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Adiponectin protein (His tag) (ab13882)

Overview

  • Product nameAdiponectin protein (His tag)See all Adiponectin proteins and peptides ...
  • Protein descriptionRecombinant full length protein (Human)
  • Properties

  • Purity> 95 % by SDS-PAGE
  • Purification notesThree-step procedure using affinity Ni-NTA chromatography and size exclusion chromatography before and after refolding.
  • FormLiquid
  • Storage instructionsStore at +4°C short term (1-2 weeks). Aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
  • Storage bufferPreservative: None
    Constituents: 0.15M Sodium chloride, 0.02M Tris buffered saline, pH 7.5
  • Concentration information loading...
  • Sequence notesMRGSHHHHHH GSGHDQETTT QGPGVLLPLP KGACTGWMAG IPGHPGHNGA PGRDGRDGTP GEKGEKGDPG LIGPKGDIGE TGVPGAEGPR GFPGIQGRKG EPGEGAYVYR SAFSVGLETY
  • Research Areas
  • Applications

    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.

    Application Notes
    WB WB: Use at an assay dependent dilution.

    Protein info

    • Alternative names
        30 kDa adipocyte complement related protein30 kDa adipocyte complement-related proteinACDC
        ACRP 30ACRP30ADIPO_HUMANAdipocyteAdipocyte C1q and collagen domain containing proteinAdipocyte complement related 30 kDa proteinAdipocyte complement related protein of 30 kDaAdipocyte complement related protein of 30 kDaAdipocyte complement-related 30 kDa proteinAdiponectinAdipoQAdipose most abundant gene transcript 1Adipose most abundant gene transcript 1 proteinAdipose specific collagen like factorADIPQTL1ADPNAPM 1apM-1ApM1ApM1C1q and collagen domain-containing proteinGBP 28GBP28GBP28Gelatin binding proteinGelatin binding protein 28Gelatin-binding protein
      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.
  • Tissue specificitySynthesized exclusively by adipocytes and secreted into plasma.
  • 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.
  • Post-translational
    modifications
    Hydroxylated 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.
  • Target information above from: UniProt accession Q15848 The UniProt Consortium
    The Universal Protein Resource (UniProt) in 2010
    Nucleic Acids Res. 38:D142-D148 (2010) .

    Information by UniProt

    References for Adiponectin protein (His tag) (ab13882)

    ab13882 has not yet been referenced specifically in any publications.

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    For ab13882 DISCOUNT CODE: ***(valid on proteins)
    For ab22554 DISCOUNT CODE: *** (valid on primary antibodies)
    Expiration date: July 28th, 2012
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    Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"