Recombinant Human Sarcolipin (SLN), partial

Code	CSB-YP021780HU
MSDS	MSDS
Size	Pls inquire
Source	Yeast
Have Questions?	Leave a Message or Start an on-line Chat

Code	CSB-EP021780HU-B
MSDS	MSDS
Size	Pls inquire
Source	E.coli
Conjugate	Avi-tag Biotinylated E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
Have Questions?	Leave a Message or Start an on-line Chat

Code	CSB-BP021780HU
MSDS	MSDS
Size	Pls inquire
Source	Baculovirus
Have Questions?	Leave a Message or Start an on-line Chat

Code	CSB-MP021780HU
MSDS	MSDS
Size	Pls inquire
Source	Mammalian cell
Have Questions?	Leave a Message or Start an on-line Chat

Product Details
Related Products
Customer Reviews and Q&A
Target Background

Product Details

Purity

>85% (SDS-PAGE)

Target Names

SLN

Uniprot No.

O00631

Alternative Names

SLN; Sarcolipin

Species

Homo sapiens (Human)

Expression Region

1-7aa

Target Protein Sequence

MGINTRE

Protein Length

Partial

Tag Info

Tag type will be determined during the manufacturing process.

The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Form

Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer before Lyophilization

Tris/PBS-based buffer, 6% Trehalose, pH 8.0

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet

Please contact us to get it.

Customer Reviews and Q&A

■ Customer Reviews

There are currently no reviews for this product.

Submit a Review here

Target Background

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.

Gene References into Functions

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