|
ORF cDNA clones
|
CRISPR / TALEN
|
Lentivirus
|
AAV
|
TALE-TF
|
ORF knockin clones
|
|
Antibody
|
Proteins
|
miRNA target clones
|
qPCR primers
|
shRNA clones
|
miRNA products
|
Promoter clones
|
Validated All-in-One™ qPCR Primer for SCNN1G(NM_001039.3) Search again
Product ID:
HQP055230
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
BESC3, ENaCg, ENaCgamma, LDLS2, PHA1, PHA1B3, SCNEG
Gene Description:
sodium channel epithelial 1 subunit gamma
Target Gene Accession:
NM_001039.3(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:
|
|
| A | B |
|
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. |
|
Gene References into function
- Novel mutations responsible for autosomal recessive multisystem pseudohypoaldosteronism and sequence variants in epithelial sodium channel gamma-subunit gene.
- GammaENaC Asn530Ser mutation increases channel open probability and is consistent with abnormally high sodium reabsorption in distal nephron. First mutation in extracellular domain of ENaC subunit with increased ENaC activity and Liddle's syndrome.
- Not only are CFTR and ENaC activated together in duct salt absorption, but ENaC activation depends on functioning CFTR.
- in ulcerative colitis, elevated proinflammatory cytokines selectively impair beta- and gamma-ENaC expression, which contributes to diarrhea by reducing colonic sodium absorption.
- The roles of these missense mutations in the SCNN1B or SCNN1G gene identified in hypertensive patients are not clear in the pathogenesis of hypertension and the regulation of electrolytes.
- cAMP regulates ENaC in part by phosphorylation and inhibition of Nedd4-2. Moreover, Nedd4-2 is a central convergence point for kinase regulation of Na(+) transport.
- The ENaC expressed in the bladder epithelium might be implicated in the mechanosensory transduction in the bladder afferent pathways, thereby inducing detrusor instability by outlet obstruction.
- Common variants of the ENaC gamma subunit confer susceptibility to human essential hypertension.
- We conclude that overexpression of ClC-5, specifically amino acids 347-647, can alter the normal translation or trafficking of ENaC and other ion transport proteins by a mechanism that is independent of the chloride conductance of ClC-5.
- the interactions of delta-ENaC with alpha beta gamma-human epithelial sodium channel subunits could account for heterogeneity of native epithelial channels
- SCNN1G is a modulator in Cystic Fibrosis.
- These observations decisively prove that Rab27a inhibits ENaC function through a complex mechanism that involves GTP/GDP status, and protein-protein interactions involving Munc13-4 and SLP-5 effector proteins.
- 14-3-3 inhibits the interaction between the WW domains of hNedd4-2 and the PY motif of the epithelial Na(+) channel, ENaC
- A synthetic peptide corresponding to the fragment cleaved from the gamma subunit is a reversible inhibitor of endogenous ENaCs in cells; results suggest that multiple proteases cleave ENaC gamma subunits to fully activate the channel.
- Concerted action of short chain fatty acids and corticosteroid hormones is required for induction of ENaC and maintenance of intestinal electrogenic sodium absorption
- Results support a model whereby ubiquitin and clathrin adaptor binding sites act in concert to remove ENaC from the cell surface.
- This study found that co-expressed cystic fibrosis transmembrane conductance regulator (CFTR) stabilizes epithelial sodium channel(ENaC) at the plasma membrane, suggesting that CFTR regulates ENaC stability, not just opening.
- both mouse and human mammary cells express all ENaC subunits, and they are regulated by steroid hormones in a temporal and cell-specific manner both in culture and in vivo
- genetic variants in ENaCgamma (epithelial sodium channel gamma) genes do not modulate disease severity in the majority of CF patients
- Relatively common polymorphisms in the SCNN1G gene are associated with high systolic blood pressure in the general Australian white population.
- alpha- & beta-hnENaC protein was increased in cystic fibrosis tissue; gamma-hnENaC was decreased; Na+ hyperabsorption not caused by hnENaC mutations, but by an increase in transcription of hnENaC subunits
- protease binding and perhaps cleavage of the gamma subunit results in ENaC activation
- Several variants in ENaCbeta and gamma genes might be deleterious for ENaC function and lead to bronchiectasis.
- Alpha-, beta- and gamma-ENaC messenger RNAs are detected in amiloride-sensitive BeWo trophoblast cells.
- Plasmin activates epithelial Na+ channels by cleaving the gamma subunit
- support a model in which protons modulate ENaC gating by relieving Na(+) self-inhibition
- Plasmin in nephrotic urine activates the epithelial sodium channel