Recombinant Human Adiponectin protein (ab13882)
- Datasheet
- References (1)
- Protocols
Overview
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Product nameRecombinant Human Adiponectin protein
See all Adiponectin proteins and peptides -
Protein lengthFull length protein
Description
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NatureRecombinant
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SourceEscherichia coli
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Amino Acid Sequence
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Accession
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SpeciesHuman
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SequenceMRGSHHHHHH GSGHDQETTT QGPGVLLPLP KGACTGWMAG IPGHPGHNGA PGRDGRDGTP GEKGEKGDPG LIGPKGDIGE TGVPGAEGPR GFPGIQGRKG EPGEGAYVYR SAFSVGLETY
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Amino acids15 to 244
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TagsHis tag N-Terminus
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Specifications
Our Abpromise guarantee covers the use of ab13882 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
Western blot
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Purity> 95 % SDS-PAGE.
Three-step procedure using affinity Ni-NTA chromatography and size exclusion chromatography before and after refolding. -
FormLyophilised
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Additional notes
The Human Adiponectin is created as a recombinant protein with N-terminal fusion of HisTag. The Human Adiponectin His-Tagged Fusion Protein, produced in E. coli, is 26.4 kDa protein containing 230 amino acid residues of the human Adiponectin and 12 additional amino acid residues - HisTag
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Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.
pH: 7.50
Constituents: 0.02% Tris buffered saline, 0.87% Sodium chloride -
ReconstitutionStore lyophilized protein at -20°C. Add 0.2 ml of distilled water and let the lyophilized pellet dissolve completely.
General Info
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Alternative names
- 30 kDa adipocyte complement related protein
- 30 kDa adipocyte complement-related protein
- ACDC
see all -
FunctionImportant 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.
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Tissue specificitySynthesized exclusively by adipocytes and secreted into plasma.
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Involvement in diseaseDefects 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 similaritiesContains 1 C1q domain.
Contains 1 collagen-like domain. -
DomainThe C1q domain is commonly called the globular domain.
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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 localizationSecreted.
- Information by UniProt
Datasheets and documents
References
This product has been referenced in:
- Kabara E et al. Adiponectin links adipose tissue function and monocyte inflammatory responses during bovine metabolic stress. Comp Immunol Microbiol Infect Dis 37:49-58 (2014). Read more (PubMed: 24296305) »