Recombinant Mouse Adiponectin/Acrp30/AdipoQ (C-6His, Human Cells)

Product code: 32-8467

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  •   10 µg

  •  50 µg

  • $363.00 

  • $505.00 

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Amount : 50 µg
Content : Lyophilized from a 0.2 µm filtered solution of 20mM PB,150mM NaCl,pH7.4.
Storage condition : Lyophilized protein should be stored at -20°C, though stable at room temperature for 3 weeks. Reconstituted protein solution can be stored at 4-7°C for 2-7 days. Aliquots of reconstituted samples are stable at -20°C for 3 months.
AA sequence : EDDVTTTEELAPALVPPPKGTCAGWMAGIPGHPGHNGTPGRDGRDGTPGEKGEKGDAGLLGPKGETGDVGMTGAEGPRGFPGTPGRKGEPGEAAYVYRSAFSVGLETRVTVPNVPIRFTKIFYNQQNHYDGSTGKFYCNIPGLYYFSYHITVYMKDVKVSLFKKDKAVLFTYDQYQEKNVDQASGSVLLHLEVGDQVWLQVYGDGDHNGLYADNVNDSTFTGFLLYHDTNHHHHHH
Gene : Adipoq
Gene ID : 11450
Uniprot ID : Q60994
Source: Human Cells.
MW :27.6kD.
Recombinant Mouse Adiponectin is produced by our Mammalian expression system and the target gene encoding Glu18-Asn247 is expressed with a 6His tag at the C-terminus. Adiponectin is a secreted protein. It is synthesized exclusively by adipocytes and secreted into plasma. Adiponectin is an important adipokine that is involved in the control of fat metabolism and insulin sensitivity, with direct anti-diabetic, anti-atherogenic and anti-inflammatory activities. Adiponectin Stimulates AMPK phosphorylation and activates in the liver and the skeletal muscle, enhancing glucose utilization and fatty-acid combustion. Adiponectin also antagonizes TNF-alpha by negatively regulating its expression in various tissues such as liver and macrophages, and also by counteracting its effects. It inhibits endothelial NF-kappa-B signaling through a cAMP-dependent pathway. Adiponectin 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.

Endotoxin : Less than 0.1 ng/µg (1 IEU/µg) as determined by LAL test.

For Research Use Only. Not for use in diagnostic/therapeutics procedures.

Subcellular location: Secreted
Post transnational modification: O-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.
Tissue Specificity: Synthesized exclusively by adipocytes and secreted into plasma.
BioGrid: 197940. 3 interactions.
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