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Casein, Hammarsten bovine

Casein from bovine milk
CAS Number:
EC Number:
MDL number:

Quality Level

biological source

bovine milk (Hammarsten)


>90% dry basis




enzyme immunoassay: suitable


280 °C (dec.) (lit.)

UniProt accession no.

storage temp.

room temp

InChI key


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General description

Casein is an amphiphilic protein.
Casein, a phosphoprotein, is the principal protein component of milk which is almost entirely expressed in the lactating mammary gland. In bovine milk they are classified according to their calcium sensitivity: αs1-, αs2-, and β-caseins precipitate in the presence of calcium; whereas κ-casein remains in solution.


Casein, Hammarsten bovine has been used as a substrate for Aplysia californica calpain to study its activity.
The product is useful as a protease substrate.


500 g in poly bottle
5 kg in poly drum

Biochem/physiol Actions

Partial gastrointestinal digestion of casein is a rich source of bioactive peptides, such as β-casomorphin. However, bovine casein is not homogeneous; variants A1 and B do lead to production of β-casomorphin 7 production, while A2 does not.
Casein is useful in food industries and non-food applications. It has the property for emulsification, foam formation, and stabilization, water-binding, and gelation. Casein is also considered heat and acid-stable.

Storage Class Code

13 - Non Combustible Solids



Certificate of Analysis

Certificate of Origin

Margaret H Hastings et al.
PloS one, 12(10), e0186646-e0186646 (2017-10-21)
Calpains are a family of intracellular proteases defined by a conserved protease domain. In the marine mollusk Aplysia californica, calpains are important for the induction of long-term synaptic plasticity and memory, at least in part by cleaving protein kinase Cs...
Bovine beta-casein: Isolation, properties and functionality. A review
Atamer Z, et al.
International dairy journal, 66, 115-125 (2017)
Krisztina Nagy et al.
The Journal of biological chemistry, 285(50), 38811-38817 (2010-10-06)
The possible mechanism of casein aggregation and micelle buildup was studied in a new approach by letting α-casein adsorb from low concentration (0.1 mg·ml(-1)) solutions onto the charged surfaces of polyelectrolyte films. It was found that α-casein could adsorb onto...
Andreas F Kolb et al.
PloS one, 6(7), e21775-e21775 (2011-07-27)
The major physiological function of milk is the transport of amino acids, carbohydrates, lipids and minerals to mammalian offspring. Caseins, the major milk proteins, are secreted in the form of a micelle consisting of protein and calcium-phosphate.We have analysed the...

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