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B1508

Sigma-Aldrich

Butyryl coenzyme A lithium salt hydrate

≥90%

Sinonimo/i:

Butyryl-CoA lithium salt hydrate

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About This Item

Formula empirica (notazione di Hill):
C25H42N7O17P3S · xLi+ · yH2O
Peso molecolare:
837.62 (free acid basis)
Numero MDL:
MFCD00038616
Codice UNSPSC:
41106305
ID PubChem:
329773188
NACRES:
NA.51

Saggio

≥90%

Forma fisica

powder

Temperatura di conservazione

−20°C

Stringa SMILE

[Li+].[Li+].[Li+].[Li+].CCCC(=O)Nc1ncnc2n(cnc12)[C@@H]3O[C@H](COP([O-])(=O)OP([O-])(=O)OCC(C)(C)C(O)C(=O)NCCC(=O)NCCS)[C@@H](OP([O-])([O-])=O)[C@H]3O

InChI

1S/C25H42N7O17P3S.4Li/c1-4-5-16(34)31-21-17-22(29-12-28-21)32(13-30-17)24-18(35)19(48-50(38,39)40)14(47-24)10-45-51(41,42)49-52(43,44)46-11-25(2,3)20(36)23(37)27-7-6-15(33)26-8-9-53;;;;/h12-14,18-20,24,35-36,53H,4-11H2,1-3H3,(H,26,33)(H,27,37)(H,41,42)(H,43,44)(H2,38,39,40)(H,28,29,31,34);;;;/q;4*+1/p-4/t14-,18-,19-,20?,24-;;;;/m1..../s1
FKMUWGIOOMBTED-VLFKLNKMSA-J

Categorie correlate

Applicazioni

Butyryl CoA is a substrate for Butyryl CoA Dehydrogenase. Butyryl CoA is involved in both lipid and butanoate metabolism. Butyryl-CoA may be used as a substrate of various lipases and as an alternate substrate for 4-hydroxybutyrate CoA-transferase. Butyryl CoA may be used to study the newly discovered process of post-translational histone modification by butyrylation.

Azioni biochim/fisiol

Butyryl CoA is a substrate for Butyryl CoA Dehydrogenase. Butyryl CoA is involved in both lipid and butanoate metabolism.

Pittogrammi

Exclamation mark
GHS07

Avvertenze

Warning

Indicazioni di pericolo

H315,H319,H335

Classi di pericolo

Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3

Organi bersaglio

Respiratory system

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

dust mask type N95 (US), Eyeshields, Gloves

Certificati d'analisi (COA)

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C Biben et al.
Molecular and cellular biology, 14(5), 3504-3513 (1994-05-01)
A DNase I-hypersensitive site analysis of the 5'-flanking region of the mouse alpha-cardiac actin gene with muscle cell lines derived from C3H mice shows the presence of two such sites, at about -5 and -7 kb. When tested for activity
Sofia Macieira et al.
Archives of microbiology, 194(3), 157-166 (2011-08-13)
Clostridium aminobutyricum ferments 4-aminobutyrate (γ-aminobutyrate, GABA) to ammonia, acetate and butyrate via 4-hydroxybutyrate that is activated to the CoA-thioester catalyzed by 4-hydroxybutyrate CoA-transferase. Then, 4-hydroxybutyryl-CoA is dehydrated to crotonyl-CoA, which disproportionates to butyryl-CoA and acetyl-CoA. Cocrystallization of the CoA-transferase with
Yue Chen et al.
Molecular & cellular proteomics : MCP, 6(5), 812-819 (2007-02-03)
The positively charged lysine residue plays an important role in protein folding and functions. Neutralization of the charge often has a profound impact on the substrate proteins. Accordingly all the known post-translational modifications at lysine have pivotal roles in cell
Li-Chiun Lee et al.
Journal of agricultural and food chemistry, 59(19), 10693-10698 (2011-08-23)
Recombinant Candida rugosa lipase 5 (LIP5) has been functionally expressed along with other isoforms in our laboratory. However, the characterization and codon optimization of LIP5 have not been done. In this work, we characterized, codon-optimized and compared LIP5 with commercial
Alison E Ringel et al.
Acta crystallographica. Section D, Structural biology, 72(Pt 7), 841-848 (2016-07-06)
Gcn5 is a conserved acetyltransferase that regulates transcription by acetylating the N-terminal tails of histones. Motivated by recent studies identifying a chemically diverse array of lysine acyl modifications in vivo, the acyl-chain specificity of the acetyltransferase human Gcn5 (Gcn5L2) was
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