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Merck

C3400

Casein from bovine milk

powder

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A propos de cet article

Numéro CAS:
9000-71-9
UNSPSC Code:
12352202
NACRES:
NA.61
EC Number:
232-555-1
MDL number:
MFCD00081481
Form:
powder
Assay:
87-94% protein basis
Biological source:
bovine milk

Principaux documents

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SMILES string

[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 key

BECPQYXYKAMYBN-UHFFFAOYSA-N

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)

biological source

bovine milk

assay

87-94% protein basis

form

powder

technique(s)

activity assay: suitable, electrophoresis: suitable, immunocytochemistry: suitable

mp

280 °C (dec.) (lit.)

solubility

H2O: insoluble (forms a cloudy suspension)

UniProt accession no.

P02662, P02663, P02666, P02668

Quality Level

200

Gene Information

bovine ... CSN1S1(282208), CSN1S2(282209), CSN2(281099), CSN3(281728)

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General description

Casein from bovine milk is a phosphoprotein and forms three-dimensional colloidal supramolecular micelles. 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. Casein is an amphiphilic protein.

Application

Casein from bovine milk has been used:
  • as a solid food sample in the in vivo and the in vitro digestion experiments using rodents
  • to prepare P407-casein hydrogels and to study the mechanical effects of the addition of casein to P407
  • 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

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.

Biochem/physiol Actions

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. It can serve as an indispensable diet for rodents.
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.

Preparation Note

Lactic acid precipitated New Zealand casein extracted with ethyl alcohol.

Analysis Note

Essentially vitamin free.

Classe de stockage

11 - Combustible Solids

wgk

WGK 1

ppe

Eyeshields, Gloves, type N95 (US)

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Certificats d'analyse (COA)

Lot/Batch Number
0000522643
0000522644
0000522644
0000522643
0000482230

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Encyclopedia of Food Chemistry (2019)
Peng Wu et al.
Journal of food science, 82(6), 1387-1394 (2017-05-05)
Previously, a dynamic in vitro rat stomach system (DIVRS-I) designed based on the principles of morphological bionics was reported. The digestibilities of casein powder and raw rice particles were found to be lower than those in vivo due to perhaps
Ercüment Aksakal et al.
Journal of enzyme inhibition and medicinal chemistry, 36(1), 885-894 (2021-03-24)
Here we investigated the effects of different levels of royal jelly in zebrafish (Danio rerio) diets [0.0% (D1); 0.1% (D2); 0.4% (D3); 1.6% (D4) vs 6.4% (D5)] on the activity and expression profiles of superoxide dismutase, catalase, glutathione reductase, glutathione
Zealyn Shi-Lin Heng et al.
Antibody therapeutics, 5(1), 30-41 (2022-02-12)
Optimizing recombinant antibody production is important for cost-effective therapeutics and diagnostics. With impact on commercialization, higher productivity beyond laboratory scales is highly sought, where efficient production can also accelerate antibody characterizations and investigations. Investigating HEK293E cells for mammalian antibody production
Sanjay K Gupta et al.
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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