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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:
EC Number:
MDL number:
NACRES:
NA.61

biological source

bovine milk

Quality Level

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

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This Item
E0789C9801C6780
assay

≥70% (PAGE)

assay

>90% dry basis

assay

≥90% (colorimetric)

assay

≥70% αs-casein basis (electrophoresis)

form

lyophilized powder

form

powder

form

essentially salt-free, lyophilized powder

form

lyophilized powder

technique(s)

isoelectric focusing (IEF): suitable

technique(s)

enzyme immunoassay: suitable

technique(s)

activity assay: suitable

technique(s)

mass spectrometry (MS): suitable

storage temp.

−20°C

storage temp.

room temp

storage temp.

−20°C

storage temp.

−20°C

Quality Level

200

Quality Level

300

Quality Level

200

Quality Level

200

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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Customers Also Viewed

Slide 1 of 5

1 of 5

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)
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
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)
Hongjun Yu et al.
Proceedings of the National Academy of Sciences of the United States of America, 115(41), E9560-E9569 (2018-09-28)
The protein disaggregase ClpB hexamer is conserved across evolution and has two AAA+-type nucleotide-binding domains, NBD1 and NBD2, in each protomer. In M. tuberculosis (Mtb), ClpB facilitates asymmetric distribution of protein aggregates during cell division to help the pathogen survive
Aprianita Aprianita et al.
The Journal of dairy research, 81(2), 183-192 (2014-03-07)
This experiment was conducted to determine the effects of diets supplemented with cottonseed oil, Acacia mearnsii-condensed tannin extract, and a combination of both on composition of bovine milk. Treatment diets included addition of cottonseed oil (800 g/d; CSO), condensed tannin from

Articles

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

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