Recombinant Mouse Thioredoxin Reductase-Like Selenoprotein T (SELENOT) Protein (His)

Name: Recombinant Mouse Thioredoxin Reductase-Like Selenoprotein T (SELENOT) Protein (His)
Brand: Beta LifeScience
SKU: BLC-09931P
Availability: InStock

Greater than 90% 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 Mouse Thioredoxin Reductase-Like Selenoprotein T (SELENOT) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P62342
Target Symbol	SELENOT
Synonyms	Selenot; Selt; Thioredoxin reductase-like selenoprotein T; SelT; EC 1.8.1.9
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	SANLGGVPSKRLKMQYATGPLLKFQICVSSGYRRVFEEYMRVISQRYPDIRIEGENYLPQPIYRHIASFLSVFKLVLIGLIIVGKDPFAFFGMQAPSIWQWGQENKVYACMMVFFLSNMIENQCMSTGAFEITLNDVPVWSKLESGHLPSMQQLVQILDNEMKLNVHMDSIPHHRS
Expression Range	20-195aa
Protein Length	Full Length of Mature Protein
Mol. Weight	24.2kDa
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	Selenoprotein with thioredoxin reductase-like oxidoreductase activity. Protects dopaminergic neurons against oxidative stress ans cell death. Involved in ADCYAP1/PACAP-induced calcium mobilization and neuroendocrine secretion. Plays a role in fibroblast anchorage and redox regulation. In gastric smooth muscle, modulates the contraction processes through the regulation of calcium release and MYLK activation. In pancreatic islets, involved in the control of glucose homeostasis, contributes to prolonged ADCYAP1/PACAP-induced insulin secretion.
Subcellular Location	Endoplasmic reticulum membrane; Single-pass membrane protein.
Protein Families	SelWTH family, Selenoprotein T subfamily
Database References	KEGG: mmu:69227 STRING: 10090.ENSMUSP00000103557 UniGene: Mm.270950
Tissue Specificity	Ubiquitous. Highly expressed in the endocrine pancreas. Expressed at low levels in the adult brain.

Gene Functions References

Selenoprotein T is a novel oligosaccharyltransferase subunit that regulates unfolded protein response signaling and ASTH secretion. PMID: 28928140
SelT exerts a neuroprotective role which is essential during brain development, and that its loss impairs mice behavior. PMID: 26497036
The SelT play a crucial role in the protection of dopaminergic neurons against oxidative stress and cell death, providing insight into the molecular underpinnings of this stress in PD. PMID: 26866473
Data suggest SelT is expressed in pancreatic beta- and delta-cells; inactivation of SelT in beta-cells leads to glucose intolerance via impaired glucose homeostasis and PACAP (pituitary adenylate cyclase-activating polypeptide) insulinotropic effect. PMID: 23913443
Data show that the loss of SelT elevates expression of another selenoprotein, selenoprotein W, suggesting that SepW1 may functionally compensate for SelT. PMID: 19935881

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.