Analytical Data
-
Gene name
aur
- Application
-
Alternative Names
Staphylococcus aureus neutral proteinase
-
Species
Staphylococcus aureus
-
Source
E. coli
-
Tag
N- His & C- Myc
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P81177
-
Expression Region
210-509aa
-
Molecular Weight
40.7 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
The study of aur proteins, particularly Aurora kinases, has gained significant attention due to their crucial role in cell cycle regulation and mitosis. Aurora kinases, specifically Aurora A, B, and C, are serine/threonine kinases that have been implicated in various cellular processes, including chromosome alignment, segregation, and cytokinesis. Dysregulation of these kinases is frequently associated with cancer, as they can contribute to genomic instability and uncontrolled cell proliferation. Research has shown that overexpression or mutation of Aurora kinases can lead to malignant transformation in several types of tumors, making them potential therapeutic targets. The development of specific inhibitors has emerged as a promising strategy for cancer treatment, with ongoing studies focused on understanding the detailed mechanisms of aur protein functions and interactions within the cell. Recent advancements in structural biology and biochemistry have enabled researchers to delve deeper into the functional domains of aur proteins, paving the way for the rational design of drugs that can selectively inhibit their activity. Furthermore, the exploration of their role in normal physiological processes and potential off-target effects of inhibitors remains critical in therapeutic contexts. Overall, the comprehensive study of aur proteins is essential not only for understanding fundamental cellular mechanisms but also for advancing cancer therapies.
