Recombinant Mouse Adiponectin/Acrp30 Protein, ＞95% (SDS-PAGE), high purity

Item Number

rp153562

• Product Name: Recombinant Mouse Adiponectin/Acrp30 Protein, ＞95% (SDS-PAGE), high purity
• Synonyms: ACDC | Acrp30 | ACRP30ADPN | adipocyte, C1Q and collagen domain containing | Adiponectin | adiponectin, C1Q and collagen domain containing | AdipoQ | ADIPQTL1 | ApM1 | apM-1 | APM1APM-1 | C1q and collagen domain-containing protein | GBP28 | GBP28apM1 | Ge
• Grade: ActiBioPure™, Animal Free, Azide Free, Bioactive, Carrier Free
• Specifications & Purity: ActiBioPure™, Bioactive, Animal Free, Carrier Free, Azide Free, ≥95%(SDS-PAGE)
• Purity: ＞95% (SDS-PAGE)
• Bioactivity: Measured by its ability to induce TIMP-1 secretion by mouse macrophages. Kumada. The ED₅₀ for this effect is 5-20 μg/mL.
• Endotoxin Concentration: <0.1 EU/μg
• Expression System: HEK293
• Species: Mouse
• Amino Acids: 18-247 aa
• Sequence: EDDVTTTEELAPALVPPPKGTCAGWMAGIPGHPGHNGTPGRDGRDGTPGEKGEKGDAGLLGPKGETGDVGMTGAEGPRGFPGTPGRKGEPGEAAYVYRSAFSVGLETRVTVPNVPIRFTKIFYNQQNHYDGSTGKFYCNIPGLYYFSYHITVYMKDVKVSLFKKDKAVLFTYDQYQEKNVDQASGSVLLHLEVGDQVWLQVYGDGDHNGLYADNVNDSTFTGFLLYHDTNHHHHHH
• Protein Tag: C-His
• Accession #: Q60994
• Predicted molecular weight: 25 kDa

Product Description

Purity

>95% SDS-PAGE.

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.

Post-translational

Hydroxylated Lys-33 was not identified in PubMed:16497731, probably due to poor representation of the N-terminal peptide in mass fingerprinting. 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. O-glycosylated. Not N-glycosylated. O-linked glycans on hydroxylysines consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups. Sialylated to varying degrees depending on tissue. Thr-22 appears to be the major site of sialylation. Higher sialylation found in SGBS adipocytes than in HEK fibroblasts. Sialylation is not required neither for heterodimerization nor for secretion. Not sialylated on the glycosylated hydroxylysines. Desialylated forms are rapidly cleared from the circulation.