Adiponectin protein (His tag) (ab13882)
Constituents: 0.15M Sodium chloride, 0.02M Tris buffered saline, pH 7.5
Our Abpromise guarantee covers the use of ab13882 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|WB||WB: Use at an assay dependent dilution.|
- 30 kDa adipocyte complement related protein30 kDa adipocyte complement-related proteinACDC
- ACRP 30ACRP30ADIPO_HUMANAdipocyteAdipocyte C1q and collagen domain containing proteinAdipocyte complement related 30 kDa proteinAdipocyte complement related protein of 30 kDaAdipocyte complement related protein of 30 kDaAdipocyte complement-related 30 kDa proteinAdiponectinAdipoQAdipose most abundant gene transcript 1Adipose most abundant gene transcript 1 proteinAdipose specific collagen like factorADIPQTL1ADPNAPM 1apM-1ApM1ApM1C1q and collagen domain-containing proteinGBP 28GBP28GBP28Gelatin binding proteinGelatin binding protein 28Gelatin-binding protein
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.
Contains 1 collagen-like domain.
modificationsHydroxylated 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.
References for Adiponectin protein (His tag) (ab13882)
ab13882 has not yet been referenced specifically in any publications.