Adiponectin (ha) Human 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.

cDNA cloning and expression of a novel adipose specific collagen-like factor, apM1 (AdiPose Most abundant Gene transcript 1) .Maeda K., Okubo K., Shimomura I., Funahashi T., Matsuzawa Y., Matsubara K.Biochem. Biophys. Res. Commun. 221:286-289(1996) Organization of the gene for gelatin-binding protein (GBP28) .Saito K., Tobe T., Minoshima S., Asakawa S., Sumiya J., Yoda M., Nakano Y., Shimizu N., Tomita M.Gene 229:67-73(1999) The human apM-1, an adipocyte-specific gene linked to the family of TNF's and to genes expressed in activated T cells, is mapped to chromosome 1q21.3-q23, a susceptibility locus identified for familial combined hyperlipidemia (FCH) .Schaeffler A., Orso E., Palitzsch K.D., Buechler C., Drobnik W., Fuerst A., Schoelmerich J., Schmitz G.Biochem. Biophys. Res. Commun. 260:416-425(1999) Signal peptide prediction based on analysis of experimentally verified cleavage sites.Zhang Z., Henzel W.J.Protein Sci. 13:2819-2824(2004) Isolation and characterization of GBP28, a novel gelatin-binding protein purified from human plasma.Nakano Y., Tobe T., Choi-Miura N.H., Mazda T., Tomita M.J. Biochem. 120:803-812(1996) Adiponectin, a new member of the family of soluble defense collagens, negatively regulates the growth of myelomonocytic progenitors and the functions of macrophages.Yokota T., Oritani K., Takahashi I., Ishikawa J., Matsuyama A., Ouchi N., Kihara S., Funahashi T., Tenner A.J., Tomiyama Y., Matsuzawa Y.Blood 96:1723-1732(2000) Adiponectin, an adipocyte-derived plasma protein, inhibits endothelial NF-kappaB signaling through a cAMP-dependent pathway.Ouchi N., Kihara S., Arita Y., Okamoto Y., Maeda K., Kuriyama H., Hotta K., Nishida M., Takahashi M., Muraguchi M., Ohmoto Y., Nakamura T., Yamashita S., Funahashi T., Matsuzawa Y.Circulation 102:1296-1301(2000) 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) Impaired multimerization of human adiponectin mutants associated with diabetes. Molecular structure and multimer formation of adiponectin.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.J. Biol. Chem. 278:40352-40363(2003) Adiponectin multimerization is dependent on conserved lysines in the collagenous domain evidence for regulation of multimerization by alterations in posttranslational modifications.Richards A.A., Stephens T., Charlton H.K., Jones A., Macdonald G.A., Prins J.B., Whitehead J.P.Mol. Endocrinol. 20:1673-1687(2006) 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) Resveratrol-induced changes of the human adipocyte secretion profile.Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P., Mariman E.C., Renes J.J. Proteome Res. 11:4733-4743(2012) Crystal structure of a single-chain trimer of human adiponectin globular domain.Min X., Lemon B., Tang J., Liu Q., Zhang R., Walker N., Li Y., Wang Z.FEBS Lett. 586:912-917(2012) Genomic structure and mutations in adipose-specific gene, adiponectin.Takahashi M., Arita Y., Yamagata K., Matsukawa Y., Okutomi K., Horie M., Shimomura I., Hotta K., Kuriyama H., Kihara S., Nakamura T., Yamashita S., Funahashi T., Matsuzawa Y.Int. J. Obes. Relat. Metab. Disord. 24:861-868(2000) Genetic variation in the gene encoding adiponectin is associated with an increased risk of type 2 diabetes in the Japanese population.Hara K., Boutin P., Mori Y., Tobe K., Dina C., Yasuda K., Yamauchi T., Otabe S., Okada T., Eto K., Kadowaki H., Hagura R., Akanuma Y., Yazaki Y., Nagai R., Taniyama M., Matsubara K., Yoda M., Nakano Y., Kimura S., Tomita M., Kimura S., Ito C., Froguel P., Kadowaki T.Diabetes 51:536-540(2002) ErratumHara K., Boutin P., Mori Y., Tobe K., Dina C., Yasuda K., Yamauchi T., Otabe S., Okada T., Eto K., Kadowaki H., Hagura R., Akanuma Y., Yazaki Y., Nagai R., Taniyama M., Matsubara K., Yoda M., Nakano Y., Kimura S., Tomita M., Kimura S., Ito C., Froguel P., Kadowaki T.Diabetes 51:1294-1294(2002) Association of adiponectin mutation with type 2 diabetes a candidate gene for the insulin resistance syndrome.Kondo H., Shimomura I., Matsukawa Y., Kumada M., Takahashi M., Matsuda M., Ouchi N., Kihara S., Kawamoto T., Sumitsuji S., Funahashi T., Matsuzawa Y.Diabetes 51:2325-2328(2002) Single-nucleotide polymorphism haplotypes in the both proximal promoter and exon 3 of the APM1 gene modulate adipocyte-secreted adiponectin hormone levels and contribute to the genetic risk for type 2 diabetes in French Caucasians.Vasseur F., Helbecque N., Dina C., Lobbens S., Delannoy V., Gaget S., Boutin P., Vaxillaire M., Lepretre F., Dupont S., Hara K., Clement K., Bihain B., Kadowaki T., Froguel P.Hum. Mol. Genet. 11:2607-2614(2002)

Small volumes of ha recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

MBS955841 is a recombinant protein targeting ha. Also known as Recombinant Human Adiponectin. Host: E Coli.