Recombinant Human DcR3 Protein (Fc Tag)

Beta LifeScience SKU/CAT #: BLPSN-1557

Recombinant Human DcR3 Protein (Fc Tag)

Beta LifeScience SKU/CAT #: BLPSN-1557
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Product Overview

Tag Fc
Host Species Human
Accession O95407
Synonym DCR3, DJ583P15.1.1, M68, M68E, TNFRSF6B, TR6
Background Tumor necrosis factor receptor superfamily member 6B (TNFRSF6B) also known as DcR3(Decoy Receptor 3) and M68 is the tumor necrosis factor receptor superfamily. DcR3/TNFRSF6B belongs to the tumor necrosis factor receptor superfamily. The encoded protein is postulated to play a regulatory role in suppressing FasL- and LIGHT-mediated cell death. It acts as a decoy receptor that competes with death receptors for ligand binding. Over-expression of this gene has been noted in gastrointestinal tract tumors. Read-through transcription into this gene from the neighboring upstream gene, which encodes regulator of telomere elongation helicase 1 (RTEL1), generates a non-coding transcript. DcR3/TNFRSF6B is detected in fetal lung, brain and liver. DcR3/TNFRSF6B is also detected in adult stomach, spinal cord, lymph node, trachea, spleen, colon and lung. This protein is highly expressed in several primary tumors from colon, stomach, rectum, esophagus and in SW48 colon carcinoma cells.
Description A DNA sequence encoding the human DCR3 (O95407)(Met1-His300) was expressed with the Fc region of human IgG1 at the C-terminus.
Source Baculovirus-Insect Cells
Predicted N Terminal Val 30
AA Sequence Met1-His300
Molecular Weight The recombinant human DCR3/Fc is a disulfide-linked homodimer. The reduced monomer comprises 508 a.a. and has a predicted molecular mass of 56.4 kDa. The apparent molecular mass of the protein is approximately 65 kDa in SDS-PAGE under reducing conditions.
Purity >85% as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity Measured by its ability to inhibit Fas Ligand induced apoptosis of Jurkat human acute T cell leukemia cells.The ED50 for this effect is typically 0.01-0.05 ug/mL in the presence of 20 ng/mL recombinant human Fas Ligand.
Formulation Lyophilized from sterile 100mM Glycine, 10mM NaCl, pH 7.0..
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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