Analytical Data
-
Gene name
Lpa
- Application
-
Alternative Names
Lpa；Liprin-alpha-2
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q92633
-
Expression Region
1-364aa
-
AA Sequence
MAAISTSIPVISQPQFTAMNEPQCFYNESIAFFYNRSGKHLATEWNTVSK LVMGLGITVCIFIMLANLLVMVAIYVNRRFHFPIYYLMANLAAADFFAGL AYFYLMFNTGPNTRRLTVSTWLLRQGLIDTSLTASVANLLAIAIERHITV FRMQLHTRMSNRRVVVVIVVIWTMAIVMGAIPSVGWNCICDIENCSNMAP LYSDSYLVFWAIFNLVTFVVMVVLYAHIFGYVRQRTMRMSRHSSGPRRNR DTMMSLLKTVVIVLGAFIICWTPGLVLLLLDVCCPQCDVLAYEKFFLLLA EFNSAMNPIIYSYRDKEMSATFRQILCCQRSENPTGPTEGSDRSASSLNH TILAGVHSNDHSVV
-
Molecular Weight
68 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
Lpa (Lipoprotein(a)) is a lipoprotein variant that consists of low-density lipoprotein (LDL) and a specific protein known as apolipoprotein(a). Elevated levels of Lpa in the bloodstream have been identified as a significant risk factor for cardiovascular diseases, including atherosclerosis, heart attacks, and strokes. The unique structure of Lpa, particularly the varying size of apolipoprotein(a) due to genetic polymorphisms, complicates its study and has led to challenges in understanding its biological functions and implications. As traditional lipid-lowering therapies do not effectively reduce Lpa levels, there is a critical need for targeted research to explore Lpa's role in lipid metabolism and its contribution to cardiovascular pathology. Recent advancements in recombinant protein technology have paved the way for the production of Lpa in laboratory settings, enabling researchers to study its properties, mechanisms of action, and interactions with other lipids and proteins in greater detail. The development of novel therapeutic strategies that specifically target Lpa represents a promising avenue for reducing cardiovascular risk and improving patient outcomes. Overall, ongoing research in Lpa recombinant proteins aims to unravel the complexities of this lipoprotein and its potential as a therapeutic target in cardiovascular disease management.
