Overview

Description

  • Nature
    Recombinant
  • Source
    HEK 293 cells
  • Amino Acid Sequence
    • Accession
    • Species
      Mouse
    • Sequence
      EDDVTTTEELAPALVPPPKGTCAGWMAGIPGHPGHNGTPGRDGRDGTPGE KGEKGDAGLLGPKGETGDVGMTGAEGPRGFPGTPGRKGEPGEAA
    • Molecular weight
      25 kDa including tags
    • Amino acids
      18 to 111
    • Tags
      DDDDK tag N-Terminus

Specifications

Our Abpromise guarantee covers the use of ab157283 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

    Functional Studies

  • Endotoxin level
    < 0.100 Eu/µg
  • Purity
    >90% by SDS-PAGE.

  • Form
    Lyophilised
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Store at -20ºC.

    Constituent: 99% PBS

  • Reconstitution
    Reconstitute with 100µl sterile water to a final concentration of 0.1 mg/ml. Further dilutions should be made with medium containing 5% fetal calf serum or a carrier protein. After reconstitution, prepare aliquots and store at -20°C. Avoid freeze/thaw cycles.

General Info

  • Alternative names
    • 30 kDa adipocyte complement related protein
    • 30 kDa adipocyte complement-related protein
    • ACDC
    • 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
    • GBP28
    • Gelatin binding protein
    • Gelatin binding protein 28
    • Gelatin-binding protein
    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

  • ab157283 does not bind to rhTNF-R1 and rhOX40:Fc in an ELISA assay.

    Method: A 96 well ELISA plate was coated O/N at RT with 100 µl of 1 µg/ml rhTNF-R1:Fc and 1 µg/ml rhOX40:Fc in PBS. 100 µl of ab157283 at 8 µg/ml were mixed with 100 µl 0.5% FCS in PBS in the first well and a series of 1:1 dilutions was prepared for the following wells. Binding of ab157283 to the receptor:Fc was detected after 1 hr incubation at 37°C using a goat anti-human HRP conjugated antibody (1/1000 dilution, 1 hr incubation). O-phenylenediamine dihydrochloride (OPD) was used as a substrate, and absorbance was measured at 490 nm in an ELISA reader.

References

ab157283 has not yet been referenced specifically in any publications.

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

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