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Safety Information

C6905

Sigma-Aldrich

β-Casein from bovine milk

BioUltra, ≥98% (PAGE)

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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

Quality Level

300

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

SMILES string

[P](=O)(OCC(NC(=O)C(NC(=O)C(N)Cc1ccccc1)CCC(=O)N)C(=O)NC(CCC(=O)O)C(=O)NC(CCC(=O)O)C(=O)NC(CCC(=O)N)C(=O)NC(CCC(=O)N)C(=O)NC(CCC(=O)N)C(=O)NC(C(O)C)C(=O)NC(CCC(=O)O)C(=O)NC(CC(=O)O)C(=O)NC(CCC(=O)O)C(=O)NC(CC(C)C)C(=O)NC(CCC(=O)N)C(=O)NC(CC(=O)O)C(=O)NC(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)

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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.

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.

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Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

动植物源性产品

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Certificates of Analysis (COA)

Lot/Batch Number
0000408988
0000408988
0000405958
0000406136
0000405990

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Bovine milk allergens: a comprehensive review
Villa C, et al.
Comprehensive Reviews in Food Science and Food Safety, 17(1), 137-164 (2018)
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
Georg Hierl et al.
Plant molecular biology, 84(6), 605-620 (2013-11-30)
Ricinosomes are specialized ER-derived organelles that store the inactive pro-forms of KDEL-tailed cysteine endopeptidases (KDEL-CysEP) associated with programmed cell death (PCD). The Arabidopsis genome encodes three KDEL-CysEP (AtCEP1, AtCEP2, and AtCEP3) that are differentially expressed in vegetative and generative tissues
Secreted protein acidic and rich in cysteine (SPARC) suppresses angiogenesis by down-regulating the expression of VEGF and MMP-7 in gastric cancer
Zhang JL, et al.
Testing, 7(9), e44618-e44618 (2012)
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
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