Analytical Data
-
Gene name
LDLRAP1
- Application
-
Alternative Names
ARH1; ARH; ARH2; FHCB1; FHCB2; Autosomal recessive hypercholesterolemia protein
-
Species
Mouse
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q8C142
-
Expression Region
Met1~Phe308
-
Molecular Weight
42kDa
-
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
LDLRAP1 (Low-Density Lipoprotein Receptor Adaptor Protein 1) is a critical protein involved in the endocytosis of lipoproteins, particularly low-density lipoproteins (LDLs), by mediating the interaction between LDL receptors and the clathrin-coated pits on the cell membrane. Mutations in the LDLRAP1 gene are linked to a rare inherited condition known as familial hypercholesterolemia, which results in severely elevated cholesterol levels and an increased risk of cardiovascular diseases. Research on LDLRAP1 has gained momentum due to its significant role in lipid metabolism and cardiovascular health. Understanding the structure and function of LDLRAP1, particularly through the use of recombinant protein techniques, has been pivotal in elucidating the molecular mechanisms by which this protein facilitates LDL uptake. Moreover, studies have shown that LDLRAP1 is involved in other cellular processes beyond lipid regulation, including cell signaling and protein trafficking. Given the increasing prevalence of hypercholesterolemia and associated metabolic disorders worldwide, the functional analysis of LDLRAP1 through recombinant protein studies is essential for identifying potential therapeutic targets and developing innovative interventions aimed at managing cholesterol levels and reducing cardiovascular risks. Additionally, characterizing the interactions of LDLRAP1 with the LDL receptor and other cellular partners will provide insights into the complexities of lipid homeostasis and its impact on human health. Overall, the investigation of LDLRAP1 through recombinant protein methodologies represents a crucial step towards understanding its diverse roles in cellular function and its broader implications in metabolic diseases.
