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Key Documents

C9801

Sigma-Aldrich

Casein, N,N-dimethylated from bovine milk

essentially salt-free, lyophilized powder

Synonyma:

N,N-dimethylcasein

Přihlásitk zobrazení cen stanovených pro organizaci a smluvních cen


About This Item

Číslo CAS:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.61

biological source

bovine milk

assay

≥90% (colorimetric)

form

essentially salt-free, lyophilized powder

technique(s)

activity assay: suitable

UniProt accession no.

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

General description

Casein is a milk protein, that is not expensive and nontoxic. highly stable. This phosphoproteins accounts for 80% of the total protein present in bovine milk. Casein is a member of one of the larger family of secretory calcium?binding phosphoproteins.

Application

Casein, N,N-dimethylated from bovine milk has been used:
  • in the determination of general proteolytic activity
  • as a substrate to study the effect of dephosphorylation on the calcium-activated neutral proteases (CANP) proteolysis of paired helical filaments (PHF) II-τ
  • in transglutaminase (TG) assay

Casein, N,N-dimethylated from bovine milk can be used in assays to detect and help determine the functional role of tissue transglutaminase (tTG) in disease. In particular, Casein, N,N-dimethylated has been used in the mechanic and kinetic analysis of tTG on protein substrates, which may be linked to neurodegenerative disease.

This preparation has less than 10% reactivity with 2,4,6-trinitrobenzenesulfonic acid (TNBS) compared to non-methylated casein.

Protease substrate that has been used to assay basilase and a subtilisin analog that had been produced by site-directed mutagenesis.

Biochem/physiol Actions

Casein is highly preferred as a drug delivery vehicle. It possess antioxidant activity.

Preparation Note

Reductive methylation of C5890 by the method of Cabacungan, J.C., et al., Anal. Biochem., 124, 272 (1982).

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


Osvědčení o analýze (COA)

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Zákazníci si také prohlíželi

Molecular effects of nicarbazin on avian reproduction
Yoder CA, et al.
Poultry Science, 85(7), 1285-1293 (2006)
Casein proteins: structural and functional aspects
Milk proteins-from structure to biological properties and health aspects. InTech, Rijeka, 1-17 (2016)
H Grøn et al.
European journal of biochemistry, 194(3), 897-901 (1990-12-27)
The subtilisins are known to be susceptible to chemical oxidation due to the conversion of Met222 into the corresponding sulfoxide. A number of derivatives with resistance towards oxidation have previously been prepared by replacement of this group with the other
Johannes Wolf et al.
Analytical biochemistry, 411(1), 10-15 (2010-12-15)
Tissue transglutaminase (tTG) is a calcium-dependent enzyme that exerts a variety of physiological functions and is involved in various pathoprocesses. To characterize the role of tTG in disease, simple assays are necessary for detection. We developed a highly sensitive enzyme-linked
Dephosphorylation of Alzheimer paired helical filaments by protein phosphatase-2A and- 2B
Wang JZ, et al.
The Journal of Biological Chemistry, 270(9), 4854-4860 (1995)

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