Analytical Data
-
Gene name
HRASLS
- Application
-
Alternative Names
PLAAT1; HRASLS; Phospholipase A and acyltransferase 1; EC 2.3.1.-; EC 3.1.1.32; EC 3.1.1.4; HRAS-like suppressor 1; HRSL1; Phospholipid-metabolizing enzyme A-C1
-
Species
Human
-
Source
E. coli
-
Tag
GST-tag at N-terminal
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9HDD0
-
Expression Region
1-168aa
-
AA Sequence
MAFNDCFSLNYPGNPCPGDLIEVFRPGYQHWALYLGDGYVINIAPVDGIPASFTSAKSVFSSKALVKMQLLKDVVGNDTYRINNKYDETYPPLPVEEIIKRSEFVIGQEVAYNLLVNNCEHFVTLLRYGEGVSEQANRAISTVEFVTAAVGVFSFLGLFPKGQRAKYY
-
Molecular Weight
45.2 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
HRASLS (HRAS-like suppressor) proteins are a family of enzymes that have garnered attention due to their potential roles in cellular processes and disease mechanisms. Initial studies suggested that HRASLS proteins act as lipid phosphate phosphohydrolases, implicating them in the regulation of lipid signaling pathways. Given their structural similarity to the HRAS oncogene, researchers are particularly interested in understanding how HRASLS may influence cancer progression and other diseases linked to dysregulated cell signaling. Recent evidence indicates that these proteins can modulate processes such as proliferation, apoptosis, and differentiation, positioning them as potential biomarkers or therapeutic targets in various cancers. Furthermore, HRASLS expression levels have been correlated with different cancer types, offering insights into their potential as prognostic indicators. Continued investigation into the biochemical properties and regulatory mechanisms of HRASLS proteins may reveal novel strategies for intervention in diseases characterized by aberrant signaling pathways, thus highlighting their relevance in both basic and applied biomedical research.
