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The different forms of phospholamban (show PLN ELISA Kits) in zebrafish may provide a novel SERCA regulatory mechanism.
study showed that accordian acc(dta5) mutants harbor a novel mutation in atp2a1; indicate the acc(dta5) mutation diminishes SERCA1 function to a greater degree than other acc alleles through haploinsufficient or dominant-negative molecular mechanisms
encodes the sarco(endo)plasmic reticulum Ca2+-ATPase 1 (SERCA1), a Ca2 (show CA2 ELISA Kits)+ pump found in the muscle sarcoplasmic reticulum (SR) that is responsible for pumping Ca2 (show CA2 ELISA Kits)+ from the cytosol back to the SR
concluded that the motility dysfunction in embryonic and larval accordion zebrafish stems directly from defective calcium transport in skeletal muscle due to mutation in SERCA rather than defective CNS drive.
Atp2a1/serca1 is expressed as soon as the end of gastrulation in a subset of the myod (show MYOD1 ELISA Kits)-positive cells, and later labels prospective slow muscle cells in the superficial part of the somite.
Cell functions regulated by protein-protein interactions of the SERCA1a-sarcolipin (show SLN ELISA Kits) complex is accomplished via s-palmitoylation and s-oleoylation of sarcolipin (show SLN ELISA Kits).
The changes in expression of SERCA1 potentially disturb the normal Ca2 (show CA2 ELISA Kits)+ channel as well as the balance of Ca2 (show CA2 ELISA Kits)+ homeostasis.
the major SR membrane lipid PC is optimal for all steps and, unlike the other headgroups, contributes favorable electrostatics and non-electrostatic elements during the Ca-ATPase (show CA-P60A ELISA Kits) transition
ATP-dependent Ca(2 (show CA2 ELISA Kits)+) transport by SERCA (show ATP2A3 ELISA Kits) in single giant unilamellar vesicles was detected directly using confocal fluorescence microscopy.
Here we describe the methods to analyze these processes in the transport cycle with a representative member of P-type ATPase (show ATP7A ELISA Kits) family, SERCA1a, sarco(endo)plasmic reticulum Ca(2+)-ATPase (show CA-P60A ELISA Kits)
oligonucleotide-based drugs could be used to fine-tune SERCA (show ATP2A3 ELISA Kits) function to counterbalance the extent of the pathological insults.
Inhibition of the sarco/endoplasmic reticulum Ca2+-ATPase (show ATP2A3 ELISA Kits) (SERCA1) by rutin derivatives.
Infrared spectroscopy was used to characterise recombinant sarcoplasmic reticulum Ca2+-ATPase (SERCA1a).
Data show that biselyngbyasides (BLSs) bind to the pump SERCA1a calcium ATPase (show CA-P60A ELISA Kits) near the cytoplasmic surface of the transmembrane region.
Rescue of mutated SERCA1 to sarcoplasmic reticulum membrane can re-establish resting cytosolic Ca(2 (show CA2 ELISA Kits)+) concentration and prevent the appearance of pathological signs of cattle pseudomyotonia
Conformation of the SERCA1A calcium ATPase (show CA-P60A ELISA Kits) in the presence of different lipids.
CAPN3 (show CAPN3 ELISA Kits) deficiency leads to degradation of SERCA (show ATP2A3 ELISA Kits) proteins and Ca2 (show CA2 ELISA Kits)+ dysregulation in the skeletal muscle.
Ebf3 (show EBF3 ELISA Kits) binds directly to the promoter of Atp2a1 and synergises with MyoD (show MYOD1 ELISA Kits) in the induction of Atp2a1
Formalin evokes calcium transients from the endoplasmatic reticulum via SERCA1-dependent, TRPA1-independent mechanism that may underlie formaldehyde-induced pan-neuronal excitation and subsequent inflammation.
SERCA1b is considered to play an essential role in the regulation of [Ca2 (show CA2 ELISA Kits)+]i and its ab ovo gene silencing results in decreased skeletal muscle differentiation.
Data show that in healthy transgenic mice, cardiac-specific sarcoplasmic reticulum calcium ATPase (show CA-P60A ELISA Kits) SERCA1a expression increased active cell-surface glucose transporter GLUT4 (show SLC2A4 ELISA Kits) and glucose uptake in the myocardium.
Data suggest that the cardiac depressant properties of neuronostatin possibly associated with loss of sarcoplasmic reticulum Ca2+-ATPase SERCA (show ATP2A3 ELISA Kits) phosphorylation.
