Adiponectin Recombinant Protein | Adipoq recombinant protein

Recombinant Mouse Adiponectin

Cat. Num. AAA718232

• Gene Names: Adipoq; Ad; APN; Acdc; apM1; 30kDa; GBP28; adipo; Acrp30
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Adiponectin; Recombinant Mouse Adiponectin; 30 kDa adipocyte complement-related protein; Adipocyte complement-related 30 kDa protein; ACRP30; Adipocyte; C1q and collagen domain-containing protein; Adipocyte-specific protein AdipoQ; Adipoq recombinant protein

• Host: E Coli
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence Positions: 18-247aa; Full Length
• Sequence: EDDVTTTEELAPALVPPPKGTCAGWMAGIPGHPGHNGTPGRDGRDGTPGEKGEKGDAGLLGPKGETGDVGMTGAEGPRGFPGTPGRKGEPGEAAYVYRSAFSVGLETRVTVPNVPIRFTKIFYNQQNHYDGSTGKFYCNIPGLYYFSYHITVYMKDVKVSLFKKDKAVLFTYDQYQEKNVDQASGSVLLHLEVGDQVWLQVYGDGDHNGLYADNVNDSTFTGFLLYHDTN
• Sequence Length: 247

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for Adipoq recombinant protein

Important adipokine involved in the control of fat metabolism and insulin sensitivity, with direct anti-diabetic, anti-atherogenic and anti-inflammatory activities. Stimulates AMPK phosphorylation and activation in the liver and the skeletal muscle, enhancing glucose utilization and fatty-acid combustion. Antagonizes TNF-alpha by negatively regulating its expression in various tissues such as liver and macrophages, and also by counteracting its effects. Inhibits endothelial NF-kappa-B signaling through a cAMP-dependent pathway. May play a role in cell growth, angiogenesis and tissue remodeling by binding and sequestering various growth factors with distinct binding affinities, depending on the type of complex, LMW, MMW or HMW.

References

A novel serum protein similar to C1q, produced exclusively in adipocytes.Scherer P.E., Williams S., Fogliano M., Baldini G., Lodish H.F.J. Biol. Chem. 270:26746-26749(1995) AdipoQ is a novel adipose-specific gene dysregulated in obesity.Hu E., Liang P., Spiegelman B.M.J. Biol. Chem. 271:10697-10703(1996) Chromosomal localization, expression pattern, and promoter analysis of the mouse gene encoding adipocyte-specific secretory protein Acrp30.Das K., Lin Y., Widen E., Zhang Y., Scherer P.E.Biochem. Biophys. Res. Commun. 280:1120-1129(2001) Cloning of murine adipocyte complement-related protein of 30 KDa from white adipose tissue.Wang S.F., Han P.Z., Mu C.J., Zhao M.H. Lineage-specific biology revealed by a finished genome assembly of the mouse.Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.PLoS Biol. 7:E1000112-E1000112(2009) Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. 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.Wang Y., Xu A., Knight C., Xu L.Y., Cooper G.J.S.J. Biol. Chem. 277:19521-19529(2002) Identification and adipocyte differentiation-dependent expression of the unique disialic acid residue in an adipose tissue-specific glycoprotein, adipo Q.Sato C., Yasukawa Z., Honda N., Matsuda T., Kitajima K.J. Biol. Chem. 276:28849-28856(2001) The fat-derived hormone adiponectin reverses insulin resistance associated with both lipoatrophy and obesity.Yamauchi T., Kamon J., Waki H., Terauchi Y., Kubota N., Hara K., Mori Y., Ide T., Murakami K., Tsuboyama-Kasaoka N., Ezaki O., Akanuma Y., Gavrilova O., Vinson C., Reitman M.L., Kagechika H., Shudo K., Yoda M., Nakano Y., Tobe K., Nagai R., Kimura S., Tomita M., Froguel P., Kadowaki T.Nat. Med. 7:941-946(2001) The adipocyte-secreted protein Acrp30 enhances hepatic insulin action.Berg A.H., Combs T.P., Du X., Brownlee M., Scherer P.E.Nat. Med. 7:947-953(2001) The fat-derived hormone adiponectin alleviates alcoholic and nonalcoholic fatty liver diseases in mice.Xu A., Wang Y., Keshaw H., Xu L.Y., Lam K.S.L., Cooper G.J.S.J. Clin. Invest. 112:91-100(2003) Testosterone selectively reduces the high molecular weight form of adiponectin by inhibiting its secretion from adipocytes.Xu A., Chan K.W., Hoo R.L.C., Wang Y., Tan K.C.B., Zhang J., Chen B., Lam M.C., Tse C., Cooper G.J.S., Lam K.S.L.J. Biol. Chem. 280:18073-18080(2005) Adiponectin inhibits cell proliferation by interacting with several growth factors in an oligomerization-dependent manner.Wang Y., Lam K.S.L., Xu J.Y., Lu G., Xu L.Y., Cooper G.J.S., Xu A.J. Biol. Chem. 280:18341-18347(2005) Post-translational modifications of the four conserved lysine residues within the collagenous domain of adiponectin are required for the formation of its high molecular weight oligomeric complex.Wang Y., Lam K.S.L., Chan L., Chan K.W., Lam J.B.B., Lam M.C., Hoo R.C.L., Mak W.W.N., Cooper G.J.S., Xu A.J. Biol. Chem. 281:16391-16400(2006) Identification and characterization of CTRP9, a novel secreted glycoprotein, from adipose tissue that reduces serum glucose in mice and forms heterotrimers with adiponectin.Wong G.W., Krawczyk S.A., Kitidis-Mitrokostas C., Ge G., Spooner E., Hug C., Gimeno R., Lodish H.F.FASEB J. 23:241-258(2009) Sialic acid modification of adiponectin is not required for multimerization or secretion but determines half-life in circulation.Richards A.A., Colgrave M.L., Zhang J., Webster J., Simpson F., Preston E., Wilks D., Hoehn K.L., Stephenson M., Macdonald G.A., Prins J.B., Cooney G.J., Xu A., Whitehead J.P.Mol. Endocrinol. 24:229-239(2010) The crystal structure of a complement-1q family protein suggests an evolutionary link to tumor necrosis factor.Shapiro L., Scherer P.E.Curr. Biol. 8:335-338(1998)

