Description

  • 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.
  • 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
    • Species

      Human
    • Sequence

      MKGEPGEGAY VYRSAFSVGL ETYVTIPNMP IRFTKIFYNQ QNHYDGSTGK FHCNIPGLYY FAYHITVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTN
    • Amino acids

      101 to 244

Associated 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.

  • Applications

    SDS-PAGE

  • Form

    Lyophilised
  • 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

  • Stability and Storage

    Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.

    pH: 8.00
    Constituents: 0.01155% DTT, 0.121% Tris

    This product is an active protein and may elicit a biological response in vivo, handle with caution.

  • Reconstitution
    Reconstitute 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

  • 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
    • gelatin-binding protein 28
    • OTTHUMP00000210047
    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
    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 localization

    Secreted.
  • Information by UniProt

Images

  • Functional analysis of ab78588
  •  SDS PAGE analysis of ab78588 under non-reducing (-) and reducing (+) conditions. Stained with Coomassie Blue.

  • ab78588 used in Functional Studies.

References

ab78588 has not yet been referenced specifically in any publications.

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