Analytical Data
-
Gene name
Enolase 3/ENO3
- Application
-
Alternative Names
(2-phospho-D-glycerate hydro-lyase)(Enolase 3)(Muscle-specific enolase)(MSE)(Skeletal muscle enolase)
-
Species
Bovine
-
Source
E. coli
-
Tag
N- His & C- Myc
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q3ZC09
-
Expression Region
2-434aa
-
Molecular Weight
54.4 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
Enolase 3, also known as ENO3, is a key glycolytic enzyme that plays a crucial role in the conversion of 2-phosphoglycerate to phosphoenolpyruvate, facilitating energy production in cells. It exists in multiple isoforms, with ENO3 being predominantly expressed in muscle and brain tissues. Research on ENO3 has garnered attention due to its involvement in various physiological and pathological processes, including muscle glycolytic capacity, cancer metabolism, and neurodegenerative diseases. The study of recombinant ENO3 protein is pivotal for elucidating its biochemical properties, regulatory mechanisms, and interactions with other metabolic pathways. Furthermore, characterizing ENO3 as a potential biomarker or therapeutic target could provide insights into diseases associated with altered energy metabolism. Advances in recombinant DNA technology have enabled the production of ENO3 in heterologous systems, allowing for detailed functional studies and high-throughput screenings for inhibitors or modulators. Understanding this enzyme's structure-function relationship may open new avenues for therapeutic intervention in metabolic disorders and enhance our knowledge of muscle function and plasticity under varying physiological conditions. Overall, the exploration of recombinant ENO3 not only underscores its importance in fundamental biology but also highlights its potential implications in clinical research and therapeutic development.
