Skip to Content
MilliporeSigma
All Photos(3)

Key Documents

View All Documentation

C6905

Sigma-Aldrich

β-Casein from bovine milk

BioUltra, ≥98% (PAGE)

Sign Into View Organizational & Contract Pricing
All Photos(3)

About This Item

CAS Number:
9000-71-9
EC Number:
232-555-1
MDL number:
MFCD00130619
UNSPSC Code:
12352202
NACRES:
NA.61

biological source

bovine milk

product line

BioUltra

assay

≥98% (PAGE)

form

essentially salt-free, lyophilized powder

technique(s)

activity assay: suitable

UniProt accession no.

P02666
P02668

storage temp.

−20°C

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

Gene Information

bovine ... CSN2(281099) , CSN3(281728)

Looking for similar products? Visit Product Comparison Guide

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.

Application

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.
It has been studied as a generator of peptides responsible for biological activities such as opiate, immunostimulating, antibacterial, and peptidase inhibitors.

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

11 - Combustible Solids

wgk_germany

WGK 1

ppe

Eyeshields, Gloves, type N95 (US)

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’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

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)
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)
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
Bence Hajdusits et al.
eLife, 10 (2021-07-31)
In Gram-positive bacteria, the McsB protein arginine kinase is central to protein quality control, labeling aberrant molecules for degradation by the ClpCP protease. Despite its importance for stress response and pathogenicity, it is still elusive how the bacterial degradation labeling
View All Related Papers

Articles

HPLC Analysis of Caseins on BIOshell™ A400 Protein C4

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

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service