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 CTRP9A 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: PROTEIN SEQUENCE OF N-TERMINUS;PARTIAL PROTEIN SEQUENCE
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Cited for: SUBUNIT;DISULFIDE BOND;MUTAGENESIS OF CYS-36;CHARACTERIZATION OF VARIANTS ARG-84; SER-90; CYS-112 AND THR-164
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Cited for: SUBUNIT;HYDROXYLATION AT PRO-44; PRO-47; PRO-53; LYS-65; LYS-68; PRO-71; PRO-76; LYS-77; PRO-91; PRO-95 AND LYS-101;GLYCOSYLATION AT LYS-65; LYS-68; LYS-77 AND LYS-101;DISULFIDE BOND;LACK OF HYDROXYLATION AT PRO-62; PRO-86 AND PRO-104;LACK OF GLYCOSYLATION AT ASN-230;MUTAGENESIS OF LYS-33; CYS-36; LYS-65; LYS-68; LYS-77 AND LYS-101;IDENTIFICATION BY MASS SPECTROMETRY
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Cited for: GLYCOSYLATION AT THR-21 AND THR-22;SUBUNIT;IDENTIFICATION BY MASS SPECTROMETRY;MUTAGENESIS OF THR-20; THR-21 AND THR-22
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 104-244;SUBUNIT
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Cited for: VARIANTS ARG-84; MET-117; THR-164; SER-221 AND PRO-241
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: VARIANTS CYS-112; THR-164; SER-221 AND PRO-241;ASSOCIATION WITH LOW PLASMA ADIPONECTIN CONCENTRATION AND DIABETES MELLITUS TYPE 2