This product is native fetuin isolated from fetal bovine serum and should contain both Fetuin A and B. The percentage of each is not determined. It is prepared by ammonium sulfate fractionation of fetal bovine serum by the method of Pederson, K.O., J. Phys. and Colloid Chem., 51, 164 (1947). The article indicates that the preparation was carried out to obtain both alpha and beta forms of Fetuin. For more information, see https://pubmed.ncbi.nlm.nih.gov/20286396/
F3004
Fetuin from fetal bovine serum
lyophilized powder
Synonim(y):
Fetuin from fetal calf serum
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Informacje o tej pozycji
Form:
lyophilized powder
Biological source:
bovine serum (fetal)
Przejdź do
Pomoc techniczna
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Pozwól nam pomócbiological 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
Quality Level
Gene Information
bovine ... FETUB(504615)
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Ta pozycja | |||
|---|---|---|---|
| biological source bovine serum (fetal) | biological source bovine serum (fetal) | biological source - | biological source bovine serum |
| technique(s) HPLC: suitable, MALDI-MS: suitable | technique(s) cell culture | mammalian: suitable | technique(s) cell culture | mammalian: suitable | technique(s) cell culture | mammalian: suitable |
| form lyophilized powder | form lyophilized powder | form lyophilized powder | form lyophilized solid |
| impurities ~0.2% free N-acetylneuraminic acid | impurities ≤0.3% free N-acetylneuraminic acid | impurities ≤0.3% free N-acetylneuraminic acid | impurities - |
| Gene Information bovine ... FETUB(504615) | Gene Information bovine ... FETUB(504615) | Gene Information - | Gene Information bovine ... AHSG(280988), FETUB(504615) |
| UniProt accession no. | UniProt accession no. | UniProt accession no. - | UniProt accession no. |
General description
Fetuin is an abundant glycosylated protein from fetal bovine serum and functions as a transport and storage protein.[1] It is also called the α2-Heremans-Schmid glycoprotein (AHSG) and corresponds to a molecular weight of 64 kDa.[2] It belongs to the statin family and is synthesized principally in the liver and partially in the kidneys, placenta and the tongue.[3]
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)[4]
- as a ligand in carbohydrate binding assay of pertussis toxin vaccine[5]
- in the synthesis of fetuin-A conjugated gold nanoparticles (F-GNPs) for drug carrier studies[6]
Biochem/physiol Actions
Preparation Note
Further processing of F2379 by gel filtration.
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Klasa składowania
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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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.
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)
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
Development of an in vitro Biochemical Assay System for the Measurement of Residual Toxin Activities in Pertussis Toxin Containing Vaccines
Ting Yuen C, et al.
Journal of vaccines & vaccination, 08 (2017)
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
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
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