Analytical Data
-
Gene name
Pcmt
- Application
-
Alternative Names
L-isoaspartyl protein carboxyl methyltransferase Protein L-isoaspartyl/D-aspartyl methyltransferase Protein-beta-aspartate methyltransferase dPIMT
-
Species
Drosophila melanogaster
-
Source
E. coli
-
Tag
N- His & C- Myc
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q27869
-
Expression Region
1-226aa
-
Molecular Weight
32.0 kDa
-
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
PCMT (Protein-L-isoaspartate O-methyltransferase) is an important enzyme that plays a critical role in the repair of misfolded proteins by catalyzing the methylation of L-isoaspartate residues, which occur as a result of spontaneous deamidation and aging processes. The accumulation of L-isoaspartate can lead to protein aggregation and loss of function, contributing to various age-related diseases and neurodegeneration. Research on PCMT has gained momentum due to its potential therapeutic implications in treating Alzheimer's disease and other conditions associated with protein misfolding. Understanding the structure-function relationship of PCMT and its activity mechanisms is essential for developing targeted interventions that could enhance protein stability and reduce the prevalence of misfolded proteins in cellular environments. Furthermore, recombinant expression of PCMT allows for detailed biophysical studies and the examination of enzyme kinetics, which could aid in the identification of small molecule modulators. As the demand for biopharmaceuticals and targeted therapies increases, studying the functional aspects of PCMT could provide innovative approaches for disease prevention and treatment, ultimately contributing to improved healthspan and longevity in aging populations.
