F3385
Fetuin from fetal bovine serum
lyophilized powder, BioReagent, suitable for cell culture
Synonym(s):
Fetuin from fetal calf serum
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About This Item
Recommended Products
product line
BioReagent
Quality Level
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
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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.
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.
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 Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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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
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