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Merck
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Documentos clave

C3400

Sigma-Aldrich

Casein from bovine milk

powder

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About This Item

Número de CAS:
Número CE:
Número MDL:
Código UNSPSC:
12352202
NACRES:
NA.61
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origen biológico

bovine milk

Ensayo

87-94% protein basis

Formulario

powder

técnicas

activity assay: suitable
electrophoresis: suitable
immunocytochemistry: suitable

mp

280 °C (dec.) (lit.)

solubilidad

H2O: insoluble (forms a cloudy suspension)

Nº de acceso UniProt

cadena SMILES

[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)

Clave InChI

BECPQYXYKAMYBN-UHFFFAOYSA-N

Información sobre el gen

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Descripción general

Casein from bovine milk is a phosphoprotein and forms three-dimensional colloidal supramolecular micelles.[1] There are four main types of casein which make up approximately 80% of the total protein in bovine milk: α-s1 casein, α-s2 casein, β-casein, and κ-casein.[2] Casein is proposed to be the main protective constituent in milk. Casein is an amphiphilic protein.[3]

Aplicación

Casein from bovine milk has been used:
  • as a solid food sample in the in vivo and the in vitro digestion experiments using rodents[3]
  • to prepare P407-casein hydrogels and to study the mechanical effects of the addition of casein to P407[4]
  • in the preincubation solution, to increase the photostability of the quantum dots and to decrease nonspecific binding, for real-time imaging of single synaptic vesicles in hippocampal neurons[5]

Casein from bovine milk is a phosphoprotein. There are four main types of Casein which make up approximately 80% of the total protein in bovine milk: α-s1 Casein, α-s2 Casein, β-Casein, and κ-Casein. Casein is proposed to be the main protective constituent in milk.

Acciones bioquímicas o fisiológicas

Casein is useful in food industries and non-food applications. It has the property for emulsification, foam formation, and stabilization, water-binding, and gelation. Casein is also considered heat and acid stable.[6] It can serve as an indispensable diet for rodents.[3]
Partial gastrointestinal digestion of casein is a rich source of bioactive peptides, such as β-casomorphin. However, bovine casein is not homogeneous; variants A1 and B do lead to production of β-casomorphin 7 production, while A2 does not.

Calidad

Essentially vitamin free.

Nota de preparación

Lactic acid precipitated New Zealand casein extracted with ethyl alcohol.

Código de clase de almacenamiento

11 - Combustible Solids

Clase de riesgo para el agua (WGK)

WGK 1

Equipo de protección personal

Eyeshields, Gloves, type N95 (US)


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Encyclopedia of Food Chemistry (2019)
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Journal of plant physiology, 165(7), 679-690 (2007-11-13)
The regulation of UDP-Glc pyrophosphorylase (UGPase) isozyme, UGP5, was investigated in potato tuber. The cDNA for UGP5 was cloned into the bacterial expression vector pET21d and recombinant (RC) enzyme was expressed in E. coli (BL21 star cells). The RC-UGP5 isozyme
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The spatiotemporal aspects of early signaling events during interactions between cells and their environment dictate multiple downstream outcomes. While advances in nanopatterning techniques have allowed the isolation of these signaling events, a major limitation of conventional nanopatterning methods is its

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