Analytical Data
-
Gene name
APOL2
- Application
-
Alternative Names
Apo-L2; APOL-II
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9BQE5
-
Expression Region
Gln186~Gln337
-
Molecular Weight
20kDa
-
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
APOL2 (Apolipoprotein L2) is a member of the apolipoprotein family, which plays a crucial role in lipid metabolism and immune response. Research on APOL2 has gained attention due to its potential implications in various diseases, including cardiovascular disorders, metabolic syndromes, and certain cancers. Studies have shown that this protein can influence cholesterol transport and contribute to the regulation of plasma lipid levels. Moreover, APOL2 has been associated with the immune system, where it may play a role in modulating inflammatory responses. The understanding of APOL2's structural and functional properties is particularly important for elucidating its mechanisms in disease pathogenesis. Recent advancements in recombinant protein technology allow for the production of APOL2 in a controlled environment, facilitating detailed studies of its biochemical characteristics and interactions with other biomolecules. This research is vital for exploring potential therapeutic strategies that target APOL2-related pathways, ultimately aiming to enhance disease prevention and treatment.
