Background:  Myristate, a rare 14 carbon saturated fatty acid, is cotranslationally attached by an amide linkage to the N terminal glycine residue of cellular and viral proteins with diverse functions. Methionine aminopeptidase cleaves the N terminal methionine from newly synthesized NMT protein substrates to expose N terminal glycine residues. N myrisotylation appears to be irreversible and is required for full expression of the biologic activities of several known N myristoylated proteins. For example, N myristoylation of the alpha subunit of the signal transducing guanine nucleotide binding protein (G protein) G0 increases its affinity for beta gamma subunits and thereby promotes formation of the heterotrimeric complex. Myristoyl CoA:protein N myristoyltransferase catalyzes the transfer of myristate from CoA to proteins. Insertional mutagenesis of the NMT1 gene in Saccharomyces cerevisiae causes recessive lethality, indicating that N myristoylation provides an essential function for one or more of the approximately 12 proteins of this yeast that are substrates for NMT. Duronio et al. (1992) isolated cDNAs encoding human NMT by complementing a point mutation of this gene in Saccharomyces cerevisiae that causes temperature sensitive myristic acid auxotrophy. Human NMT is encoded by a single copy gene, contains 416 amino acids, and is 44% identical to the yeast NMT.

Description: Rabbit polyclonal to NMT1

Immunogen: KLH conjugated synthetic peptide derived from NMT1

Specificity:  ·Reacts with Human, Mouse and Rat.

·Isotype: IgG

Application:  ·Western blotting: 1/100-500. Predicted Mol wt: 57 kDa;

·Immunohistochemistry (Paraffin/frozen tissue section): 1/100-500;

·Immunocytochemistry: 1/100-200;

·ELISA: 1/500;

· Optimal working dilutions must be determined by the end user.