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Sarcoplasmic reticulum Ca(2+)-ATPases are transmembrane proteins that catalyze the ATP-dependent transport of Ca(2+) from the cytosol into the lumen of the sarcoplasmic reticulum in muscle cells. Additionally we are shipping Sarcolipin Kits (7) and many more products for this protein.
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Cardiac function of Sln(Cre/+) mice was not significantly different from WT mice in all aspects that were examined.
the N termini of SLN and PLB (show PLN Antibodies) influence their respective unique functions
UCP1 (show UCP1 Antibodies) and SLN are required to maintain optimal thermogenesis and loss of both systems compromises survival of mice under cold stress
both SLN knockout (Sln(-/-)) and skeletal muscle-specific (show EIF3K Antibodies) SLN overexpression (Sln(OE)) mice to explore energy metabolism by pair feeding (fixed calories) and high-fat diet feeding (ad libitum)
overexpression of neither wild type nor FLAG-tagged variants of sarcolipin in transgenic mice had any major significant effects on body mass, energy expenditure, even when mice were fed on a high fat diet
SLN and PLN (show PLN Antibodies) are co-expressed in most fibers, which suggests that super-inhibition of SERCAs may be physiologically important in the regulation of intracellular Ca2 (show CA2 Antibodies)+ in human skeletal muscle.
results suggest that beta-AR signaling partially compensates for a lack of SLN to activate muscle-based DIT, but SLN is the primary and more effective mediator.
Sarcolipin deficiency increases the transport stoichiometry of SERCA (show ATP2A3 Antibodies) pumps and decreases the relative contribution of SERCA (show ATP2A3 Antibodies) pumps to resting oxygen consumption.
Data indicate that phospholamban (PLB (show PLN Antibodies)) is not involved in heat generation and that sarcolipin (SLN) alone is responsible for muscle thermogenesis.
During mouse muscle development SLN is highly expressed in embryonic muscle and plays role in regulation of sarcoplasmic reticulum Ca(2 (show CA2 Antibodies)+) stores during muscle differentiation
Although SLN and PLB (show PLN Antibodies) binding to SERCA (show ATP2A3 Antibodies) have different functional outcomes on the coupling efficiency of SERCA (show ATP2A3 Antibodies), both proteins decrease the apparent Ca(2 (show CA2 Antibodies)+) affinity of the pump, suggesting that SLN and PLB (show PLN Antibodies) inhibit SERCA (show ATP2A3 Antibodies) by using a similar mechanism.
The C-terminal tail of SLN is a distinct, essential domain in the regulation of SERCA (show ATP2A3 Antibodies).
The selective downregulation of SLN and enhanced sarcoplasmic reticulum Ca(2 (show CA2 Antibodies)+) uptake in human AF suggest that SLN downregulation could play an important role in abnormal intracellular Ca(2 (show CA2 Antibodies)+) cycling in atrial pathology.
sarcolipin binds to phospholamban (show PLN Antibodies) and inhibits polymerization
sarcolipin is likely to be an atrial chamber-specific regulator of Ca2 (show CA2 Antibodies)+ cycling in heart
role in regulating sarco(endo)plasmic reticulum Ca2+-ATPase by binding to transmembrane helices alone or in association with phospholamban (show PLN Antibodies)
Gene expression of SLN was studied in children with congenital heart defects.
Cell functions regulated by protein-protein interactions of the SERCA1a (show ATP2A1 Antibodies)-sarcolipin complex is accomplished via s-palmitoylation and s-oleoylation of sarcolipin.
The expression of SLN and PLB (show PLN Antibodies) mRNA and protein relative to SERCA1 (show ATP2A1 Antibodies) or SERCA2 (show ATP2A2 Antibodies) was assessed in ventricle, atrium, and skeltal msucle of mouse, rat, rabbit and pig.
Sarcoplasmic reticulum Ca(2+)-ATPases are transmembrane proteins that catalyze the ATP-dependent transport of Ca(2+) from the cytosol into the lumen of the sarcoplasmic reticulum in muscle cells. This gene encodes a small proteolipid that regulates several sarcoplasmic reticulum Ca(2+)-ATPases. The transmembrane protein interacts with Ca(2+)-ATPases and reduces the accumulation of Ca(2+) in the sarcoplasmic reticulum without affecting the rate of ATP hydrolysis.