Analytical Data
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Gene name
SLN
- Application
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Alternative Names
SLN；Sarcolipin
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O00631
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Expression Region
1-31aa
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AA Sequence
MGINTRELFLNFTIVLITVILMWLLVRSYQY
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Molecular Weight
19.1 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
SLN (Sarcolipin) is a small integral membrane protein primarily expressed in skeletal muscle and cardiac tissue, where it plays a critical role in regulating calcium homeostasis and muscle contraction. The study of SLN has gained momentum due to its significant impact on energy metabolism and thermogenesis, particularly in the context of obesity and metabolic disorders. SLN is known to modulate the activity of the sarcoplasmic reticulum calcium ATPase (SERCA), influencing calcium uptake and muscle relaxation. Research indicates that SLN overexpression can improve muscle function and metabolic efficiency, while its dysfunction may contribute to various cardiac and metabolic diseases. Given the rising prevalence of obesity and related metabolic syndromes globally, understanding the molecular mechanisms underlying SLN's function could pave the way for novel therapeutic strategies. Additionally, recombinant SLN proteins are being explored for their potential in creating muscle-selective therapies and improving muscle regeneration. The ongoing investigation into SLN's structural characteristics, interaction with SERCA, and effects on muscle physiology is poised to advance our knowledge of muscle biology and its implications for metabolic health.
