Myristoylation is an essential cotranslational modification for many mammalian, viral, and fungal signaling proteins. N-terminal
myristoylation is a lipid modification that is catalyzed by N-myristoyltransferase (NMT). NMT transfers myristic acid from myristoyl
coenzyme A to the amino group of a protein's N-terminal glycine residue. This modification is important for localization and/or function of
many of these proteins. Two human NMTs (NMT-1, NMT-2) have been identified. These proteins share 95% amino acid identity with their
mouse homologs. NMT-1 is processed to form four protein isoforms with molecular weights ranging from 49-68 kDa. It is not known if these
four isoforms are derived from single or multiple gene(s) and their exact functional roles are yet to be determined. In contrast to NMT-1,
NMT-2 is a single 65 kDa protein. It contains 77% sequence identity with NMT-1, indicating that these proteins comprise two distinct
families with overlapping, but distinct, substrate preferences. Additionally, NMT enzymatic activity is increased in colorectal tumors. Thus,
NMTs are transferases whose function is essential for biological function of a variety of signaling proteins.
原厂资料：
注意事项：
1.Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2.Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
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