Recombinant Human Sarcolipin (SLN) Protein (His-KSI)

Name: Recombinant Human Sarcolipin (SLN) Protein (His-KSI)
Brand: Beta LifeScience
SKU: BLC-07438P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description	Recombinant Human Sarcolipin (SLN) Protein (His-KSI) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	O00631
Target Symbol	SLN
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-KSI
Target Protein Sequence	MGINTRELFLNFTIVLITVILMWLLVRSYQY
Expression Range	1-31aa
Protein Length	Full Length
Mol. Weight	19.1 kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Reversibly inhibits the activity of ATP2A1 and ATP2A2 in sarcoplasmic reticulum by decreasing the apparent affinity of the ATPase for Ca(2+). Modulates calcium re-uptake during muscle relaxation and plays an important role in calcium homeostasis in muscle. Required for muscle-based, non-shivering thermogenesis.
Subcellular Location	Sarcoplasmic reticulum membrane; Single-pass membrane protein. Endoplasmic reticulum membrane; Single-pass membrane protein.
Protein Families	Sarcolipin family
Database References	HGNC: 11089 OMIM: 602203 KEGG: hsa:6588 STRING: 9606.ENSP00000304707 UniGene: Hs.334629

Gene Functions References

Structure-Function Relationship of the SERCA Pump and Its Regulation by Phospholamban and Sarcolipin. PMID: 29594859
Self-assembling study of sarcolipin and its mutants in multiple molecular dynamic simulations has been reported. PMID: 28241400
These results suggest that sAnk1 interacts with SLN both directly and in complex with SERCA1 and reduces SLN's inhibitory effect on SERCA1 activity. PMID: 28487373
analysis of transmembrane dynamics of the Thr-5 phosphorylated sarcolipin pentameric channel PMID: 27378083
Phospholamban and sarcolipin are membrane proteins that differentially regulate SERCA function. (Review) PMID: 26743715
Molecular dynamics simulations help to clarify and to understand better the SLN pentamer channel that had a hydrophobic gate and could switch Na(+) and Cl(-) ion permeability by hydrated and vacuum states. PMID: 26522287
Although SLN and PLB binding to SERCA have different functional outcomes on the coupling efficiency of SERCA, both proteins decrease the apparent Ca(2+) affinity of the pump, suggesting that SLN and PLB inhibit SERCA by using a similar mechanism. PMID: 25983321
SLN and PLN are co-expressed in most fibers, which suggests that super-inhibition of SERCAs may be physiologically important in the regulation of intracellular Ca2+ in human skeletal muscle. PMID: 24358354
The C-terminal tail of SLN is a distinct, essential domain in the regulation of SERCA. PMID: 23362265
The selective downregulation of SLN and enhanced sarcoplasmic reticulum Ca(2+) uptake in human AF suggest that SLN downregulation could play an important role in abnormal intracellular Ca(2+) cycling in atrial pathology. PMID: 21640081
sarcolipin binds to phospholamban and inhibits polymerization PMID: 12032137
sarcolipin is likely to be an atrial chamber-specific regulator of Ca2+ cycling in heart PMID: 12645548
role in regulating sarco(endo)plasmic reticulum Ca2+-ATPase by binding to transmembrane helices alone or in association with phospholamban PMID: 12692302
Gene expression of SLN was studied in children with congenital heart defects. PMID: 17515962

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.