Recombinant Human DcR2 Protein (His Tag)

Name: Recombinant Human DcR2 Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-1554
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	His
Host Species	Human
Accession	NP_003831.2
Synonym	CD264, DCR2, TRAIL-R4, TRAILR4, TRUNDD
Background	Tumor necrosis factor receptor superfamily member 1D (TNFRSF1D), also known as TNF-related apoptosis-inducing ligand receptor 4 (TRAIL R4), CD264, and Decoy receptor 2, is a member of the TNF-receptor superfamily. This receptor contains an extracellular TRAIL-binding domain, a transmembrane domain, and a truncated cytoplamic death domain. This receptor does not induce apoptosis, and has been shown to play an inhibitory role in TRAIL-induced cell apoptosis. TRAIL R4/CD264/TNFRSF1D is widely expressed, in particular in fetal kidney, lung and liver, and in adult testis and liver. TRAIL R4/CD264/TNFRSF1D is also expressed in peripheral blood leukocytes, colon and small intestine, ovary, prostate, thymus, spleen, pancreas, kidney, lung, placenta and heart. The signaling capacity of TRAIL R4 is similar to that of TRAIL R1 and TRAIL R2 with respect to NF-κB activation, but differs in its inability to induce apoptosis. TRAIL R4 retains a C-terminal element containing one third of a consensus death domain motif. Transient overexpression of TRAIL R4 in cells normally sensitive to TRAIL-mediated killing confers complete protection, suggesting that one function of TRAIL R4 may be inhibition of TRAIL cytotoxicity.
Description	A DNA sequence encoding the human TNFRSF10D (NP_003831.2) extracellular domain (Met 1-His 211) was fused with a His tag at the C-terminus.
Source	HEK293
Predicted N Terminal	Ala 56
AA Sequence	Met 1-His 211
Molecular Weight	The recombinant human TNFRSF10D consists of 167 a.a. after removal of the signal peptide and has a predicted a molecular mass of 18.4 kDa. As a result of glycosylation, the apparent molecular mass of rhTNFRSF10D is approximately 30-40 kDa in SDS-PAGE under reducing conditions.
Purity	>90% as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	1. Measured by its binding ability in a functional ELISA. Immobilized human TNFRSF10D at 10 ug/ml (100 ul/well) can bind biotinylated TNFSF10 with a linear range of 0.625-40 ng/ml.2. Measured by its ability to inhibit TRAIL-mediated cytotoxicity using L-929 mouse fibroblast cells treated with TRAIL. The ED50 for this effect is typically 0.05-0.5 ug/mL in the presence of 20 ng/ml Recombinant Human TRAIL/TNFSF10.
Formulation	Lyophilized from sterile PBS, pH 7.4.
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.