Results indicated that sine oculis homeobox (show PRRX1 ELISA Kits) 1 (Six1 (show SIX1 ELISA Kits)) overexpression could significantly promote the expression of fast-type muscle genes Atp2a1, Srl (show SRL ELISA Kits), and Mylpf (show MYLPF ELISA Kits).
Protein levels of CSQ1 (show CASQ1 ELISA Kits), SERCA1, and SERCA2 (show ATP2A2 ELISA Kits) are re-adjusted in skeletal muscles depending on the demands of diverse exercise training programs.
dystrophic phenotype observed in delta-sarcoglycan (show SGCD ELISA Kits)-null (Sgcd (show SGCD ELISA Kits)(-/-)) mice and dystrophin (show DMD ELISA Kits) mutant mdx (show DMD ELISA Kits) mice is dramatically improved by skeletal muscle-specific (show EIF3K ELISA Kits) overexpression of sarcoplasmic reticulum Ca(2+) ATPase 1 (SERCA1)
Sarcolipin (show SLN ELISA Kits) is a novel regulator of SERCA (show ATP2A3 ELISA Kits) pump activity, and its inhibitory effect can be reversed by beta-adrenergic agonists.
These results suggest that sAnk1 interacts with SLN (show SLN ELISA Kits) both directly and in complex with SERCA1 and reduces SLN's inhibitory effect on SERCA1 activity.
The sphingolipid sphingosine increases the [Ca(2 (show CA2 ELISA Kits)+)]i by inhibiting the sarco(endo)plasmic reticulum Ca(2+)-ATPase (SERCA (show CA-P60A ELISA Kits)), in a similar manner to thapsigargin (Tg), a specific inhibitor of this Ca(2 (show CA2 ELISA Kits)+) pump.
Thus the human SERCA1b has a different expression pattern from that of rodents and it is associated with DM2 (show CNBP ELISA Kits).
We conclude that PLB (show PLN ELISA Kits) C-terminal residues are critical for localization, oligomerization, and regulatory function. In particular, the PLB (show PLN ELISA Kits) C terminus is an important determinant of the quaternary structure of the SERCA (show ATP2A3 ELISA Kits) regulatory complex.
Aberrant splicing of SERCA1 may alter intracellular Ca(2 (show CA2 ELISA Kits)+) signalling in myotonic dystrophy 1 and 2 myotubes. The differing dysregulation of intracellular Ca(2 (show CA2 ELISA Kits)+) handling in DM1 (show DMPK ELISA Kits) and DM2 (show CNBP ELISA Kits) may explain their distinct sarcolemmal hyperexcitabilities.
We performed a detailed study of SERCA1 protein expression in muscle of patients with BD and BS, and evaluated the alternative splicing of SERCA1 in primary cultures of normal human muscle
These results indicate that PKC signaling is involved in the splicing of SERCA1 and provide new evidence for a link between alternative splicing and PKC signaling.
both topology and function of PLN (show PLN ELISA Kits) are shaped by the interactions with lipids, which fine-tune the regulation of SERCA (show ATP2A3 ELISA Kits)
Results demonstrate that a cattle congenital pseudomyotonia is caused by a SERCA1 deficiency, resulting from a defect in the ATP2A1 gene
crystal structure of SERCA (show ATP2A3 ELISA Kits), crystallized in the E1 conformation and determined at 2.9A resolution
Mutation in ATP2A1 is associated with congenital muscular dystony type 1
study reports the identification of a missense mutation in ATP2A1 in congential pseudomytonia of Chianina cattle; mutation analysis of ATP2A1 exons revealed a perfectly associated missense mutation in exon 6 (c.491G>A) leading to p.Arg164His substitution
In this study, we provide biochemical evidence for a selective deficiency in SERCA1 protein levels in sarcoplasmic reticulum membranes from Chianina cattle with congenital pseudomyotonia
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. Alternative splicing results in two transcript variants encoding different isoforms.
ATPase, Ca++ transporting, fast twitch 1
, sarcoendoplasmic reticulum calcium ATPase
, ATPase, Ca++ transporting, cardiac muscle, fast twitch 1
, ATPase, Ca++ transporting, cardiac muscle, slow twitch 2
, sarcoplasmic/endoplasmic reticulum calcium ATPase 1-like
, ATPase, Ca++ transporting, slow twitch 2
, sarcoplasmic/endoplasmic reticulum calcium ATPase 1
, ATPase, Ca++ transporting, ubiquitous
, SR Ca(2+)-ATPase 1
, calcium pump 1
, calcium-transporting ATPase sarcoplasmic reticulum type, fast twitch skeletal muscle isoform
, endoplasmic reticulum class 1/2 Ca(2+) ATPase