Recombinant human Adiponectin (gAcrp30/Adipolean Variant) protein (ab50219)
Key features and details
- Expression system: Escherichia coli
- Purity: > 98% SDS-PAGE
- Active: Yes
- Suitable for: SDS-PAGE, Functional Studies
Description
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Product name
Recombinant human Adiponectin (gAcrp30/Adipolean Variant) protein
See all Adiponectin proteins and peptides -
Biological activity
Biological Activity : Determined by a cytotoxicity assay using M1 cells. The expected ED50 for this effect is 0.5-1.0 µg/ml.
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Purity
> 98 % SDS-PAGE.
Greater than 98% by HPLC analyses. Endotoxin level is less than 0.1 ng per g (1EU/g). -
Expression system
Escherichia coli -
Protein length
Full length protein -
Animal free
No -
Nature
Recombinant -
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Species
Human -
Sequence
PGAEGPRGFP GIQGRKGEPG EGAYVYRSAF SVGLETYVTI PNMPIRFTKI FYNQQNHYDG STGKFHCNIP GLYYFAYHIT VYMKDVKVSL FKKDKAMLFT YDQYQENNVD QASGSVLLHL EVGDQVWLQV YGEGERNGLY ADNDNDSTFT GFLLYHDTN -
Predicted molecular weight
18 kDa -
Additional sequence information
This naturally occurring variant of human gAcrp30/Adipolean is an 18.1 kDa protein, containing 14 extra amino acids extra at the N-terminus of human gAcrp30/Adipolean.
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Description
Recombinant human Adiponectin protein
Associated products
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Related Products
Specifications
Our Abpromise guarantee covers the use of ab50219 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
Functional Studies
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Form
Lyophilized -
Additional notes
The gAcrp30 variant is a naturally occurring globular protein obtained by proteolytic processing of adiponectin. Adiponectin is produced and secreted exclusively by adipocytes, and is a relatively abundant plasma protein, accounting for up to 0.05% of total serum protein. Like Adiponectin, Acrp30 is capable of decreasing hyperglycemia and reversing insulin resistance. Additionally, gAcrp30 has been shown to be an important factor in promoting fat loss by signaling muscle to absorb and burn Free-Fatty Acids (FFAs). The signaling receptors for adiponectin and gAcrp30 have recently been identified and named AdipoR1 and AdipoR2. AdipoR2 is predominantly expressed in the liver.
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Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped at 4°C. The lyophilized protein is stable for a few weeks at room temperature. Store at -20°C long term.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
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ReconstitutionReconstitute to 1mg/ml using sterile water.
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
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)
ab50219 has not yet been referenced specifically in any publications.