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Validated All-in-One™ qPCR Primer for ATP2A1(NM_004320.4) Search again
Product ID:
HQP011898
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
ATP2A, SERCA1
Gene Description:
ATPase sarcoplasmic/endoplasmic reticulum Ca2+ transporting 1
Target Gene Accession:
NM_004320.4(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 encodes one of the SERCA Ca(2+)-ATPases, which are intracellular pumps located in the sarcoplasmic or endoplasmic reticula of muscle cells. This enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen, and is involved in muscular excitation and contraction. Mutations in this gene cause some autosomal recessive forms of Brody disease, characterized by increasing impairment of muscular relaxation during exercise.
Gene References into function
- Modeling of the inhibitory interaction of phospholamban with the Ca2+ ATPase.
- regulation by sarcolipin's involvement in binding to transmembrane helices alone or in association with phospholamban
- kinetic analysis of SERCA1 and SERCA2 isoforms and the effects of mutation
- The coexistence of SERCA1 and -2, together with complex mixtures of MyHCs in most of the fibers provide the human EOMs with a unique molecular portfolio that allows a highly specific fine-tuning regimen of contraction and relaxation.
- The combination of these histological and immunoblot results is consistent with the hypothesis that diaphragm remodeling elicited by severe COPD is characterized by a fast-to-slow SERCA isoform transformation.
- SERCA1 gene transfer increased fractional myocardial cell shortening (compared to LacZ) and accelerated relengthening kinetics.
- We suggest that aberrant splicing of SERCA1 mRNAs might contribute to impaired Ca2+ homeostasis in DM1 muscle
- The maximal turnover rates of the ATPase activity for SPCA1 isoforms were 4.7-6.4-fold lower than that of SERCA1a (lowest for the shortest SPCA1a isoform).
- SERCA1, 2, and 3 sensitivity to thapsigargin is dependent on a phenylalanine 256 to valine mutation
- a functional abnormality in SERCA1 may have a role in inferior oblique overaction, an ocular motor disorder
- Preload stimulates SERCA expression. BNP antagonizes this mechanism. Inhibition of cGMP-dependent protein kinase restored preload-dependent SERCA upregulation in the presence of recombinant human BNP.
- Despite similar total calcium contents, lower SERCA and PMCA activities were found in sacs associated with hydrocele compared to those associated with undescended testis suggest a difference among the levels of cytosolic calcium.
- Our studies point to an important regulation of SERCA1b expression at the protein level and hints to a role in the growth of the developing muscle.
- Overexpression of the CUG repeat expansion of DMPK mRNA resulted in exclusion of exon 22 of SERCA1.
- Ca (2+) binding to Site I of SERCA1a in fact slightly reduces Trp fluorescence, and consequently that the rise in this fluorescence generally observed when two Ca (2+) ions bind to WT SERCA1a mainly reflects Ca (2+) binding at Site II of SERCA1a.
- the increase in mechanical efficiency of cycling occurring during first weeks of endurance training may be due to down-regulation of SERCA pumps
- The truncated variant of the sarcoendoplasmic reticulum Ca(2+)-ATPase 1 (S1T) amplifies endoplasmic reticulum stress through the PERK-eIF2alpha-ATF4-CHOP pathway.