Human LDLR Protein 2987

Additional Information:
accession P01130|express systemHEK293|product tagC-His-Avi|purity> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC|backgroundThe low density lipoprotein receptor (LDLR) is the founding member of the LDL R family of widely expressed cell surface scavenger receptors. It is a cell-surface receptor that recognizes the apoprotein B100 which is embedded in the phospholipid outer layer of LDL particles.|molecular weightThe protein has a predicted MW of 87.6 kDa, Due to glycosylation, the protein migrates to 110-130 kDa based on Tris-Bis PAGE result.|available size100 g, 500 g|endotoxinLess than 1EU per g by the LAL method.|Human LDLR Protein 2987proteinSize and concentration100, 500g and lyophilizedFormLyophilizedStorage InstructionsValid for 12 months from date of receipt when stored at -80C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.Storage bufferShipped at ambient temperature.Purity> 95% as determined by Tris-Bis PAGEtarget relevanceThe low density lipoprotein receptor (LDLR) is the founding member of the LDL R family of widely expressed cell surface scavenger receptors. It is a cell-surface receptor that recognizes the apoprotein B100 which is embedded in the phospholipid outer layer of LDL particles.Protein namesLow-density lipoprotein receptor (LDL receptor)Gene namesLDLR,LDLRProtein familyLDLR familyMass9606DaFunctionBinds low density lipoprotein /LDL, the major cholesterol-carrying lipoprotein of plasma, and transports it into cells by endocytosis. In order to be internalized, the receptor-ligand complexes must first cluster into clathrin-coated pits. Forms a ternary complex with PGRMC1 and TMEM97 receptors which increases LDLR-mediated LDL internalization (PubMed:30443021).; (Microbial infection) Acts as a receptor for hepatitis C virus in hepatocytes, but not through a direct interaction with viral proteins.; (Microbial infection) Acts as a receptor for Vesicular stomatitis virus.; (Microbial infection) In case of HIV-1 infection, may function as a receptor for extracellular Tat in neurons, mediating its internalization in uninfected cells.; (Microbial infection) Acts as a receptor for Crimean-Congo hemorrhagic fever virus (CCHFV).; (Microbial infection) Acts as a receptor for many Alphavirus, including Getah virus (GETV), Ross river virus (RRV) and Semliki Forest virus.Subellular locationCell membrane ; Single-pass type I membrane protein. Membrane, clathrin-coated pit. Golgi apparatus. Early endosome. Late endosome. Lysosome. Note=Rapidly endocytosed upon ligand binding. Localized at cell membrane, probably in lipid rafts, in serum-starved conditions (PubMed:30443021).StructureInteracts (via NPXY motif) with DAB2 (via PID domain); the interaction is impaired by tyrosine phosphorylation of the NPXY motif (By similarity). Interacts (via NPXY motif) with LDLRAP1 (via PID domain) (PubMed:12221107, PubMed:22509010). Interacts with ARRB1 (PubMed:12944399). Interacts with SNX17 (PubMed:14739284). Interacts with the full-length immature form of PCSK9 (via C-terminus) (PubMed:17461796, PubMed:21149300). Interacts with PGRMC1 and TMEM97; the interaction increases LDL internalization (PubMed:30443021).; (Microbial infection) Interacts with C.difficile toxin TcdA, suggesting that it may contribute to TcdA toxin entry into cells.; (Microbial infection) Interacts with vesicular stomatitis virus glycoprotein.; (Microbial infection) Interacts with Crimean-Congo hemorrhagic fever virus (CCHFV) glycoprotein C.; (Microbial infection) Interacts with Getah virus (GETV) E2-E1 spike protein complex.; (Microbial infection) May interact with HIV-1 Tat.Post-translational modificationN- and O-glycosylated.; Ubiquitinated by MYLIP leading to degradation.DomainThTarget Relevance information above includes information from UniProt accession: P01130The UniProt Consortium|