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Adiponectin (HEK) Murine,
Rabbit Polyclonal Antibody

Product of BioVendor
Other names: Acrp30, GBP28, AdipoQ
Cat. No.: RD281023100
Size: 0.1 mg |
Cat. No.: RD281023100+
Size: 10 x 0.1 mg |
Files: Datasheet PDF MSDS
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Source of Antigen

HEK293

Host

Rabbit

Preparation

The antibody was raised in rabbits by immunization with the recombinant Murine Adiponectin.

Amino Acid Sequence

EDDVTTTEEL APALVPPPKG TCAGWMAGIP GHPGHNGTPG RDGRDGTPGE KGEKGDAGLL GPKGETGDVG MTGAEGPRGF PGTPGRKGEP GEAAYMYRSA FSVGLETRVT VPNVPIRFTK IFYNQQNHYD GSTGKFYCNI PGLYYFSYHI TVYMKDVKVS LFKKDKAVLF TYDQYQEKNV DQASGSVLLH LEVGDQVWLQ VYGDGDHNGL YADNVNDSTF TGFLLYHDTN DYKDDDDK

Species Reactivity

Mouse
Not yet tested in other species.

Purification Method

Immunoaffinity chromatography on a column with immobilized mouse recombinant Adiponectin.

Antibody Content

0.1 mg (determined by BCA method)

Formulation

Sterile filtered and lyophilized from 1 mg/ml in 0.05 M phosphate buffer, 0.1 M NaCl, pH 7.2. AZIDE FREE.

Reconstitution

Add 0.1 ml of deionized water and let the lyophilized pellet dissolve completely. Slight turbidity may occur after reconstitution, which does not affect activity of the antibody. In this case clarify the solution by centrifugation.

Storage/Stability

The lyophilized antibody remains stable and fully active until the expiry date when stored at –20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles and store frozen at –80°C. Reconstituted antibody can be stored at 4°C for a limited period of time; it does not show decline in activity after two weeks at 4°C.

Quality Control Test

Indirect ELISA – to determine titer of the antibody
SDS PAGE – to determine purity of the antibody

Applications

ELISA, Western blotting

References to this Product

  • Bauche IB, El Mkadem SA, Pottier AM, Senou M, Many MC, Rezsohazy R, Penicaud L, Maeda N, Funahashi T, Brichard SM . Overexpression of adiponectin targeted to adipose tissue in transgenic mice: impaired adipocyte differentiation. Endocrinology . Jan 4 (2007)

References

  • Berg AH, Combs TP, Scherer PE. ACRP30/adiponectin: an adipokine regulating glucose and lipid metabolism. Trends Endocrinol Metab. 2002;13:84-89.
  • 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 May 6;280(18):18341-7.
  • Okamoto Y, Kihara S, et al. Adiponectin reduces atherosclerosis in apolipoprotein E-deficient mice. Circulation. 2002;106:2767-2770.
  • Yamauchi T, Kamon J, Minokoshi Y, Ito Y, Waki H, Uchida S, Yamashita S, Noda M, Kita S, Ueki K, Eto K, Akanuma Y, Froguel P, Foufelle F, Ferre P, Carling D, Kimura S, Nagai R, Kahn BB, Kadowaki T. Adiponectin stimulates glucose utilization and fatty-acid oxidation by activating AMP-activated protein kinase. Nat Med. 2002; 8:1288-1295.
  • Chen H, Montagnani M, Funahashi T, Shimomura I, Quon MJ. Adiponectin stimulates production of nitric oxide in vascular endothelial cells. J Biol Chem. 2003;278:45021-45026.
  • Waki H, Yamauchi T, Kamon J, Kita S, Ito Y, Hada Y, Uchida S, Tsuchida A, Takekawa S, Kadowaki T. Generation of globular fragment of adiponectin by leukocyte elastase secreted by monocytic cell line THP-1. Endocrinology. 2005 Feb;146(2):790-6. Epub 2004 Nov 4.
  • 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.
  • 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.
  • Matsuda M, Shimomura I, et al. Role of adiponectin in preventing vascular stenosis. The missing link of adipo-vascular axis. J Biol Chem. 2002;277:37487-37491.
  • Kobayashi H, Ouchi N, Kihara S, Walsh K, Kumada M, Abe Y, Funahashi T, Matsuzawa Y, Ferre P. Selective Suppression of Endothelial Cell Apoptosis by the High Molecular Weight.
  • Kobayashi H, Ouchi N, Kihara S, Walsh K, Kumada M, Abe Y, et al. Selective suppression of endothelial cell apoptosis by the high molecular weight form of adiponectin. Circulation research. 2004 Mar 5;94(4):e27-31.
  • 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 fpr metabolic regulation and bioactivity. J Biol Chem. 2003; 278:9073-85.
  • 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 fpr metabolic regulation and bioactivity. J Biol Chem. 2003; 278:9073-85.
  • Berg AH, Combs TP, Du X, Brownlee M, Scherer PE. The adipocyte-secreted protein Acrp30 enhances hepatic insulin action. Nat Med. 2001; 7:947-953.
  • Xu A, Wang Y, Keshaw H, Xu LY, Lam KS, Cooper GJ. The fat-derived hormone adiponectin alleviates alcoholic and nonalcoholic fatty liver diseases in mice. J Clin Invest. 2003; 112:91-100.
  • Yamauchi T, Kamon J, et al. The fat-derived hormone adiponectin reverses insulin resistance associated with both lipoatrophy and obesity. Nat Med. 2001;7:941-946.

Note

This product is for research use only.



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