Recombinant Mouse Adiponectin (mutated C39A) protein (ab94676)
Key features and details
- Expression system: HEK 293 cells
- Purity: > 98% SDS-PAGE
- Suitable for: Functional Studies, WB, ELISA
Description
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Product name
Recombinant Mouse Adiponectin (mutated C39A) protein
See all Adiponectin proteins and peptides -
Purity
> 98 % SDS-PAGE. -
Expression system
HEK 293 cells -
Protein length
Full length protein -
Animal free
No -
Nature
Recombinant -
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Species
Mouse -
Sequence
EDDVTTTEEL APALVPPPKG TAAGWMAGIP GHPGHNGTPG RDGRDGTPGE KGEKGDAGLL GPKGETGDVG MTGAEGPRGF PGTPGRKGEP GEAAYMYRSA FSVGLETRVT VPNVPIRFTK IFYNQQNHYD GSTGKFYCNI PGLYYFSYHI TVYMKDVKVS LFKKDKAVLF TYDQYQEKNV DQASGSVLLH LEVGDQVWLQ VYGDGDHNGL YADNVNDSTF TGFLLYHDTN DYKDDDDK -
Modifications
mutated C39A
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Associated products
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Related Products
Specifications
Our Abpromise guarantee covers the use of ab94676 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Applications
Functional Studies
Western blot
ELISA
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Form
Lyophilized -
Additional notes
The cystenine 39 was replaced with alanine (C39A)9. mAd-C39A can only form trimer, but not hexamer or HMW form.
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Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped at 4°C. Store at -20ºC.
Constituent: PBS
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ReconstitutionAdd 100µl of deionized water to prepare a working stock solution of approximately 1 mg/mL and let the lyophilized pellet dissolve completely. Product is not sterile, please filter the product by an appropriate sterile filter before using it in cell culture. Aliquot reconstituted protein and avoid repeated freezing/thawing cycles and store at –80°C for long term storage.
General Info
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Alternative names
- 30 kDa adipocyte complement related protein
- 30 kDa adipocyte complement-related protein
- ACDC
see all -
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. -
Tissue specificity
Synthesized exclusively by adipocytes and secreted into plasma. -
Involvement in disease
Defects in ADIPOQ are the cause of adiponectin deficiency (ADPND) [MIM:612556]. ADPND results in very low concentrations of plasma adiponectin.
Genetic variations in ADIPOQ are associated with non-insulin-dependent diabetes mellitus (NIDDM) [MIM:125853]; also known as diabetes mellitus type 2. NIDDM is characterized by an autosomal dominant mode of inheritance, onset during adulthood and insulin resistance. -
Sequence similarities
Contains 1 C1q domain.
Contains 1 collagen-like domain. -
Domain
The C1q domain is commonly called the globular domain. -
Post-translational
modificationsHydroxylated 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. -
Cellular localization
Secreted. - Information by UniProt
Images
Protocols
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
Datasheets and documents
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Datasheet download
References (1)
ab94676 has been referenced in 1 publication.
- Wang L et al. Adiponectin restrains ILC2 activation by AMPK-mediated feedback inhibition of IL-33 signaling. J Exp Med 218:N/A (2021). PubMed: 33104171