Recommended Products
biological source
bovine blood (Fetal)
form
saline suspension
extent of labeling
≥200 μg per mL
technique(s)
affinity chromatography: suitable
matrix
cross-linked 4% beaded agarose
matrix activation
cyanogen bromide
matrix attachment
amino
matrix spacer
1 atom
suitability
suitable for chromatography
storage temp.
2-8°C
Application
Fetuin-agarose is an agarose conjugate in saline suspension used in affinity chromatography, protein chromatography and specialty resins. Fetuin-agarose columns have been used in studies that inform the detection and quantification of tumor markers.
Physical form
Suspension in 0.5M NaCl containing preservative
Preparation Note
Prepared with Fetuin, F2379
Storage Class Code
10 - Combustible liquids
WGK
WGK 3
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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Nohora Vega et al.
Phytochemistry, 67(4), 347-355 (2006-01-18)
A lectin was isolated and characterised from Salvia bogotensis seeds. Removal of the abundant pigments and polysaccharides, which are present in seeds, was an essential step in its purification. Several procedures were assayed and the best suited, including Pectinex treatment
M J Friedman
Proceedings of the National Academy of Sciences of the United States of America, 80(17), 5421-5424 (1983-09-01)
During malaria and other infections, the plasma concentration of alpha 1-acid glycoprotein (AGP) increases 3- to 4-fold, but the function of this glycoprotein has been unknown. This study demonstrates, by in vitro culture of the malaria parasite Plasmodium falciparum, that
A K Satapathy et al.
Immunology, 80(4), 546-552 (1993-12-01)
A cell-ELISA was developed using monolayers of glutaraldehyde-fixed normal as well as Plasmodium berghei-infected mouse erythrocytes for quantification and characterization of anti-erythrocytic autoantibodies in murine malaria. Testing normal (NMS) and peak parasitaemic sera (PPS) on erythrocyte monolayers treated with trypsin
M Haidar et al.
Glycoconjugate journal, 11(2), 73-79 (1994-04-01)
Envelope glycoproteins of human immunodeficiency virus (gp120 and gp41) occur as oligomers. Here, we show by gel filtration analysis that gp120 oligomerization in vitro is calcium- and temperature-dependent. Recombinant gp120 (rgp120) species were recovered as monomers at 20 degrees C
M Sherman et al.
The Journal of biological chemistry, 269(50), 31479-31483 (1994-12-16)
During heat shock of Escherichia coli, the expression of the major molecular chaperone, GroEL, increases; in addition, a small fraction of the GroEL becomes phosphorylated (Sherman, M. Yu., and Goldberg, A. L. (1992) Nature 367, 166-1692). This heat shock-induced phosphorylation
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