Adiponectin (Protein name
), ADIPO_MOUSE from NCBI database.
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General Annotation
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Antigen Annotation
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3D
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Predicted Eptitope
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Vaild Sequence
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Gene name:
Adipoq(Acdc;Acrp30;Apm1);
Protein name:
Adiponectin;
Alternative:
Adipocyte complement-related 30 kDa protein(ACRP30);30 kDa adipocyte complement-related protein;Adipocyte-specific protein AdipoQ;Adipocyte, C1q and collagen domain-containing protein;
Organism:
Mouse (Mus musculus).
General Annotation
Sub Unit:
Homomultimer. Forms trimers, hexamers and 12- to 18-mers. The trimers (low molecular weight complexes / LMW) are assembled via non-covalent interactions of the collagen-like domains in a triple helix and hydrophobic interactions within the globular C1q domain. Several trimers can associate to form disulfide-linked hexamers (middle molecular weight complexes / MMW) and larger complexes (higher molecular weight / HMW). The HMW-complex assembly may rely aditionally on lysine hydroxylation and glycosylation. LMW, MMW and HMW complexes bind to HBEGF, MMW and HMW complexes bind to PDGFB, and HMW complex binds to FGF2. Interacts with CTRP9 via the C1q domain (heterotrimeric complex).
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.
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12% SDS-PAGE Analysis
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Precision
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Intra-assay Precision (Precision within an assay):Three samples of known concentration were tested twenty times on one plate to assess intra-assay precision.
Intra-Assay CV: ≤ 4.5%
Inter-assay Precision (Precision between assays):Three samples of known concentration were tested in five separate assays to assess inter-assay precision.
Inter-Assay CV: ≤ 7.1%
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Recovery
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Recovery was determined by spiking various levels of ACE into serum and plasma .
Sample Type
Average(%)
Recovery Range(%)
Serum
95
91-98
Plasma
97
92-102
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Linearity
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The linearity of the kit was assayed by testing samples spiked with appropriate concentration of ACE and their serial dilutions. The results were demonstrated by the percentage of calculated concentration to the expected.
Sample
1:2
1:4
1:8
1:16
serum(n=5)
87-95%
90-101%
92-103%
90-98%
EDTA plasma(n=5)
89-95%
91-102%
89-101%
90-102%
heparin plasma(n=5)
90-98%
92-105%
96-101%
89-99%
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Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]
4.
"Cloning of murine adipocyte complement-related protein of 30 KDa from white adipose tissue." Wang S.F.
,
Han P.Z.
,
Mu C.J.
,
Zhao M.H.
Submitted (2004-09) to the EMBL/GenBank/DDBJ databases
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Cited for: NUCLEOTIDE SEQUENCE [MRNA]
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Cited for: PROTEIN SEQUENCE OF 18-25;HYDROXYLATION AT LYS-68; LYS-71; LYS-80; PRO-94 AND LYS-104;GLYCOSYLATION AT LYS-68; LYS-71; LYS-80 AND LYS-104;GLYCAN STRUCTURE;ABSENCE OF HYDROXYLATION AT PRO-79; PRO-98 AND PRO-107;ABSENCE OF GLYCOSYLATION AT ASN-233;IDENTIFICATION BY MASS SPECTROMETRY
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Cited for: SUBUNIT;MUTAGENESIS OF LYS-68; LYS-71; LYS-80 AND LYS-104
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Cited for: SUBUNIT;INTERACTION WITH CTRP9;MUTAGENESIS OF CYS-39
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Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 111-247