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C0406

Sigma-Aldrich

κ-Casein from bovine milk

≥70% (PAGE), lyophilized powder

Synonym(s):

Kappa-Casein

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About This Item

CAS Number:
EC Number:
MDL number:
UNSPSC Code:
12352202
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

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

11 - Combustible Solids

wgk_germany

WGK 1

ppe

Eyeshields, Gloves, type N95 (US)


Certificates of Analysis (COA)

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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
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
Caterina Villa et al.
Comprehensive reviews in food science and food safety, 17(1), 137-164 (2018-01-01)
Cow milk allergy is one of the most common food allergies in early childhood and often persists through adult life, forcing an individual to a complete elimination diet. Milk proteins are present in uncounted food products, such as cheese, yogurt
Presence of functional, autoreactive human milk-specific IgE in infants with cow's milk allergy.
Jarvinen KM., et al.
Clinical and Experimental Allergy (2011)
A study on bovine kappa-casein aggregation after the enzymatic action of chymosin.
Maria Eugenia Hidalgo., et al
Colloids Surf., 76, 556-563 (2010)

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