Product Name
Fetuin from fetal bovine serum, lyophilized powder, BioReagent, suitable for cell culture
product line
BioReagent
form
lyophilized powder
mol wt
48.4 kDa
technique(s)
cell culture | mammalian: suitable
impurities
≤0.3% free N-acetylneuraminic acid
solubility
H2O: 1 mg/mL
storage temp.
2-8°C
Quality Level
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Application
Fetuin from fetal bovine serum has been used:
- as a substrate to determine neuraminidase activity
- to validate the specificity of sialidases
- to stabilize m-calpain
Biochem/physiol Actions
Fetuin acts as an inhibitor of insulin receptor tyrosine kinase. It modulates bone remodeling and calcium metabolism. Fetuin regulates vascular calcification, insulin resistance, protease activity control, keratinocytes migration and breast tumor cell proliferative signaling. It functions as a biomarker for neurodegenerative diseases. Fetuin exhibits anti-inflammatory property.
General description
Fetuin from fetal bovine serum is a plasma glycoprotein. It is a 64 kDa glycoprotein, which is produced by the liver and adipose tissue.
A glycoprotein derived from FBS that is used as Fetuin has been used at a concentration of 500 mg/ml to supplement serum free F12 medium (along with insulin, transferrin and 2-mercaptoethanol) in culture of embryonal carcinoma cells.
A glycoprotein derived from FBS that is used as Fetuin has been used at a concentration of 500 mg/ml to supplement serum free F12 medium (along with insulin, transferrin and 2-mercaptoethanol) in culture of embryonal carcinoma cells.
Preparation Note
Prepared by ammonium sulfate fractionation of fetal bovine serum by the method of Pederson, K.O., J. Phys. and Colloid Chem., 51, 164 (1947).
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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Analyses of N-linked glycans of PrPSc revealed predominantly 2, 6-linked sialic acid residues
Katorcha E and Baskakov IV
FEBS Journal, 284(21), 3727-3738 (2017)
Antiviral activity of fermented ginseng extracts against a broad range of influenza viruses
Wang Y, et al.
Viruses, 10(9), 471-471 (2018)
Christopher Ashwood et al.
Journal of the American Society for Mass Spectrometry, 29(6), 1194-1209 (2018-04-01)
Profiling cellular protein glycosylation is challenging due to the presence of highly similar glycan structures that play diverse roles in cellular physiology. As the anomericity and the exact linkage type of a single glycosidic bond can influence glycan function, there
Fetuin A stabilizes m-calpain and facilitates plasma membrane repair
Mellgren RL and Huang X
The Journal of Biological Chemistry, 282(49), 35868-35877 (2007)
Fetuin-A: a multifunctional protein
Mori K, et al.
Recent Patents on Endocrine, Metabolic & Immune Drug Discovery, 5(2), 124-146 (2011)
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