Adiponectin Recombinant Protein | ha recombinant protein

Recombinant Human Adiponectin

Cat. Num. AAA955841

• Gene Names: ADIPOQ; ACDC; ADPN; APM1; APM-1; GBP28; ACRP30; ADIPQTL1
• Purity: Greater than 90% as determined by SDS-PAGE.
• Synonyms: Adiponectin; Recombinant Human Adiponectin; 30 kDa adipocyte complement-related protein; Adipocyte complement-related 30 kDa protein; ACRP30; Adipocyte; C1q and collagen domain-containing protein; Adipose most abundant gene transcript 1 protein; apM-1; Gelatin-binding protein; ha recombinant protein

• Host: E Coli
• Purity/Purification: Greater than 90% as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence Positions: 19-244
• Sequence: ETTTQGPGVLLPLPKGACTGWMAGIPGHPGHNGAPGRDGRDGTPGEKGEKGDPGLIGPKGDIGETGVPGAEGPRGFPGIQGRKGEPGEGAYVYRSAFSVGLETYVTIPNMPIRFTKIFYNQQNHYDGSTGKFHCNIPGLYYFAYHITVYMKDVKVSLFKKDKAMLFTYDQYQENNVDQASGSVLLHLEVGDQVWLQVYGEGERNGLYADNDNDSTFTGFLLYHDTN
• Sequence Length: 244

• Product Note: Applications are user defined. Product is developed and quality control tested in house, data or additional information may be provided upon request. The researcher needs to establish and confirm the suitability of the product for their application.
• 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 ha 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.

Product Categories/Family for ha recombinant protein

Cardiovascular; Raw Materials Assay Development

References

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)

NCBI and Uniprot Product Information

• NCBI GI #: 295317372
• NCBI GeneID: 9370
• NCBI Accession #: NP_001171271.1
• NCBI GenBank Nucleotide #: NM_001177800.1
• UniProt Accession #: Q15848; Q58EX9
• Molecular Weight: 28.6kD
• NCBI Official Full Name: adiponectin
• NCBI Official Synonym Full Names: adiponectin, C1Q and collagen domain containing
• NCBI Official Symbol: ADIPOQ
• NCBI Official Synonym Symbols: ACDC; ADPN; APM1; APM-1; GBP28; ACRP30; ADIPQTL1
• NCBI Protein Information: adiponectin
• UniProt Protein Name: Adiponectin
• Protein Family: Adiponectin
• UniProt Gene Name: ADIPOQ
• UniProt Synonym Gene Names: ACDC; ACRP30; APM1; GBP28; ACRP30; apM-1
• UniProt Entry Name: ADIPO_HUMAN

NCBI Description

This gene is expressed in adipose tissue exclusively. It encodes a protein with similarity to collagens X and VIII and complement factor C1q. The encoded protein circulates in the plasma and is involved with metabolic and hormonal processes. Mutations in this gene are associated with adiponectin deficiency. Multiple alternatively spliced variants, encoding the same protein, have been identified. [provided by RefSeq, Apr 2010]

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

Chromosomal Location of Human Ortholog: 3q27

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

Molecular Function: cytokine activity; 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; circadian rhythm; fatty acid beta-oxidation; fatty acid oxidation; generation of precursor metabolites and energy; 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 signal transduction; protein homooligomerization; response to activity; response to ethanol; response to glucocorticoid stimulus; response to glucose stimulus; response to hypoxia; response to nutrient; response to sucrose stimulus

Disease: Adiponectin, Serum Level Of, Quantitative Trait Locus 1