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2-Hydroxymyristic acid

Inhibits protein myristoylation
 
BML-G230-0050 50 mg 59.00 USD
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Replaces Prod. #: ALX-300-131

Selective inhibitor of protein myristoylation in cells, able to distinguish myristoylation from palmitoylation. Metabolic activation in cultured cells (0.5 mM) appears to be required. Myristoylation takes place on glycine residues at the N-terminus of proteins and provides a strong membrane anchor for the modified proteins, many of which require myristoylation for full activity. Blocks p56lck mediated signal transduction and inhibits Varicella-zoster virus replication.

Product Specification

Alternative Name:2-Hydroxy-tetradecanoic acid
 
Formula:C14H28O3
 
MW:244.4
 
CAS:2507-55-3
 
Purity:≥97% (GC)
 
Appearance:White to off-white solid.
 
Solubility:Soluble in DMSO (25mg/ml) or 100% ethanol (25mg/ml).
 
Shipping:Shipped on Blue Ice
 
Long Term Storage:+4°C
 
Use/Stability:Stable for at least 2 years after receipt when stored at +4°C. Stock solutions are stable for up to 3 months at -20°C.
 
Scientific Background:p56lck and other members of the Src family of protein-tyrosine kinases as well as the αo, αi and αz subfamilies of G protein α subunits are covalently modified by N-myristoylation of their amino-terminal glycine residues. Myristoylation aids in membrane anchoring and is a requirement for full activity.
 
Technical Info/Product Notes:Note: Product is not sterile.
 
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Product Literature References

Dual acylation of PDE2A splice variant 3: targeting to synaptic membranes: C. Russwurm, et al.; J. Biol. Chem. 284, 25782 (2009), Abstract;
Inhibition of varicella-zoster virus replication by an inhibitor of protein myristoylation: D.R. Harper, et al.; J. Gen. Virol. 74, 1181 (1993), Abstract;
Reversible palmitoylation of the protein-tyrosine kinase p56lck: L.A. Paige, et al.; J. Biol. Chem. 268, 8669 (1993), Abstract; Full Text
Treatment of T cells with 2-hydroxymyristic acid inhibits the myristoylation and alters the stability of p56lck: M.J.S. Nadler, et al.; Biochemistry 32, 9250 (1993), Abstract;
The G protein connection: molecular basis of membrane association [published erratum appears in TIBS 17, 177 (1992)]: A.M. Spiegel, et al.; TIBS 16, 338 (1991), (Review), Abstract;
Activation of p56lck through mutation of a regulatory carboxy-terminal tyrosine residue requires intact sites of autophosphorylation and myristylation: N. Abraham & A. Veillette; Mol. Cell. Biol. 10, 5197 (1990), Abstract;
Metabolic activation of 2-substituted derivatives of myristic acid to form potent inhibitors of myristoyl CoA:protein N-myristoyltransferase: L.A. Paige, et al.; Biochemistry 29, 10566 (1990), Abstract;

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