Description

  • Product name

    Recombinant Mouse Adiponectin (mutated C39 A) protein
    See all Adiponectin proteins and peptides
  • Expression system

    HEK 293 cells
  • Protein length

    Full length protein
  • Animal free

    No
  • Nature

    Recombinant
    • Species

      Mouse
    • Sequence

      EDDVTTTEEL APALVPPPKG TAAGWMAGIP GHPGHNGTPG RDGRDGTPGE KGEKGDAGLL GPKGETGDVG MTGAEGPRGF PGTPGRKGEP GEAAYMYRSA FSVGLETRVT VPNVPIRFTK IFYNQQNHYD GSTGKFYCNI PGLYYFSYHI TVYMKDVKVS LFKKDKAVLF TYDQYQEKNV DQASGSVLLH LEVGDQVWLQ VYGDGDHNGL YADNVNDSTF TGFLLYHDTN DYKDDDDK
    • Modifications

      mutated C39A

Specifications

Our Abpromise guarantee covers the use of ab94676 in the following tested applications.

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

  • Applications

    Functional Studies

    Western blot

    ELISA

  • Form

    Lyophilised
  • Additional notes

    The cystenine 39 was replaced with alanine (C39A)9. mAd-C39A can only form trimer, but not hexamer or HMW form.

  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Store at -20ºC.

    Constituent: PBS

  • Reconstitution
    Add 100µl of deionized water to prepare a working stock solution of approximately 1 mg/mL and let the lyophilized pellet dissolve completely. Product is not sterile, please filter the product by an appropriate sterile filter before using it in cell culture. Aliquot reconstituted protein and avoid repeated freezing/thawing cycles and store at –80°C for long term storage.

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

  • SDS-PAGE analysis of Mouse Adiponectin protein (Trimeric form)
    Lane 1: MW marker
    Lane 2: non-reduced/non heated Adiponectin protein

    Gel concentration: 12%.

References

ab94676 has not yet been referenced specifically in any publications.

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