NCBI and Uniprot Product Information

• NCBI GI #: 87252711
• NCBI GeneID: 11450
• NCBI Accession #: NP_033735.3
• NCBI GenBank Nucleotide #: NM_009605.4
• UniProt Accession #: Q60994; Q62400; Q6GTX4; Q9DC68
• Molecular Weight: 20.5 kDa
• NCBI Official Full Name: adiponectin
• NCBI Official Synonym Full Names: adiponectin, C1Q and collagen domain containing
• NCBI Official Symbol: Adipoq
• NCBI Official Synonym Symbols: Ad; APN; Acdc; apM1; 30kDa; GBP28; adipo; Acrp30
• NCBI Protein Information: adiponectin
• UniProt Protein Name: Adiponectin
• Protein Family: Adiponectin
• UniProt Gene Name: Adipoq
• UniProt Synonym Gene Names: Acdc; Acrp30; Apm1; ACRP30
• UniProt Entry Name: ADIPO_MOUSE

Uniprot Description

adiponectin: Important adipokine involved in the control of fat metabolism and insulin sensitivity, with direct anti-diabetic, anti-atherogenic and anti-inflammatory activities. Stimulates AMPK phosphorylation and activation in the liver and the skeletal muscle, enhancing glucose utilization and fatty-acid combustion. Antagonizes TNF-alpha by negatively regulating its expression in various tissues such as liver and macrophages, and also by counteracting its effects. Inhibits endothelial NF-kappa-B signaling through a cAMP-dependent pathway. May play a role in cell growth, angiogenesis and tissue remodeling by binding and sequestering various growth factors with distinct binding affinities, depending on the type of complex, LMW, MMW or HMW. Homomultimer. Forms trimers, hexamers and 12- to 18-mers. The trimers (low molecular weight complexes / LMW) are assembled via non-covalent interactions of the collagen-like domains in a triple helix and hydrophobic interactions within the globular C1q domain. Several trimers can associate to form disulfide-linked hexamers (middle molecular weight complexes / MMW) and larger complexes (higher molecular weight / HMW). The HMW-complex assembly may rely aditionally on lysine hydroxylation and glycosylation. LMW, MMW and HMW complexes bind to HBEGF, MMW and HMW complexes bind to PDGFB, and HMW complex binds to FGF2. Interacts with CTRP9A via the C1q domain (heterotrimeric complex). Synthesized exclusively by adipocytes and secreted into plasma.

Protein type: Hormone; Endoplasmic reticulum; Secreted, signal peptide; Secreted

Cellular Component: cell surface; collagen; endoplasmic reticulum; extracellular region; extracellular space; protein complex

Molecular Function: hormone activity; identical protein binding; protein binding; protein homodimerization activity; receptor binding; sialic acid binding

Biological Process: adiponectin-mediated signaling pathway; brown fat cell differentiation; cellular response to insulin stimulus; fatty acid beta-oxidation; fatty acid oxidation; glucose homeostasis; glucose metabolic process; membrane depolarization; membrane hyperpolarization; negative regulation of blood pressure; negative regulation of cell migration; negative regulation of fat cell differentiation; negative regulation of gluconeogenesis; negative regulation of granulocyte differentiation; negative regulation of heterotypic cell-cell adhesion; negative regulation of hormone secretion; negative regulation of I-kappaB kinase/NF-kappaB cascade; negative regulation of inflammatory response; negative regulation of low-density lipoprotein receptor biosynthetic process; negative regulation of macrophage differentiation; negative regulation of MAP kinase activity; negative regulation of phagocytosis; negative regulation of protein amino acid autophosphorylation; negative regulation of smooth muscle cell migration; negative regulation of smooth muscle cell proliferation; negative regulation of synaptic transmission; negative regulation of transcription, DNA-dependent; negative regulation of tumor necrosis factor production; positive regulation of blood pressure; positive regulation of cellular protein metabolic process; positive regulation of fatty acid metabolic process; positive regulation of glucose import; positive regulation of I-kappaB kinase/NF-kappaB cascade; positive regulation of interleukin-8 production; positive regulation of myeloid cell apoptosis; positive regulation of peptidyl-tyrosine phosphorylation; positive regulation of protein amino acid phosphorylation; positive regulation of protein kinase activity; positive regulation of signal transduction; protein homooligomerization; response to glucose stimulus