Recombinant Mouse TRAIL Protein (aa 118-291, His Tag)

Beta LifeScience SKU/CAT #: BLPSN-4622

Recombinant Mouse TRAIL Protein (aa 118-291, His Tag)

Beta LifeScience SKU/CAT #: BLPSN-4622
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Product Overview

Tag His
Host Species Mouse
Accession P50592
Synonym A330042I21Rik, AI448571, APO-2L, Ly81, TL2, Trail
Background Tumor necrosis factor ligand superfamily member 1 (TNFSF1), also known as TNF-related apoptosis-inducing ligand (TRAIL), Apo-2 ligand, and CD253, is a cytokine that belongs to the tumor necrosis factor (TNF) ligand family. TNFSF1 / Apo-2L / CD253 functions as a ligand that induces the process of cell death called apoptosis. TNFSF1 / TRAIL shows homology to other members of the tumor necrosis factor superfamily. As one member of the cluster of differentiation system, TNFSF1 / CD253 is commonly used as cell markers in immunophynotyping. Different kinds of cells in the immune system can be identified through the surface CD molecules which associating with the immune function of the cell. There are more than 32 CD unique clusters and subclusters have been identified. Some of the CD molecules serve as receptors or ligands important to the cell through initiating a signal cascade which then alter the behavior of the cell. Some CD proteins do not take part in cell signal process but have other functions such as cell adhesion TNFSF1 / Apo-2L / CD253 / TRAIL binds to several members of TNF receptor superfamily including TNFRSF1A / TRAILR1, TNFRSF1B / TRAILR2, TNFRSF1C / TRAILR3, TNFRSF1D / TRAILR4, and possibly also to TNFRSF11B/OPG. The activity of TNFSF1 / TRAIL may be modulated by binding to the decoy receptors TNFRSF1C / TRAILR3, TNFRSF1D/TRAILR4, and TNFRSF11B/OPG that cannot induce apoptosis. The binding of this protein to its receptors has been shown to trigger the activation of MAPK8 / JNK, caspase 8, and caspase 3. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.Immune CheckpointImmunotherapyCancer ImmunotherapyTargeted Therapy
Description A DNA sequence encoding the mouse TNFSF10 (P50592) (Pro 118-Asn 291) was expressed, with a His tag at the N-terminus.
Source E.coli
Predicted N Terminal Met
AA Sequence Pro 118-Asn 291
Molecular Weight The recombinant mouse TNFSF10 consisting of 190 a.a. and has a calculated molecular mass of 22.2 kDa. rm TNFSF10 migrates as an approximately 22 KDa band in SDS-PAGE under reducing conditions.
Purity >95% as determined by SDS-PAGE
Endotoxin Please contact us for more information.
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile PBS, pH 7.5.
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

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.

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