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M4414

Sigma-Aldrich

Myristoyl coenzyme A lithium salt

≥80.0% (HPLC), powder, protein myristoylation substrate

Sinónimos:

n-Tetradecanoyl Coenzyme A lithium salt

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About This Item

Fórmula empírica (notación de Hill):
C35H62N7O17P3S · xLi+
Número de CAS:
187100-75-0
Peso molecular:
977.89 (free acid basis)
UNSPSC Code:
12352202
NACRES:
NA.77

Nombre del producto

Myristoyl coenzyme A lithium salt, ≥80.0%

Quality Level

200

assay

≥80.0%

storage temp.

−20°C

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Biochem/physiol Actions

Myristoyl coenzyme A is a combination of coenzyme A and myristate. It serves as a substrate in protein myristoylation, catalyzed by the enzyme N-myristoyl transferase. Myristyolation involves the transfer of the myristoyl group to the glycine residue at the amino-terminal of the protein.

Features and Benefits

This compound is a featured product for Cyclic Nucleotide research. Click here to discover more featured Cyclic Nucleotide products. Learn more about bioactive small molecules for other areas of research at sigma.com/discover-bsm.

Substrates

Long chain fatty acid (C14) covalently linked to Coenzyme A. Substrate for de novo fatty acid synthesis. Fatty acylation has been shown to block G protein-associated calcium release by a direct allosteric modification of a component of the GTP-activated process.

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)

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Certificados de análisis (COA)

Lot/Batch Number
SLBT8502
SLBG3952V
SLBB8309V
080M5063V
080M5063

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Functional significance of myristoyl moiety in N-myristoyl proteins.
L J Knoll et al.
Methods in enzymology, 250, 405-435 (1995-01-01)
Signal Transduction - Single Cell Techniques, 327-327 (2008)
F Dittrich et al.
European journal of biochemistry, 252(3), 477-485 (1998-04-18)
Elongation of long-chain fatty acids was investigated in yeast mutants lacking endogenous de novo fatty acid synthesis. In this background, in vitro fatty acid elongation was dependent strictly on the substrates malonyl-CoA, NADPH and a medium-chain or long-chain acyl-CoA primer
K E Rys-Sikora et al.
The Journal of biological chemistry, 269(50), 31607-31613 (1994-12-16)
A sensitive and specific GTP-activated Ca2+ translocation process induces rapid Ca2+ movements within cells and appears to reflect G protein-induced membrane fusion or junctional communication between discrete subpopulations of Ca(2+)-pumping organelles (Ghosh, T. K., Mullaney, J. M., Tarazi, F. I.
C M D Swarbrick et al.
Acta crystallographica. Section D, Biological crystallography, 71(Pt 4), 986-995 (2015-04-08)
Acyl-CoA thioesterases catalyse the hydrolysis of the thioester bonds present within a wide range of acyl-CoA substrates, releasing free CoASH and the corresponding fatty-acyl conjugate. The TesB-type thioesterases are members of the TE4 thioesterase family, one of 25 thioesterase enzyme
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Discover Bioactive Small Molecules for Cyclic Nucleotides

Cyclic nucleotides, including cyclic AMP (cAMP), cyclic GMP (cGMP) and cyclic ADP-ribose, have been extensively studied as second messengers of intracellular events initiated by activation of GPCRs. cAMP modifies cell function in all eukaryotic cells, principally through the activation of cAMP-dependent protein kinase (PKA), but also through cAMP-gated ion channels and guanine nucleotide exchange factors directly activated by cAMP.

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