Human Adiponectin full length protein (ab51294)

Overview

Description

  • NatureRecombinant
  • SourceE. coli
  • Amino Acid Sequence
    • SpeciesHuman
    • SequenceMGHDQETTTQ GPGVLLPLPK GACTGWMAGI PGHPGHNGAP GRDGRDGTPG EKGEKGDPGL IGPKGDIGET GVPGAEGPRG FPGIQGRKGE PGEGAYVYRS AFSVGLETYV TIPNMPIRFT KIFYNQQNHY DGSTGKFHCN IPGLYYFAYH ITVYMKDVKV SLFKKDKAML FTYDQYQENN VDQASGSVLL HLEVGDQVWL QVYGEGERNG LYADNDNDST FTGFLLYHDT N
    • Amino acids0 to 0

Specifications

Our Abpromise guarantee covers the use of ab51294 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications

    SDS-PAGE

  • Endotoxin level< 1.000 Eu/µg
  • Purity> 90 % by SDS-PAGE.

  • FormLiquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.

    Preservative: None
    Constituents: PBS, 1mM DTT, pH 7.4

General info

  • Alternative names
    • 30 kDa adipocyte complement related protein
    • 30 kDa adipocyte complement-related protein
    • ACDC
    • ACRP 30
    • ACRP30
    • ADIPO_HUMAN
    • Adipocyte
    • Adipocyte C1q and collagen domain containing protein
    • Adipocyte complement related 30 kDa protein
    • Adipocyte complement related protein of 30 kDa
    • Adipocyte complement-related 30 kDa protein
    • adipocyte-specific secretory protein
    • Adiponectin
    • Adiponectin precursor
    • adiponectin, C1Q and collagen domain containing
    • AdipoQ
    • Adipose most abundant gene transcript 1
    • Adipose most abundant gene transcript 1 protein
    • Adipose specific collagen like factor
    • ADIPQTL1
    • ADPN
    • APM 1
    • apM-1
    • ApM1
    • C1q and collagen domain-containing protein
    • GBP 28
    • GBP28
    • Gelatin binding protein
    • Gelatin binding protein 28
    • Gelatin-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

Human Adiponectin full length protein images

  • 15% SDS-PAGE analysis of recombinant mature human adiponectin ab51294

References for Human Adiponectin full length protein (ab51294)

ab51294 has not yet been referenced specifically in any publications.

Product Wall

Regrettablywe have not determied ifab51294 can detect the higher molecular weight forms of adiponectin.

I am sorry to not be more helpful in this instance. Please contact us again if you have any further questions.

Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"