Analytical Data
-
Gene name
NMT1
- Application
-
Alternative Names
Myristoyl-CoA:protein N-myristoyltransferase 1; Glycylpeptide N-tetradecanoyltransferase 1
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P30419
-
Expression Region
Met1~Leu222
-
Molecular Weight
34kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
NMT1 (N-myristoyltransferase 1) is an essential enzyme involved in the post-translational modification of proteins through the addition of a myristoyl group, a process that significantly influences protein function, localization, and interactions. The study of NMT1 is particularly relevant in the context of various diseases, including cancer and infectious diseases, as it plays a crucial role in the life cycle of certain pathogens and the signaling pathways of host cells. Research has shown that myristoylation can affect cell signaling, membrane localization, and protein stability, thereby influencing cellular behaviors and disease progression. The recombinant expression of NMT1 allows for detailed investigations into its enzymatic mechanisms, substrate specificity, and potential as a therapeutic target. Moreover, understanding NMT1's role in the myristoylation of key proteins may lead to the development of novel inhibitors that could disrupt pathogenic processes or promote tumor suppression. Consequently, the exploration of NMT1 as a recombinant protein not only enhances our understanding of myristoylation but also opens avenues for innovative strategies in drug development and therapeutic interventions against a range of diseases.
