Adiponectin Recombinant Protein | Adipoq recombinant protein

Recombinant mouse Adiponectin protein

Cat. Num. AAA717148

• Gene Names: Adipoq; APN; Acdc; apM1; 30kDa; GBP28; adipo; Acrp30
• Applications: ELISA, Western Blot
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Adiponectin; Recombinant mouse Adiponectin protein; Adipoq recombinant protein

• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence: MLLLQALLFLLILPSHAEDDLVPPPKGTCAGWMAGIPGHP GHNGTPGRDGRDGTPGEKGEKGDAGLLGPKGETGDVGMTG AEGPRGFPGTPGRKGEPGEAAYMYRSAFSVGLETRVTVPN VPIRFTKIFYNQQNHYDGSTGKFYCNIPGLYYFSYHITVY MKDVKVSLFKKDKAVLFTYDQYQEKNVDQASGSVLLHLEV GDQVWLQVYGDGDHNGLYAD NVNDSTFTGFLLYHDTN

• Applicable Applications for Adipoq recombinant protein: ELISA, Western Blot
• Preparation and Storage: Store working aliquots at 4 degree C for up to one week. For extended storage, conserve at -20 degree C or -80 degree C. Repeated freezing and thawing is not recommended.

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

[5] "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)
[7] "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)

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; Q9DC68; Q6GTX4; Q8BRW2
• Molecular Weight: 23 KD
• NCBI Official Full Name: adiponectin
• NCBI Official Synonym Full Names: adiponectin, C1Q and collagen domain containing
• NCBI Official Symbol: Adipoq
• NCBI Official Synonym Symbols: APN; Acdc; apM1; 30kDa; GBP28; adipo; Acrp30
• NCBI Protein Information: adiponectin; adipocyte-specific protein AdipoQ; adipocyte complement related protein; 30 kDa adipocyte complement-related protein; adipocyte complement-related 30 kDa protein; adipocyte, C1Q and collagen domain containing; adipocyte, C1q and collagen domain-containing protein
• UniProt Protein Name: Adiponectin
• Protein Family: Adiponectin
• UniProt Gene Name: Adipoq
• UniProt Synonym Gene Names: Acdc; Acrp30; Apm1
• UniProt Entry Name: ADIPO_MOUSE

Uniprot Description

Function: 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. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11Subunit structure: 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 CTRP9 via the C1q domain (heterotrimeric complex). Ref.10 Ref.11 Ref.12 Ref.13 Ref.14Subcellular location: Secreted. Tissue specificity: Synthesized exclusively by adipocytes and secreted into plasma.Induction: During hormone-induced adipose differentiation and activated by insulin.Post-translational modification: HMW complexes are more extensively glycosylated than smaller oligomers. Hydroxylation and glycosylation of the lysine residues within the collagene-like domain of adiponectin seem to be critically involved in regulating the formation and/or secretion of HMW complexes and consequently contribute to the insulin-sensitizing activity of adiponectin in hepatocytes. Ref.5 Ref.6 Ref.14O-glycosylated. Not N-glycosylated By similarity O-linked glycans on hydroxylysine residues consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups By similarity. O-linked glycosylation in the N-terminal is disialylated with the structure Neu5Acalpha2->8Neu5Acalpha2->3Gal. Sialylated by alpha 2,8-sialyltransferase III. Ref.5 Ref.6 Ref.14Miscellaneous: HMW-complex blood contents are higher in females than in males, are increased in males by castration and decreased again upon subsequent testosterone treatment, which blocks HMW-complex secretion.Sequence similarities: Contains 1 C1q domain.Contains 1 collagen-like domain.