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About This Item
Form:
lyophilized powder
Biological source:
bovine serum (fetal)
biological source
bovine serum (fetal)
Quality Level
form
lyophilized powder
technique(s)
HPLC: suitable, MALDI-MS: suitable
impurities
~0.2% free N-acetylneuraminic acid
UniProt accession no.
storage temp.
2-8°C
Gene Information
bovine ... FETUB(504615)
General description
Fetuin is an abundant glycosylated protein from fetal bovine serum and functions as a transport and storage protein. It is also called the α2-Heremans-Schmid glycoprotein (AHSG) and corresponds to a molecular weight of 64 kDa. It belongs to the statin family and is synthesized principally in the liver and partially in the kidneys, placenta and the tongue.
Application
Fetuin from fetal bovine serum has been used:
- as a standard glycoprotein in matrix-assisted laser desorption/ionization-mass spectrometry (MALDI-MS) and high-performance liquid chromatography-fluorescence detection analysis (HPLC-FLD)
- as a ligand in carbohydrate binding assay of pertussis toxin vaccine
- in the synthesis of fetuin-A conjugated gold nanoparticles (F-GNPs) for drug carrier studies
Biochem/physiol Actions
In humans, polymorphism in the fetuin gene is implicated in type 2 diabetes mellitus and modulates adipocyte functionality. Elevated level of fetuin is observed in obesity and nonalcoholic fatty liver diseases (NAFLD). Fetuin is a potential marker in clinical diagnosis of metabolic disorders.
Preparation Note
Further processing of F2379 by gel filtration.
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Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Related Content
Fetuin-A (alpha2HS-glycoprotein) is a major serum adhesive protein that mediates growth signaling in breast tumor cells
Sakwe AM, et al.
Test, 285(53), 41827-41835 (2010)
Helga Hevér et al.
Methods in molecular biology (Clifton, N.J.), 1934, 93-125 (2019-07-01)
Even if a consensus sequence has been identified for a posttranslational modification, the presence of such a sequence motif only indicates the possibility, not the certainty that the modification actually occurs. Proteins can be glycosylated on certain amino acid side
M Demetriou et al.
The Journal of biological chemistry, 271(22), 12755-12761 (1996-05-31)
The serum glycoprotein fetuin is expressed during embryogenesis in multiple tissues including limb buds and has been shown to promote bone remodeling and stimulate cell proliferation in vitro. In this report, we demonstrate that fetuin antagonizes the antiproliferative action of