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View ProductsSize | 100ug, 50ug |
---|---|
Brand | ProteoGenix |
Product type | Recombinant Proteins |
Host Species | Escherichia coli (E. coli) |
Applications | Elisa, WB |
Product name | Human NPC1L1 Recombinant Protein |
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Uniprot ID | Q9UHC9 |
Uniprot link | http://www.uniprot.org/uniprot/Q9UHC9 |
Origin species | Homo sapiens (Human) |
Expression system | Prokaryotic expression |
Sequence | MAHNHRHKHKLRLRHLQVWSPEAQRNISLQDICYAPLNPDNTSLYDCCINSLLQYFQNNRTLLLLTANQTLMGQTSQVDW KDHFLYCANAPLTFKDGTALALSCMADYGAPVFPFLAIGGYKGKDYSEAEALIMTFSLNNYPAGDPRLAQAKLWEEAFLE EMRAFQRRMAGMFQVTFMAERS |
Molecular weight | 20,81 kDa |
Protein delivered with Tag? | Yes |
Purity estimated | 50% |
Buffer | PBS, imidazole 300mM in native conditions. |
Form | liquid |
Delivery condition | Dry Ice |
Delivery lead time in business days | 10-25 |
Storage condition | 4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection) |
Brand | ProteoGenix |
Host species | Escherichia coli (E.coli) |
Fragment Type | Partial |
Protein Accession | AAF20397.1 |
Spec:Entrez GeneID | 29881 |
Spec:NCBI Gene Aliases | NPC11L1 |
Spec:SwissProtID | Q9UHC9 |
NCBI Reference | AAF20397.1 |
Aliases /Synonyms | NPC1L1 [450-620], NPC1L1 protein, truncated Niemann-Pick C1-like protein 1 |
Reference | PX-P1131 |
Note | For research use only |
Human NPC1L1 (Niemann-Pick C1-Like 1) is a protein that plays a crucial role in cholesterol absorption in the small intestine. It is a key drug target for the treatment of hypercholesterolemia, a condition characterized by high levels of cholesterol in the blood. In this article, we will discuss the structure, activity, and application of Human NPC1L1 Recombinant Protein.
Human NPC1L1 is a transmembrane protein that is primarily expressed in the small intestine. It is composed of 13 transmembrane domains and a large extracellular loop. The protein has a molecular weight of approximately 145 kDa and is glycosylated, meaning it has sugar molecules attached to it.
The extracellular loop of Human NPC1L1 contains two putative cholesterol-binding sites, which are essential for the protein’s function in cholesterol absorption. The transmembrane domains are responsible for anchoring the protein in the cell membrane.
Human NPC1L1 plays a critical role in cholesterol absorption in the small intestine. It works by binding to cholesterol molecules in the intestinal lumen and transporting them into the enterocytes, the cells that line the small intestine. Once inside the enterocytes, cholesterol is packaged into chylomicrons and transported to the liver for further processing.
The activity of Human NPC1L1 is tightly regulated by various factors, including dietary cholesterol intake, bile acids, and hormones such as insulin and glucagon. When cholesterol intake is high, the expression of NPC1L1 is downregulated, reducing the absorption of cholesterol from the diet. This mechanism helps to maintain cholesterol homeostasis in the body.
The crucial role of Human NPC1L1 in cholesterol absorption makes it an attractive drug target for the treatment of hypercholesterolemia. Several pharmaceutical companies have developed inhibitors of NPC1L1, which work by blocking the protein’s activity and reducing cholesterol absorption from the diet.
One such inhibitor is ezetimibe, which is used in combination with statins to lower cholesterol levels in patients with hypercholesterolemia. Ezetimibe works by binding to the putative cholesterol-binding sites on Human NPC1L1, preventing cholesterol from being transported into the enterocytes.
In addition to its role as a drug target, Human NPC1L1 is also used in research studies to better understand its function and potential therapeutic applications. Recombinant Human NPC1L1 protein is widely available for purchase and can be used in various biochemical and cell-based assays to study its binding properties, expression, and activity.
In summary, Human NPC1L1 is a transmembrane protein involved in cholesterol absorption in the small intestine. It is composed of 13 transmembrane domains and a large extracellular loop and is regulated by various factors. The protein is a key drug target for the treatment of hypercholesterolemia and is also used in research studies. The availability of recombinant Human NPC1L1 protein allows for further exploration of its structure, activity, and potential therapeutic applications.
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