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C3400

Sigma-Aldrich

Casein from bovine milk

powder

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About This Item

CAS Number:
EC Number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.61

biological source

bovine milk

Assay

87-94% protein basis

form

powder

technique(s)

activity assay: suitable
electrophoresis: suitable
immunocytochemistry: suitable

mp

280 °C (dec.) (lit.)

solubility

H2O: insoluble (forms a cloudy suspension)

UniProt accession no.

InChI

1S/C81H125N22O39P/c1-36(2)31-50(76(132)94-43(15-24-57(87)108)71(127)101-52(34-64(120)121)78(134)98-49(81(137)138)11-7-8-30-82)99-72(128)47(19-28-61(114)115)95-77(133)51(33-63(118)119)100-73(129)48(20-29-62(116)117)97-80(136)65(37(3)104)103-75(131)44(16-25-58(88)109)92-68(124)42(14-23-56(86)107)90-67(123)41(13-22-55(85)106)91-69(125)45(17-26-59(110)111)93-70(126)46(18-27-60(112)113)96-79(135)53(35-142-143(139,140)141)102-74(130)40(12-21-54(84)105)89-66(122)39(83)32-38-9-5-4-6-10-38/h4-6,9-10,36-37,39-53,65,104H,7-8,11-35,82-83H2,1-3H3,(H2,84,105)(H2,85,106)(H2,86,107)(H2,87,108)(H2,88,109)(H,89,122)(H,90,123)(H,91,125)(H,92,124)(H,93,126)(H,94,132)(H,95,133)(H,96,135)(H,97,136)(H,98,134)(H,99,128)(H,100,129)(H,101,127)(H,102,130)(H,103,131)(H,110,111)(H,112,113)(H,114,115)(H,116,117)(H,118,119)(H,120,121)(H,137,138)(H2,139,140,141)

InChI key

BECPQYXYKAMYBN-UHFFFAOYSA-N

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General description

Casein from bovine milk is a phosphoprotein and forms three-dimensional colloidal supramolecular micelles. There are four main types of casein which make up approximately 80% of the total protein in bovine milk: α-s1 casein, α-s2 casein, β-casein, and κ-casein. Casein is proposed to be the main protective constituent in milk. Casein is an amphiphilic protein.

Application

Casein from bovine milk has been used:
  • as a solid food sample in the in vivo and the in vitro digestion experiments using rodents
  • to prepare P407-casein hydrogels and to study the mechanical effects of the addition of casein to P407
  • in the preincubation solution, to increase the photostability of the quantum dots and to decrease nonspecific binding, for real-time imaging of single synaptic vesicles in hippocampal neurons

Casein from bovine milk is a phosphoprotein. There are four main types of Casein which make up approximately 80% of the total protein in bovine milk: α-s1 Casein, α-s2 Casein, β-Casein, and κ-Casein. Casein is proposed to be the main protective constituent in milk.

Biochem/physiol Actions

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. It can serve as an indispensable diet for rodents.
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.

Quality

Essentially vitamin free.

Preparation Note

Lactic acid precipitated New Zealand casein extracted with ethyl alcohol.

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Zealyn Shi-Lin Heng et al.
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Tauqeerunnisa Syeda et al.
Journal of Alzheimer's disease : JAD, 66(4), 1657-1682 (2018-11-27)
Recent investigations have demonstrated an important role of gut microbiota (GM) in the pathogenesis of Alzheimer's disease (AD). GM modulates a host's health and disease by production of several substances, including lipopolysaccharides (LPS) and short-chain fatty acids (SCFAs), among others.
Comparison between the digestive behaviors of a new in vitro rat soft stomach model with that of the in vivo experimentation on living rats-Motility and morphological influences
Chen L, et al.
Journal of Food Engineering, 117(2), 183-192 (2013)
Impact of dietary proteins on energy balance, insulin sensitivity, and glucose homeostasis: From proteins to peptides to amino acids
The Molecular Nutrition of Amino Acids and Proteins, 241-264 (2016)

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