PubMed
  • Kamio N, Akifusa S, Yamaguchi N, Yamashita Y. Induction of granulocyte colony-stimulating factor by globular adiponectin via the MEK-ERK pathway. Mol Cell Endocrinol. 2008 Sep 24;292(1-2):20-5. doi: 10.1016/j.mce.2008.05.002. Epub 2008 May 9. PubMed PMID: 18555587. See more on PubMed
  • Jalovaara K, Santaniemi M, Timonen M, Jokelainen J, Kesäniemi YA, Ukkola O, Keinänen-Kiukaanniemi S, Rajala U. Low serum adiponectin level as a predictor of impaired glucose regulation and type 2 diabetes mellitus in a middle-aged Finnish population. Metabolism. 2008 Aug;57(8):1130-4. doi: 10.1016/j.metabol.2008.03.019. PubMed PMID: 18640392. See more on PubMed
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Summary References (17)

References to Adiponectin

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  • 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.
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  • 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.
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  • 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.
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  • 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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