30 kDa adipocyte complement-related protein ; Adipocyte complement-related 30 kDa protein ; ACRP30 ; Adipocyte ; C1q and collagen domain-containing protein ; Adipose most abundant gene transcript 1 protein ; apM-1 ; ACRP30 ; APM1
Categories
Elisa
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.
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).
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA];PROTEIN SEQUENCE OF 18-26; 194-197; 203-208 AND 221-228;GLYCOSYLATION;STRUCTURE OF CARBOHYDRATES
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PROTEIN SEQUENCE OF 18-26;PARTIAL PROTEIN SEQUENCE;HYDROXYLATION AT LYS-28; PRO-39; PRO-42; PRO-48; LYS-60; LYS-63; LYS-72; PRO-86 AND LYS-96;GLYCOSYLATION AT LYS-28; LYS-60; LYS-63 AND LYS-96;ABSENCE OF HYDROXYLATION AT PRO-57; PRO-66; PRO-71; PRO-90 AND PRO-99;ABSENCE OF GLYCOSYLATION AT ASN-225;IDENTIFICATION BY MASS SPECTROMETRY