Low Density Lipoprotein Receptor (LDLR) (AA 22-788) (Active) protein (His tag)

Détails pour le produit réf. ABIN2181455, Fournisseur: Connectez-vous pour afficher
Nom de la protéine
  • FH
  • FHC
  • LDLCQ2
  • Hlb301
  • LDLRA
  • LDLA
  • low density lipoprotein receptor a
  • low density lipoprotein receptor
  • ldlra
  • LDLR
  • Ldlr
Attributs du protein
AA 22-788
11
4
4
4
2
1
1
1
1
1
1
1
1
1
1
1
1
Origine
Humain
22
12
2
2
Source
HEK-293 Cells
20
6
5
4
2
1
Type de proteíne
Recombinant
Activité biologique
Active
Purification/Conjugué
Cette LDLR protéine est marqué à la His tag.
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Fournisseur
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N° du produit (Fournisseur)
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Attributs du produit This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 86 kDa. The protein migrates as 95-110 kDa &125-140 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
Pureté >90 % as determined by SDS-PAGE.
Stérilité 0.22 μm filtered
niveau d'endotoxine Less than 1.0 EU per μg by the LAL method.
Nom de la protéine
Sujet Low-Density Lipoprotein (LDL) Receptor is also known as LDLR, FH, FHC, LDLCQ2, and is a mosaic protein of ~840 amino acids (after removal of signal peptide) that mediates the endocytosis of cholesterol-rich LDL. It is a cell-surface receptor that recognizes the apoprotein B100 which is embedded in the phospholipid outer layer of LDL particles. The receptor also recognizes the apoE protein found in chylomicron remnants and VLDL remnants (IDL). It belongs to the Low density lipoprotein receptor gene family. LDL receptor complexes are present in clathrin-coated pits (or buds) on the cell surface, which when bound to LDL-cholesterol via adaptin, are pinched off to form clathrin-coated vesicles inside the cell. This allows LDL-cholesterol to be bound and internalized in a process known as endocytosis and prevents the LDL just diffusing around the membrane surface. This occurs in all nucleated cells (not erythrocytes), but mainly in the liver which removes ~70 % of LDL from the circulation. Synthesis of receptors in the cell is regulated by the level of free intracellular cholesterol, if it is in excess for the needs of the cell then the transcription of the receptor gene will be inhibited. LDL receptors are translated by ribosomes on the endoplasmic reticulum and are modified by the Golgi apparatus before travelling in vesicles to the cell surface. LDL is directly involved in the development of atherosclerosis, due to accumulation of LDL-cholesterol in the blood. Atherosclerosis is the process responsible for the majority of cardiovascular diseases.
Poids moléculaire 86 kDa
NCBI Accession NP_000518
Pathways Hepatitis C, Lipid Metabolism
Restrictions For Research Use only
Format Lyophilized
Reconstitution Please see Certificate of Analysis for specific instructions. For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
Buffer PBS, pH 7.4
Conseil sur la manipulation Avoid repeated freeze-thaw cycles.
Stock -20 °C
Stockage commentaire No activity loss was observed after storage at: In lyophilized state for 1 year (4 °C-8 °C), After reconstitution under sterile conditions for 1 month (4 °C-8 °C) or 3 months (-20 °C to -70 °C).
Images (Fournisseur)
SDS-PAGE (SDS) image for Low Density Lipoprotein Receptor (LDLR) (AA 22-788) (Active) protein (His tag) (ABIN2181455) Human LDL R, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained ov...
Binding Studies (Bind) image for Low Density Lipoprotein Receptor (LDLR) (AA 22-788) (Active) protein (His tag) (ABIN2181455) Immobilized Human LDL R, His Tag (Cat# LDR-H5224) at 10 μg/mL (100 μl/well) can bind ...
Binding Studies (Bind) image for Low Density Lipoprotein Receptor (LDLR) (AA 22-788) (Active) protein (His tag) (ABIN2181455) Immobilized Human LDL R, His Tag (Cat# LDR-H5224) at 10 μg/mL (100 μl/well) can bind ...
Background publications Nomura, Merched, Nour, Dieker, Oka, Chan: "Low-density lipoprotein receptor gene therapy using helper-dependent adenovirus produces long-term protection against atherosclerosis in a mouse model of familial hypercholesterolemia." dans: Gene therapy, Vol. 11, Issue 20, pp. 1540-8, 2004 (PubMed).

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