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Key Documents

Altri documenti

C6905

Sigma-Aldrich

β-Casein from bovine milk

BioUltra, ≥98% (PAGE)

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About This Item

Numero CAS:
9000-71-9
Numero CE:
232-555-1
Numero MDL:
MFCD00130619
Codice UNSPSC:
12352202
NACRES:
NA.61

Origine biologica

bovine milk

Nome Commerciale

BioUltra

Saggio

≥98% (PAGE)

Forma fisica

essentially salt-free, lyophilized powder

tecniche

activity assay: suitable

N° accesso UniProt

P02666
P02668

Temperatura di conservazione

−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)
BECPQYXYKAMYBN-UHFFFAOYSA-N

Informazioni sul gene

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

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Descrizione generale

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.

Applicazioni

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.

Azioni biochim/fisiol

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.

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 1

Dispositivi di protezione individuale

Eyeshields, Gloves, type N95 (US)

Certificati d'analisi (COA)

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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
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Articoli

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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