Recombinant human Adiponectin protein (ab78588)
Key features and details
- Expression system: Escherichia coli
- Purity: > 95% SDS-PAGE
- Active: Yes
- Suitable for: SDS-PAGE
Description
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Product name
Recombinant human Adiponectin protein
See all Adiponectin proteins and peptides -
Biological activity
Biological Activity: Adiponectin is fully biologically active when compared to standard. Activity is determined by the ability to inhibit the proliferation of mouse M1 cells. The expected ED50 for this effect is 1.0 - 2.5 µg/ml.
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Purity
> 95 % SDS-PAGE.
Purity Approximately 90% as determined by: - Analysis by RP-HPLC. - Reducing and non-reducing SDS-PAGE. This product was filter sterilised. -
Expression system
Escherichia coli -
Protein length
Protein fragment -
Animal free
No -
Nature
Recombinant -
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Species
Human -
Sequence
MKGEPGEGAY VYRSAFSVGL ETYVTIPNMP IRFTKIFYNQ QNHYDGSTGK FHCNIPGLYY FAYHITVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTN -
Amino acids
101 to 244
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Associated products
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Related Products
Specifications
Our Abpromise guarantee covers the use of ab78588 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
SDS-PAGE
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Form
Lyophilized -
Additional notes
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). -
Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
Constituents: 0.01155% DTT, 0.121% Tris
This product is an active protein and may elicit a biological response in vivo, handle with caution.
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ReconstitutionReconstitute with sterile 5 mM Tris, pH 8.0 + 0.75 mM DTT at 0.1 - 1.0 mg/ml, which can then be further diluted to other aqueous solutions.
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 (0)
ab78588 has not yet been referenced specifically in any publications.