Recombinant Human LDL R Protein (C-6His)

Name: Recombinant Human LDL R Protein (C-6His)
Brand: Beta LifeScience
SKU: BL-0706NP
Availability: InStock

BL-0706NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Low-Density Lipoprotein Receptor is produced by our Mammalian expression system and the target gene encoding Ala22-Arg788 is expressed with a 6His tag at the C-terminus.
Accession	P01130
Synonym	Low-Density Lipoprotein Receptor; LDL Receptor; LDLR
Gene Background	Low-Density Lipoprotein Receptor (LDLR) is a transmembrane glycoprotein that plays a critical role in cholesterol homeostasis. LDLR mediates blood cholesterol level by interacting with lipoprotein particles like LDL and VLDL. The extracellular domain of LDLR contains LDL receptor type A (ligand-binding) modules (LA repeats), epidermal growth factor-like modules, and LY repeats containing the YWTD consensus motif that are important in binding and releasing of ApoB-100 and ApoE in lipoprotein particles. The C terminal domain of LDLR inside the cell is required for the receptor internalization. Loss of function mutations in the LDLR gene causes Familial Hypercholesterolemia (FH).
Molecular Mass	86.56 KDa
Apmol Mass	99-135 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of 20mM HEPES, 150mM NaCl, pH 7.4.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution	Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	Binds 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.; (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.
Subcellular Location	Cell membrane; Single-pass type I membrane protein. Membrane, clathrin-coated pit. Golgi apparatus. Early endosome. Late endosome. Lysosome.
Protein Families	LDLR family
Database References	HGNC: 6547 OMIM: 143890 KEGG: hsa:3949 STRING: 9606.ENSP00000454071 UniGene: PMID: 29660344 A randomized trial and novel SPR technique identifies altered lipoprotein-LDL receptor binding as a mechanism underlying elevated LDL-cholesterol in APOE4s PMID: 28276521 Authors performed an analysis of public databases and literature for every variant published associated with FH, in the genes LDLR, APOB, and PCSK9. PMID: 29261184 In this review we present a broad spectrum of functionally characterized missense LDLr variants identified in patients with Familial hypercholesterolemia (FH), which is mandatory for a definite diagnosis of FH. PMID: 29874871 The frequency of known mutations in the LDLR gene in this cohort of patients was markedly low compared to frequencies reported in other populations. PMID: 29720182 This study adds 9 novel variations and 11 recurrent variations to the spectrum of LDLR gene mutations in Indian population. The in silico analysis for all the variations detected in this study were done to predict the probabilistic effect in pathogenicity of Familial Hypercholesterolemia. PMID: 29269200 Data suggest maternal glycemic response during pregnancy is associated with lower DNA methylation of 4 CpG sites within PDE4B gene in placenta (collected after normal-weight term birth); 3 additional CpG sites are differentially methylated relative to maternal glucose response within TNFRSF1B, LDLR, and BLM genes. (PDE4B = phosphodiesterase-4B; TNFRSF1B = TNF receptor superfamily member-1B; BLM = Bloom syndrome protein) PMID: 29752424 Vesicular stomatitis virus G protein complex with two distinct cysteine-rich domains (CR2 and CR3) of LDL-R PMID: 29531262 Report familial hypercholesterolemia patients with multiple mutations at the LDLR gene presenting with more severe phenotype than single mutants. PMID: 28645073 LDLr in the activated PSFs may become a novel target receptor for controlled drug delivery. PMID: 28686975 Systematic mutation of the AREs (ARE1-3) in the LDLR 3'UTR and expression of each mutant coupled to a luciferase reporter in Huh7 cells demonstrated that ARE1 is required for rapid LDLR mRNA decay and 5-AzaC-induced mRNA stabilization via the IRE1alpha-EGFR-ERK1/2 signaling cascade. PMID: 29208426 The genotype-risk associations were examined between LDLR (rs885765, rs688, rs5925, rs55903358, rs5742911) and obesity-related phenotypes and other comorbidities in Sucre, Venezuela. The association between LDLR rs5742911 ancestral genotype A/A and high risk condition related to HDL-cholesterol was the only one found to be significant:(A/A: 41.50+/-14.81 mg/dL; A/G: 45.00+/-12.07 mg/dL; G/G: 47.17+/-9.43 mg/dL). PMID: 27622441 Heparan sulfate proteoglycans binding is required for PCSK9-induced LDLR degradation. PMID: 28894089 membrane LDLR was reduced and lost the ability to take up LDL. Our data also expand the spectrum of known LDLR mutations PMID: 29228028 Liposomes modified with both apolipoproteins A-I and E were internalized in HepG2 cells in FBS-depleted culture medium at the same levels as unmodified liposomes in FBS-containing culture medium, which indicates that apolipoproteins A-I and E were the major serum components involved in liposomal binding to SR-B1 or LDLR (or both). PMID: 28888368 These findings suggest that LDLR rs2738464 may affect the affinity of miR-330 binding to the LDLR 3'-UTR, thus regulating LDLR expression and contributing to clear cell renal cell carcinoma risk PMID: 29029037 the p.