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Key Documents

C6905

Sigma-Aldrich

β-Casein from bovine milk

BioUltra, ≥98% (PAGE)

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About This Item

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

biological source

bovine milk

Quality Level

product line

BioUltra

Assay

≥98% (PAGE)

form

essentially salt-free, lyophilized powder

technique(s)

activity assay: suitable

UniProt accession no.

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

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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.

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

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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)
Bovine milk allergens: a comprehensive review
Villa C, et al.
Comprehensive Reviews in Food Science and Food Safety, 17(1), 137-164 (2018)
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
F Valentino et al.
Soft matter, 12(47), 9429-9435 (2016-11-11)
Pulling membrane nanotubes from liposomes presents a powerful method to gain access to membrane mechanics. Here we extend classical optical tweezers studies to infer membrane nanotube dynamics with high spatial and temporal resolution. We first validate our force measurement setup
Jun-Ling Zhang et al.
PloS one, 7(9), e44618-e44618 (2012-09-08)
Secreted protein acidic and rich in cysteine (SPARC) is a glycoprotein that functions to inhibit angiogenesis, proliferation, and invasion in different types of cancer. The ability of SPARC to modulate neovascularisation is believed to be mediated in part by its

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