Weight | 1 lbs |
---|---|
Dimensions | 9 × 5 × 2 in |
accession | P01130 |
express system | HEK293 |
product tag | C-His-Avi |
purity | > 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC |
background | The 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 weight | The 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 size | 100 µg, 500 µg |
endotoxin | Less than 1EU per μg by the LAL method. |
Human LDLR Protein 2987
$300.00 – $1,000.00
Summary
- Expression: HEK293
- Binding assay: Yes (SPR)
- Amino Acid Range: Ala22-Arg788
Human LDLR Protein 2987
protein |
---|
Size and concentration 100, 500µg and lyophilized |
Form Lyophilized |
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles. |
Storage buffer Shipped at ambient temperature. |
Purity > 95% as determined by Tris-Bis PAGE |
target relevance |
---|
The 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 names Low-density lipoprotein receptor (LDL receptor) |
Gene names LDLR,LDLR |
Protein family LDLR family |
Mass 95376Da |
Function FUNCTION: Binds 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). {ECO:0000269|PubMed:3005267, ECO:0000269|PubMed:30443021, ECO:0000269|PubMed:6091915}.; FUNCTION: (Microbial infection) Acts as a receptor for hepatitis C virus in hepatocytes, but not through a direct interaction with viral proteins. {ECO:0000269|PubMed:10535997, ECO:0000269|PubMed:12615904}.; FUNCTION: (Microbial infection) Acts as a receptor for Vesicular stomatitis virus. {ECO:0000269|PubMed:23589850}.; FUNCTION: (Microbial infection) In case of HIV-1 infection, may function as a receptor for extracellular Tat in neurons, mediating its internalization in uninfected cells. {ECO:0000269|PubMed:11100124}.; FUNCTION: (Microbial infection) Acts as a receptor for Crimean-Congo hemorrhagic fever virus (CCHFV). {ECO:0000269|PubMed:38182887}.; FUNCTION: (Microbial infection) Acts as a receptor for many Alphavirus, including Getah virus (GETV), Ross river virus (RRV) and Semliki Forest virus. {ECO:0000269|PubMed:38245515}. |
Subellular location SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17461796, ECO:0000269|PubMed:19520913}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P01131}. Membrane, clathrin-coated pit {ECO:0000303|PubMed:6091915}. Golgi apparatus {ECO:0000269|PubMed:17461796}. Early endosome {ECO:0000269|PubMed:17461796}. Late endosome {ECO:0000269|PubMed:17461796}. Lysosome {ECO:0000269|PubMed:17461796}. Note=Rapidly endocytosed upon ligand binding. Localized at cell membrane, probably in lipid rafts, in serum-starved conditions (PubMed:30443021). {ECO:0000269|PubMed:30443021, ECO:0000269|PubMed:3104336}. |
Structure SUBUNIT: Interacts (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). {ECO:0000250|UniProtKB:P35951, ECO:0000269|PubMed:12221107, ECO:0000269|PubMed:12944399, ECO:0000269|PubMed:14739284, ECO:0000269|PubMed:17461796, ECO:0000269|PubMed:21149300, ECO:0000269|PubMed:22509010, ECO:0000269|PubMed:30443021}.; SUBUNIT: (Microbial infection) Interacts with C.difficile toxin TcdA, suggesting that it may contribute to TcdA toxin entry into cells. {ECO:0000269|PubMed:31160825}.; SUBUNIT: (Microbial infection) Interacts with vesicular stomatitis virus glycoprotein. {ECO:0000269|PubMed:23589850}.; SUBUNIT: (Microbial infection) Interacts with Crimean-Congo hemorrhagic fever virus (CCHFV) glycoprotein C. {ECO:0000269|PubMed:38182887}.; SUBUNIT: (Microbial infection) Interacts with Getah virus (GETV) E2-E1 spike protein complex. {ECO:0000269|PubMed:38245515}.; SUBUNIT: (Microbial infection) May interact with HIV-1 Tat. {ECO:0000269|PubMed:11100124}. |
Post-translational modification PTM: N- and O-glycosylated. {ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19520913, ECO:0000269|PubMed:3005267}.; PTM: Ubiquitinated by MYLIP leading to degradation. {ECO:0000269|PubMed:19520913}. |
Domain DOMAIN: The NPXY motif mediates the interaction with the clathrin adapter DAB2 and with LDLRAP1 which are involved in receptor internalization. A few residues outside the motif also play a role in the interaction. {ECO:0000269|PubMed:22509010}. |
Target Relevance information above includes information from UniProt accession: P01130 |
The UniProt Consortium |
Data
Publications
Publications
pmid | title | authors | citation |
---|---|---|---|
We haven't added any publications to our database yet. |
Protocols
relevant to this product |
---|
Documents
# | ||
---|---|---|
Please enter your product and batch number here to retrieve product datasheet, SDS, and QC information. |