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C6780

Sigma-Aldrich

α-Casein from bovine milk

≥70% αs-casein basis (electrophoresis), lyophilized powder

Synonym(s):

alpha-S1-casein, alpha-S2-casein

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About This Item

CAS Number:
9000-71-9
EC Number:
232-555-1
MDL number:
MFCD00130477
UNSPSC Code:
12352202
NACRES:
NA.61

biological source

bovine milk

Quality Level

200

Assay

≥70% αs-casein basis (electrophoresis)

form

lyophilized powder

technique(s)

mass spectrometry (MS): suitable

UniProt accession no.

P02662
P02663

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

cow ... CSN1(282208) , CSN1S2(282209)

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Application

α-Casein from bovine milk is an Immunoglobulin E (IgE)-binding epitope belonging to the Casein phosphoprotein family. It has been used in studies of children with insulin-dependent diabetes mellitus (IDDM), due to the strong cross-reactivity of α-casein antibodies with insulin. Studies of children displaying (IDDM) show higher levels of α-casein antibodies than control siblings, which may serve as a risk marker for IDDM.

Biochem/physiol Actions

α-Casein can be an immunogen in young children, and anti-a-casein antibodies have strong cross-reactivity with insulin. This effect can explain the uncommon insulin autoimmunity, but it does not appear to progress to Type I diabetes.

Preparation Note

Chromatographically purified

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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Richard D Unwin et al.
Nature protocols, 4(6), 870-877 (2009-05-16)
The application of a targeted mass spectrometric workflow to the sensitive identification of post-translational modifications is described. This protocol employs multiple reaction monitoring (MRM) to search for all putative peptides specifically modified in a target protein. Positive MRMs trigger an
T Saukkonen et al.
Diabetologia, 41(1), 72-78 (1998-03-14)
Dietary factors are suspected to play an aetiological role in the development of insulin-dependent diabetes mellitus (IDDM). We analysed cow's milk formula, betalactoglobulin, and bovine serum albumin antibodies by an enzyme-linked immunoassay in unselected children with newly diagnosed IDDM and
Andreas Luxenburger et al.
Molecules (Basel, Switzerland), 24(5) (2019-03-06)
In this study, we report on the modification of a 3,4-diaryl-isoxazole-based CK1 inhibitor with chiral pyrrolidine scaffolds to develop potent and selective CK1 inhibitors. The pharmacophore of the lead structure was extended towards the ribose pocket of the adenosine triphosphate
Serena Di Palma et al.
Nature protocols, 7(11), 2041-2055 (2012-10-27)
Multidimensional liquid chromatography (LC) combined with mass spectrometry (MS) has become a standard technique in proteomics to reduce sample complexity and to tackle the dynamic range in protein abundance. Fractionation is necessary to obtain a comprehensive analysis of complex biological
Simone Talens et al.
Thrombosis and haemostasis, 119(10), 1624-1631 (2019-08-23)
Many proteins bind to fibrin during clot formation in plasma. We previously identified by mass spectrometry the most abundant proteins that noncovalently bind to fibrin clots. Several of these proteins (e.g., apolipoprotein J/clusterin, haptoglobin, α2-macroglobulin, α1-antitrypsin) can act as extracellular
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