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C0406

Sigma-Aldrich

κ-Casein from bovine milk

≥70% (PAGE), lyophilized powder

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Synonym(s):
Kappa-Casein
CAS Number:
9000-71-9
EC Number:
232-555-1
MDL number:
MFCD00081481
NACRES:
NA.61

biological source

bovine milk

Assay

≥70% (PAGE)

form

lyophilized powder

technique(s)

isoelectric focusing (IEF): suitable

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

cow ... MKCAS(100531419) , MKCASP(105755569)

General description

Caseins constitute 80% of the total milk proteins in the cow. κ-Casein is one of the major allergens in cow milk. It is a glycosylated protein comprising galactose, galactosamine, and sialic acid. It exists as tri- or tetrasaccharides and occurs in different isoforms based on the number of oligosaccharides attached to it. κ-Casein has a hydrophobic N-terminus and a hydrophilic C-terminus region.

Application

κ-Casein from bovine milk has been used:
  • as a standard to quantify the casein concentration and to evaluate the ability of the bacterial strain to hydrolyze caseins released by HM Mozzarella
  • in LPS-depleted cow′s milk protein preparation for lymphoproliferation assay
  • as standard to quantify κ-casein concentration in skimmed milk samples by reversed-phase high-performance liquid chromatography (RP-HPLC)

Biochem/physiol Actions

κ-Casein from bovine milk is an immunoglobulin E (IgE)-binding epitope belonging to the casein phosphoprotein family. κ-Casein is important to the electrostatic and steric stabilization of casein micelles suspensions. It resists calcium precipitation and therefore, stabilizes other caseins. κ-Casein has been a target of research for creating low-phenylalanine milk through gene modification, which is important for patients suffering from metabolic diseases such as phenylketonuria (PKU).

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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Control of Mozzarella spoilage bacteria by using bovine lactoferrin pepsin-digested hydrolysate
Worldwide Research Efforts in the Fighting Against Microbial Pathogens From Basic Research to Technological Developments, 118-122 (2013)
Genetic variants of bovine $\beta$-and $\kappa$-casein result in different immunoglobulin E-binding epitopes after in vitro gastrointestinal digestion
Lisson M, et al.
Journal of Dairy Science, 96, 5532-5543 (2013)
Mária Baranyi et al.
Journal of biotechnology, 128(2), 383-392 (2006-12-13)
Patients suffering certain metabolic diseases (e.g. phenylketonuria) need a low-phenylalanine diet throughout their lives. Transgenic rabbits were created to express low-phenylalanine kappa-casein in their milk. The aim was to demonstrate for the first time the feasibility of producing a modified
Paramjit S Bansal et al.
Biochemical and biophysical research communications, 340(4), 1098-1103 (2006-01-13)
The caseins (alphas1, alphas2, beta, and kappa) are phosphoproteins present in bovine milk that have been studied for over a century and whose structures remain obscure. Here we describe the chemical synthesis and structure elucidation of the N-terminal segment (1-44)
Antigen-specific T-cell responses in patients with non-IgE-mediated gastrointestinal food allergy are predominantly skewed to T(H)2.
Hideaki Morita et al.
The Journal of allergy and clinical immunology, 131(2), 590-592 (2012-10-23)
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