(Gly20Arg) change in the LDL receptor, previously described as disease causing, has no detrimental effect on protein expression or LDL particle binding PMID: 27175606 Twenty mutations including synonymous, missense, and intronic mutations were identified in the LDLR coding region of 32 Brazilian patients with familial hypercholesterolemia. PMID: 28873201 Results indicate the importance of the LDL receptor (LDLR) in the growth of triple-negative and HER2-overexpressing breast cancers in the setting of elevated circulating LDL cholesterol (LDL-C). PMID: 28759039 Identify LDLR, APOB and PCSK9 novel mutations causing familial hypercholesterolemia in the central south region of China. PMID: 28235710 This study updates the LDLR variant database and identifies a number of reported variants of unknown significance where additional family and in vitro studies will be required to confirm or refute their pathogenicity. PMID: 27821657 Data indicate that proteasomal degradation, lysosomal degradation, autophagy or ectodomain cleavage were not the underlying mechanism for degradation of these mutant LDLRs. PMID: 28334946 PCSK9 inhibits lipoprotein(a) clearance through the LDLR. PMID: 28750079 4 siblings found to be compound heterozygotes for 2 LDLR gene mutations but showing a different phenotype severity PMID: 27578127 LDLR is a relevant receptor for CNS drug delivery via receptor-mediated transcytosis and that the peptide vectors we developed have the potential to transport drugs PMID: 28108572 Higher Gleason grade was associated with lower LDLR expression, lower SOAT1 and higher SQLE expression. Besides high SQLE expression, cancers that became lethal despite primary treatment were characterized by low LDLR expression (odds ratio for highest versus lowest quintile, 0.37; 95% CI 0.18-0.76) and by low SOAT1 expression (odds ratio, 0.41; 95% CI 0.21-0.83). PMID: 28595267 LDLR associated with Familial Hypercholesterolemia and Polygenic Hypercholesterolemia in patients with Acute Coronary Syndrome , age /=160 mg/dl. PMID: 28958330 Chinese W483X mutation in the low-density lipoprotein-receptor gene in young patients with homozygous familial hypercholesterolemia PMID: 27206941 Proprotein convertase subtilisin/kexin 9 V4I variant with LDLR mutations modifies the phenotype of familial hypercholesterolemia PMID: 27206942 both LDLR rs6511720 and rs57217136 are functional variants; both these minor alleles create enhancer-binding protein sites for transcription factors and may contribute to increased LDLR expression, which is consequently associated with reduced LDL-C levels and 12% lower coronary heart disease risk PMID: 27973560 Using assays that measured conformational change, acid-dependent lipoprotein release, LDLR recycling, and net lipoprotein uptake, we show that H635 plays important roles in acid-dependent conformational change and lipoprotein release, while H264, H306, and H439 play ancillary roles in the response of the LDLR to acidic pH PMID: 27895090 these studies support that reductions in Lp(a) with PCSK9 inhibition are partly due to increased LDLR-mediated uptake. In most situations, Lp(a) appears to compete poorly with LDL for LDLR binding and internalization, but when LDLR expression is increased with evolocumab, particularly in the setting of low circulating LDL, Lp(a) is reduced. PMID: 27102113 Genetic etiology of familial hypercholesterolemia was confirmed in 103 probands following analysis of the whole LDLR gene in a Slovak population. PMID: 27824480 Heterozygous Familial Hypercholesterolemia patients with the null low-density lipoprotein (LDL) receptor DEL15Kb mutation develop severe Aortic Calcifications in an age- and gene dosage-dependent manner. PMID: 28449836 hepatocytes clear lipopolysaccharides from the circulation via the LDLR. PMID: 27171436 the zymogen form of PCSK9 adopts a structure that is distinct from the processed form and is unable to bind a mimetic peptide based on the EGF-A domain of the LDLr. PMID: 27534510 PCSK9 C-terminal domain (CTD) was found to be essential to induce LDLR degradation both upon its overexpression in cells or via the extracellular pathway. PMID: 27280970 LDLR mutation is associated in children and adolescent with familial hypercholesterolemia. PMID: 28161202 Even though LDLR-R410S and LDLR-WT were similar in levels of cell surface and total receptor and bound equally well to LDL or extracellular PCSK9, the LDLR-R410S was resistant to exogenous PCSK9-mediated degradation in endosomes/lysosomes and showed reduced LDL internalization and degradation relative to LDLR-WT. PMID: 27998977 study provides the first evidence that GPC3 can modulate the PCSK9 extracellular activity as a competitive binding partner to the LDLR in HepG2 cells. PMID: 27758865 ox-LDL play a role in the pathogenesis of AMD by NLRP3 inflammasome activation. Suppression of NLRP3 inflammasome activation could attenuate RPE degeneration and AMD progression. PMID: 27607416 Proprotein Convertase Subtilisin/Kexin Type 9 (PCSK9) Single Domain Antibodies Are Potent Inhibitors of Low Density Lipoprotein Receptor Degradation. PMID: 27284008 This study demonstrated that IL-2 and IL-10 were related to gene polymorphisms of LDL-R, which might be involved in the development and progress of hypercholesterolemia. PMID: 27121486 Lipoprotein profiles get improved by liver-directed gene transfer of human LDLR gene in hypercholesterolaemia mice. PMID: 27350674 Multiple novel LDLR and ApoB mutations have been identified in a-United Kingdom-based cohort with familial hypercholesterolemia. PMID: 26748104 Mutations in LDLR is associated with coronary artery disease. PMID: 26927322 LDLR A(+)A(+) genotype, ApoB X(+) allele and ApoE E4 allele increased the risk of premature coronary artery disease by 1.8, 2.1 and 12.1 respectively. PMID: 27236033 The TT genotype of rs688 in the LDLR gene was not found to be associated with elevated levels of total cholesterol or LDL-C PMID: 25601895 Report increased intestinal cholesterol absorption and elevated serum cholesterol in families with primary hypercholesterolemia without mutations in LDLR. PMID: 26802983 We have used atomistic simulations to explore the complete SNP mutational space (227 mutants) of the LA5 repeat, the key domain for interacting with LDL that is coded in the exon concentrating the highest number of mutations. PMID: 26755827

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.