LDLR Protein, Mouse (Biotinylated, A23V, C27G, HEK293, His)

LDLR Protein crucially binds to LDL, transporting cholesterol through endocytosis. Clustering into clathrin-coated pits initiates internalization. Interactions with DAB2, LDLRAP1, ARRB1, SNX17, and immature PCSK9 contribute to its functional versatility. The NPXY motif interaction is impaired by tyrosine phosphorylation. LDLR Protein, Mouse (Biotinylated, A23V, C27G, HEK293, His) is the recombinant mouse-derived LDLR protein, expressed by HEK293 , with C-His labeled tag and A23V, C27G mutation. The total length of LDLR Protein, Mouse (Biotinylated, A23V, C27G, HEK293, His) is 790 a.a., with molecular weight of ~85.7 kDa.

The LDLR protein plays a crucial role in binding to LDL, the primary lipoprotein responsible for transporting cholesterol in the bloodstream, and facilitating its internalization into cells through endocytosis. To undergo internalization, receptor-ligand complexes must first cluster into clathrin-coated pits. Additionally, LDLR interacts with various proteins, including DAB2 and LDLRAP1 through its NPXY motif, with the interaction impaired by tyrosine phosphorylation of the NPXY motif. It also interacts with ARRB1 and SNX17, further contributing to its functional versatility. Furthermore, LDLR interacts with the immature form of PCSK9, aiding in the regulation of LDL cholesterol levels.

Mouse

HEK293

C-His

P35951 (M1-R790, A23V, C27G)

16835  [NCBI]

Approximately 85.7 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.