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Validated All-in-One™ qPCR Primer for AQP2(NM_000486.5) Search again
Product ID:
HQP009705
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
AQP-CD, NDI2, WCH-CD
Gene Description:
aquaporin 2
Target Gene Accession:
NM_000486.5(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 encodes a water channel protein located in the kidney collecting tubule. It belongs to the MIP/aquaporin family, some members of which are clustered together on chromosome 12q13.
Gene References into function
- increase in urinary AQP2 excretion during normal pregnancy without there being a significant increase in plasma AVP
- mutations cause autosomal dominant nephrogenic diabetes insipidus
- Misrouting, instead of a lack of function, is a mechanism for the 'loss of function' phenotype in nephrogenic diabetes insipidus
- changes in urinary excretion of aquaporin-2 indicates circulatory blood volume depletion, and estimates the AVP-dependent recovery of circulatory blood volume during the therapeutic period in patients with diabetic ketoacidosis
- Two novel aquaporin-2 mutations responsible for congenital nephrogenic diabetes insipidus in Chinese families.
- Most AQP2 missense mutants in recessive NDI are retained in the endoplasmic reticulum (ER), but AQP2-T125M and AQP2-G175R were reported to be nonfunctional channels unimpaired in their routing to the plasma membrane.
- in collecting duct cells, AQP2 trafficking to vasopressin-sensitive vesicles is phosphorylation-independent and phosphorylation of Ser-256 is necessary for expression of AQP2 in the apical membrane
- A mutation screen of AQP2 in 12 individuals with Meniere's disease did not identify any sequence alterations or mutations within the four coding exons of AQP2 and their intron-exon junctions.
- The excretion of AQP-2 in urine is abnormal both in liver cirrhosis in which we find less suppression of u-AQP2 by an acute water load and in heart failure with a high baseline level and an exaggerated suppression of u-AQP2 by an acute water load.
- Mixed oligomers of wild-type and mutant AQP2s are mistargeted to basolateral membrane due to dominant-negative effect of mutant. Likely explains pathogenesis of autosomal-dominant nephrogenic diabetes insipidus.
- Data suggest the involvement of different protein quality control processes in the processing of aquaporin 2 mutants.
- reduction in the amounts of AQP-2 and AQP-3 expression, especially in lesions with substantial interstitial fibrosis and nephron loss, as compared with a healthy region of normal kidneys.
- glycosylation is essential for exit from the Golgi complex and sorting of AQP2 to the plasma membrane.
- Data report a frame-shift mutation in aquaporin-2 causing dominant nephrogenic diabetes insipidus.
- Where renal water retention is stimulated via arginine vasopressin (AVP), urinary AQP2 measurements provide a reproducible measurement of the renal actions of AVP.
- population of the Mexican town with nephrogenic diabetes insipidus; 30% of the population was heterozygous for the V168M AQP2 mutation and 1% was homozygous for the mutation.
- AQP2 resides in a recycling compartment at the apical side in polarized MDCK-hAQP2 cells, and its retrieval uses the apical endosomal system and the phosphatidylinositol 3-kinase-dependent pathway.
- exaggerated urinary excretion of AQP-2 is dependent on baroreceptor-mediated release of arginine vasopressin in patients with congestive heart failure.
- The distribution and expression levels of AQP2 in normal human tissue.
- crystallization of recombinantly expressed human AQP2 into two-dimensional protein-lipid arrays and their structural characterization by atomic force microscopy and electron crystallography
- increased protein abundance of ENaC subunits as well as the increased apical targeting of AQP2 may contribute to renal sodium and water retention observed during the development of hypertension in spontaneously hypertensive rats
- Differential regulation of AQP2 trafficking in endosomes by microtubules and actin filaments
- This study shows that aldosterone treatment perturbs diabetes insipidus and is associated with AQP2 redistribution in CNT and iCCD
- The sequence at 256-271 is sufficient for apical trafficking in AQP-2.
- hyperosmolality plays an important role in the stability, degradation, expression, and targeting of ng-AQP2
- data indicate that AQP2 constitutively recycles between the apical membrane and intracellular vesicles in principal cells in situ
- The high level of endometrial AQP2 expression was observed at the mid-secretory phase, the time of embryo implantation, suggesting that AQP2 might play physiological roles in the uterine receptivity.
- After VP stimulation of renal epithelial cells, AQP2 accumulates at the cell surface, while the V2R is actively internalized. This endocytotic block may involve a reduced capacity of phosphorylated AQP2 to interact with the endocytotic machinery.
- AQP2 mutation in NDI families and perinatal mutation testing is of direct clinical value because early diagnosis and treatment can avert the physical and mental retardation associated with repeated episodes of dehydration.
- The disorder nephrogenic diabetes insipidus (NDI) is inherited in an X-linked or autosomal fashion due to mutations in the genes encoding V2R or AQP2, respectively.
- Two novel mutations were identified in each of AVPR2 and AQP2 underlying Congenital Nephrogenic Diabetes Insipidus in Arab families.
- Increase in urine osmolality and creatinine clearance during the diuretic phase, paralleled by an increase in total AQP2 excretion, suggests that AQP2 can contribute to the urinary concentrating ability early in postnatal life.
- Results demonstrate that a mutant monomer of aquaporin 2 gains a dominant-negative effect that reverses the normal polarized sorting of multimers.
- The presence of AQP2 in human endometrium was also confirmed by RT-PCR. CONCLUSION(S): AQP2 is present in the human endometrium.
- Of note, homology modeling revealed that the two mutations involve two highly conserved residues providing important clues about the role of the wt residues in AQP2 stability and function.
- Urinary AQP2 excretion was absent in patients with severely debilitating mutations, a novel total deletion of the A VPR2 gene, and a novel nonsense mutation W296X.
- 70-kDa heat shock proteins as a AQP2 interactors and have shown for hsc70 that this interaction is involved in AQP2 trafficking.
- Our data indicate that no association exists between the -667 AQP-2 A/G polymorphism and susceptibility to chronic kidney disease or its clinical course.
- vasopressin-induced Ca2+ signal including calmodulin, myosin light chain kinase, calmodulin kinase II, and calcineurin have been implicated in the regulation of aquaporin-2 trafficking and/or water permeability--REVIEW
- A homozygous mutation, R85X, was detected in the aquaporin 2 gene (AQP2) of our patient, which has been described only once previously.
- we describe the role of actin at each step of intracellular reservation, exocytosis, docking, fusion with the plasma membrane, and endocytosis, focusing on aquaporin-2 trafficking--REVIEW
- The aim of this study was to use immunohistochemsitry to investigate the expression of aquaporins 1, 2 and 3 within the human intervertebral disc.
- annexin-2 is required for cAMP-induced AQP2 exocytosis in renal cells
- there are associations between several AQP2 SNPs and the risk of venous thrombosis, and weak associations with arterial blood pressure, but not with plasma levels of VWF propeptide, VWF or FVIII
- AQP2 mutations in nephrogenic diabetes insipidus (Review)
- Dynamic interactions between AQP2 and the actin cytoskeleton are critical for initiating AQP2 apical targeting.