Analytical Data
-
Gene name
Lpa
- Application
-
Alternative Names
Lp(a); AK38; APOA; LP; Sinking Pre-β-Lipoprotein
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P08519
-
Expression Region
Asp1719~Arg2038
-
Molecular Weight
39kDa
-
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
Lipoprotein-associated phospholipase A2 (Lp-PLA2) is an enzyme that plays a crucial role in lipid metabolism and cardiovascular disease. It is primarily produced by macrophages and is associated with low-density lipoprotein (LDL) particles in the bloodstream. Elevated levels of Lp-PLA2 have been linked to atherosclerosis and coronary artery disease, making it a potential biomarker for cardiovascular risk assessment. The enzyme catalyzes the hydrolysis of oxidized phospholipids, leading to the release of lysophosphatidylcholine and free fatty acids, which can promote inflammatory responses and plaque instability. Consequently, Lp-PLA2 has emerged as a target for therapeutic intervention, inspiring research into the development of Lp-PLA2 inhibitors that could mitigate cardiovascular events. Recent advances in recombinant protein technology have enabled the production of Lp-PLA2 in a more standardized and effective manner, allowing researchers to better understand its biochemical properties and interactions within biological systems. By elucidating the structure-function relationship of Lp-PLA2 through recombinant protein studies, scientists are aiming to clarify its role in disease pathogenesis and to explore its potential as a drug target, thus opening new avenues for the prevention and treatment of cardiovascular diseases.
