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Validated All-in-One™ qPCR Primer for NPC1(NM_000271.4) Search again
Product ID:
HQP011887
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
NPC, POGZ, SLC65A1
Gene Description:
NPC intracellular cholesterol transporter 1
Target Gene Accession:
NM_000271.4(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
This gene was identified as the gene that when mutated, results in Niemann-Pick C disease. The encoded protein is a putative integral membrane protein that contains motifs consistent with a role in intracellular transport of cholesterol to post-lysosomal destinations. [provided by RefSeq].
Gene References into function
- Mutational analysis of the complete genomic sequence of NPC1 and characterization of haplotypes suggest that the expression of missense mutations is influenced by haplotypic background.
- Niemann-Pick C1 protein regulates cholesterol transport to the trans-Golgi network and plasma membrane caveolae.
- Review of NPC1 and HE1/NPC2 roles regulating cholesterol transport through endosomal/lysosomal system and in Niemann-Pick type C disease
- NPC2, NPC1 and MLN64 may act in an ordered sequence to sense cholesterol, effect sterol movement, and consequently, influence the process of vesicular trafficking.
- 15 mutations, eight of which were previously unreported, from Niemann-Pick type C disease patients
- Our results will contribute to defining the association between the clinical phenotypes and the genetic abnormalities in Niemann-Pick C disease.
- NPC1 and NPC2 have a role in the regulation of sterol homeostasis through generation of LDL cholesterol-derived oxysterols
- findings suggest that sequestration of theta-toxin to raft-enriched cell surface vesicles may underlie reduced sensitivity of NPC1-deficient cells to theta-toxin.
- Results demonstrate that there is direct binding between Niemann-Pick type C1 protein (NPC1) and azocholestanol, which does not require NPC2 but requires a functional sterol-sensing domain within NPC1.
- Data show that multiple signals are responsible for the trafficking of NPC1 to the endosomal compartment, including the dileucine motif and a previously unidentified signal residing within the putative sterol-sensing domain transmembrane domain 3.
- first example of a splicing defect due to a mutation in the lariat branch point sequence in an intron of NPC1, found in Niemann-Pick type C patients
- fatty acid flux through NPC1-deficient lysosomes is normal
- ATP7B resides in the late endosomes with Rab7 and the Niemann-Pick C1 protein and translocates copper from the cytosol to the late endosomal lumen, participating in biliary copper excretion via lysosomes
- Six novel NPC1 mutations were identified of which three are missense mutations located in the cysteine-rich domain. These are the first NPC1 mutations reported from Chinese patients with NPC.
- D787N and L657F are activating NPC1 mutations provide evidence for a conserved mechanism for the sterol-sensing domain among cholesterol homeostatic proteins.
- proposes a new hypothesis for the potential action or function of the NPC1 protein in the endosome; in this context, the relationship of NPC2 and NPC1 is also discussed.
- NPC1 has a role in a vesicle-mediated pathway responsible for the clearance of drugs from cells and provides an explanation for a drug sequestration phenotype exhibited by the MDR HL-60 cell line
- cholesterol contributes directly to the sequestration of Rab9 on Niemann-Pick type C cell membranes, which in turn, disrupts mannose 6-phosphate receptor trafficking
- Ubiquitylation of NPC1 and its association with the ESCRT complex are controlled by endosomal cholesterol levels utilizing a mechanism that involves NPC2.
- We report a Japanese patient with NPC caused by a homozygous c.2974 G > T mutation of the NPC1 gene,presenting with cataplexy at the age of 9 years and moderately low CSF-hypocretin 1 level.
- Modulation of human NPC1L1 expression and promoter activity by cholesterol in a =sterol regulatory element binding protein-2 dependent mechanism.
- NPC1 protein function is non-essential for the trafficking and removal of cellular cholesterol by ApoAI if the down-stream defects in ABCA1 and ABCG1 regulation in NPC disease cells are corrected using an LXR agonist
- mutations in the NPC1 gene impair verbal working memory more than visuospatial working memory
- human NPC1 can functionally substitute for the Caenorhabditis elegans genes ncr-1 and/or ncr-2.
- Sterol binding site on luminal loop-1 is not essential for NPC1 function in fibroblasts, but may function in other cells where NPC1 deficiency produces more complicated lipid abnormalities.
- novel approaches to treat NPC disease caused by the NPC1(I1061T) mutation
- Transport of LDL-derived cholesterol from late endosomes/lysosomes to the sterol-regulatory pool is regulated by the NPC1 protein and promotes feedback inhibition of the SREBP pathway.
- NPC-1 is sterol-regulated, achieved by SREBP protein acting via the sterol regulated element and the E-box sequences.
- Niemann-Pick C1 functions in regulating lysosomal amine content
- ATP7B localizes in the late endosomes. Copper in the late endosomes is transported to the secretory compartment via NPC1-dependent pathway and incorporated into apo-ceruloplasmin to form holo-ceruloplasmin.
- The use of fluorescent cholesterol analogs provides novel information on the molecular properties of the sterol-binding site in the full-length NPC1 protein.
- In addition to FTO and MC4R, we detected significant association of obesity with three new risk loci in NPC1 (endosomal/lysosomal Niemann-Pick C1 gene), near MAF (encoding the transcription factor c-MAF) and near PTER (phosphotriesterase-related gene).