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β-Casein from bovine milk

BioUltra, ≥98% (PAGE)

CAS Number:
EC Number:
MDL number:

Quality Level

biological source

bovine milk

product line



≥98% (PAGE)


essentially salt-free, lyophilized powder


activity assay: suitable

UniProt accession no.

storage temp.


Gene Information

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General description

β-Casein from bovine milk is an immunoglobulin E (IgE)-binding epitope belonging to the secretory calcium-binding phosphoprotein family. It consists of 209 amino acids and five phosphate groups. β-Casein has a globular hydrophobic domain at the C-terminal, a highly solvated and charged domain at the N-terminal and proline residues.


It has been studied as a generator of peptides responsible for biological activities such as opiate, immunostimulating, antibacterial, and peptidase inhibitors.
β-Casein from bovine milk has been used as a protein substrate in proteolytic assays. It has also been used to embed polyacrylamide gels in β-casein zymography.


250 mg in poly bottle
1 g in poly bottle

Biochem/physiol Actions

A polymorphic fraction of the major milk protein, casein. The A1 and B (but not A2) isoforms yield the bioactive peptide, ß-casomorphin upon gastrointestinal proteolytic digestion, which can have widely varied effects on human health. There is some effort to select dairy cattle for the A2 isoform to avoid this possibility.

Storage Class Code

11 - Combustible Solids

WGK Germany


Personal Protective Equipment

dust mask type N95 (US),Eyeshields,Gloves

Certificate of Analysis

Certificate of Origin

Crystal structure of the cysteine-rich secretory protein stecrisp reveals that the cysteine-rich domain has a K+ channel inhibitor-like fold
Guo M, et al.
The Journal of Biological Chemistry, 280(13), 12405-12412 (2005)
Evgenia Deryusheva et al.
Proteomics, 19(6), e1800098-e1800098 (2018-12-29)
Intrinsically disordered proteins (IDPs) are implicated in a range of human diseases, some of which are associated with the ability to bind to lipids. Although the presence of solvent-exposed hydrophobic regions in IDPs should favor their interactions with low-molecular-weight hydrophobic/amphiphilic...
Bovine milk allergens: a comprehensive review
Villa C, et al.
Comprehensive Reviews in Food Science and Food Safety, 17(1), 137-164 (2018)
Elen A Perpetuo et al.
Journal of protein chemistry, 22(7-8), 601-606 (2004-01-13)
Peptides that display bradykinin-potentiating activity have been obtained from a number of distinct sources, such as snake venoms, fibrinogen, and casein. This paper describes the characterization of two new peptides generated by tryptic hydrolysis of casein. No homology was found...
Esther Dolze et al.
Plant molecular biology, 83(6), 607-624 (2013-08-15)
Matrix enzymes are imported into peroxisomes and glyoxysomes, a subclass of peroxisomes involved in lipid mobilization. Two peroxisomal targeting signals (PTS), the C-terminal PTS1 and the N-terminal PTS2, mediate the translocation of proteins into the organelle. PTS2 processing upon import...


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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