Caseins constitute 80% of the total milk proteins in the cow. κ-Casein is one of the major allergens in cow milk. It is a glycosylated protein comprising galactose, galactosamine, and sialic acid. It exists as tri- or tetrasaccharides and occurs in different isoforms based on the number of oligosaccharides attached to it. κ-Casein has a hydrophobic N-terminus and a hydrophilic C-terminus region.
κ-Casein from bovine milk has been used:
as a standard to quantify the casein concentration and to evaluate the ability of the bacterial strain to hydrolyze caseins released by HM Mozzarella
in LPS-depleted cow′s milk protein preparation for lymphoproliferation assay
as standard to quantify κ-casein concentration in skimmed milk samples by reversed-phase high-performance liquid chromatography (RP-HPLC)
100, 250 mg in poly bottle
1 g in poly bottle
κ-Casein from bovine milk is an immunoglobulin E (IgE)-binding epitope belonging to the casein phosphoprotein family. κ-Casein is important to the electrostatic and steric stabilization of casein micelles suspensions. It resists calcium precipitation and therefore, stabilizes other caseins. κ-Casein has been a target of research for creating low-phenylalanine milk through gene modification, which is important for patients suffering from metabolic diseases such as phenylketonuria (PKU).
Biochemical and biophysical research communications, 340(4), 1098-1103 (2006-01-13)
The caseins (alphas1, alphas2, beta, and kappa) are phosphoproteins present in bovine milk that have been studied for over a century and whose structures remain obscure. Here we describe the chemical synthesis and structure elucidation of the N-terminal segment (1-44)...
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