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κ-Casein from bovine milk

≥70% (PAGE), lyophilized powder

CAS Number:
EC Number:
MDL number:

Quality Level

biological source

bovine milk


≥70% (PAGE)


lyophilized powder


isoelectric focusing (IEF): suitable

storage temp.


Gene Information

General description

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

Biochem/physiol Actions

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).

Storage Class Code

11 - Combustible Solids

WGK Germany


Personal Protective Equipment

dust mask type N95 (US),Eyeshields,Gloves

Certificate of Analysis

Certificate of Origin

Paramjit S Bansal et al.
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)...
Antigen-specific T-cell responses in patients with non-IgE-mediated gastrointestinal food allergy are predominantly skewed to T(H)2.
Hideaki Morita et al.
The Journal of allergy and clinical immunology, 131(2), 590-592 (2012-10-23)
Hongjun Yu et al.
Proceedings of the National Academy of Sciences of the United States of America, 115(41), E9560-E9569 (2018-09-28)
The protein disaggregase ClpB hexamer is conserved across evolution and has two AAA+-type nucleotide-binding domains, NBD1 and NBD2, in each protomer. In M. tuberculosis (Mtb), ClpB facilitates asymmetric distribution of protein aggregates during cell division to help the pathogen survive...
A study on bovine kappa-casein aggregation after the enzymatic action of chymosin.
Maria Eugenia Hidalgo., et al
Colloids Surf., 76, 556-563 (2010)
Presence of functional, autoreactive human milk-specific IgE in infants with cow's milk allergy.
Jarvinen KM., et al.
Clinical and Experimental Allergy (2011)


HPLC Analysis of Caseins on BIOshell™ A400 Protein C4

-casein basis (electrophoresis), lyophilized powder; β-Casein from bovine milk, BioUltra, ≥98% (PAGE)

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