Recombinant Human BCMA/TNFRSF17 Trimer Protein, Active

Beta LifeScience SKU/CAT #: BLK-02666P-100UG
Human BCMA Trimer on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.
Human BCMA Trimer on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Recombinant Human BCMA/TNFRSF17 Trimer Protein, Active

Beta LifeScience SKU/CAT #: BLK-02666P-100UG
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.

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Product Overview

Description Recombinant Human BCMA/TNFRSF17 Trimer Protein is expressed from HEK293 with His tag and Avi tag at the C-Terminus.It contains Met1-Ala54.
Purity > 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC
Accession Q02223
Target Symbol BCMA/TNFRSF17 Trimer
Synonyms CD269; TNFRSF17; BCMA; BCM; TNFRSF13A
Species Human
Expression System HEK293
Tag C-His-Avi
Expression Range Met1-Ala54
Mol. Weight The protein has a predicted MW of 29.5 kDa. Due to glycosylation, the protein migrates to 30-48 kDa based on Tris-Bis PAGE result.
Form Lyophilized
Formulation Lyophilized from 0.22um filtered solution in PBS (pH 7.4). Normally 8% trehalose is added as protectant before lyophilization.
Endotoxin Less than 1EU per ug by the LAL method.
Activity Immobilized Human BCMA Trimer at 0.5ug/ml (100ul/Well) on the plate. Dose response curve for Human BAFF, hFc Tag with the EC50 of 6.6ng/ml determined by ELISA (QC Test). Contact us for detailed testing images.
Storage Reconstituted protein stable at -80°C for 12 months, 4°C for 1 week. Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
Shipping Shipped at ambient temperature.
Gene Background B-cell maturation antigen (BCMA or BCM), also known as tumor necrosis factor receptor superfamily member 17 (TNFRSF17), is a protein that in humans is encoded by the TNFRSF17 gene.TNFRSF17 is a cell surface receptor of the TNF receptor superfamily which recognizes B-cell activating factor (BAFF).


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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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