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F3004

Sigma-Aldrich

Fetuin from fetal bovine serum

lyophilized powder

Synonym(s):

Fetuin from fetal calf serum

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About This Item

CAS Number:
EC Number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.32

biological source

bovine serum (fetal)

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)

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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.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


Certificates of Analysis (COA)

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Site-specific analysis of the O-glycosylation of bovine fetuin by electron-transfer dissociation mass spectrometry
Windwarder M and Altmann F
Journal of Proteomics, 108, 258-268 (2014)
Iqra Munir et al.
International journal of biological macromolecules, 101, 131-145 (2017-03-23)
Present study was conducted to establish the interaction of bovine fetuin-A to validate its binding modalities with doxorubicin (Dox). Fetuin-A was purified to highest purity and monodispersity. Green synthesis of fetuin-A conjugated gold nanoparticles (F-GNPs) has been performed giving typical
Fast purification of glycans and glycopeptides using silk-packed micropipette tip for matrix-assisted laser desorption/ionization-mass spectrometry and high-performance liquid chromatography-fluorescence detection analysis
Kayili H, et al.
Microchemical Journal, Devoted to the Application of Microtechniques in All Branches of Science, 139(2), 492-499 (2018)
A C Araujo et al.
The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society, 41(4), 571-578 (1993-04-01)
We investigated the localization of carbohydrate residues on the surface structures of microfilariae of Wuchereria bancrofti and Brugia malayi, using a panel of 10 different gold-labeled lectins and chitinase. The sheath, a structure that encloses the microfilariae, is not a
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

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