TNFRSF17 Human, His
Description
TNFRSF17 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 130 amino acids (78-184 a.a) and having a molecular mass of 14.1kDa.
TNFRSF17 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Recombinant human TNFRSF17 protein has been produced in E. coli. It is a single, non-glycosylated polypeptide chain consisting of 130 amino acids (residues 78-184). The protein has a molecular mass of 14.1 kDa. For purification purposes, a 23 amino acid His-tag is fused to the N-terminus of TNFRSF17. The protein is purified using proprietary chromatographic techniques.
Product Science Overview
B-Cell Maturation Antigen (BCMA), also known as tumor necrosis factor receptor superfamily member 17 (TNFRSF17), is a protein encoded by the TNFRSF17 gene in humans . BCMA is a cell surface receptor that plays a crucial role in the regulation of B cell proliferation, survival, and maturation into plasma cells . The recombinant form of BCMA, tagged with a His-tag, is widely used in research and therapeutic applications.
The human recombinant BCMA with a His-tag is typically produced in various expression systems such as E. coli or baculovirus . The His-tag, a sequence of histidine residues, is added to the protein to facilitate purification using immobilized metal affinity chromatography (IMAC). This tag does not interfere with the protein’s function and allows for efficient isolation of the recombinant protein.
For example, TNFRSF17 Human Recombinant produced in E. coli is a single, non-glycosylated polypeptide chain containing 130 amino acids and a 23 amino acid His-tag at the N-terminus . Another variant produced in baculovirus is a glycosylated polypeptide chain containing 296 amino acids and a 242 amino acid hIgG-His-Tag at the C-terminus .
BCMA is primarily expressed on mature B lymphocytes and plasma cells . It is a receptor for B-cell activating factor (BAFF) and a proliferation-inducing ligand (APRIL), both of which are crucial for B cell development and immune response . The interaction of BCMA with these ligands leads to the activation of NF-kappaB and MAPK8/JNK pathways, promoting cell survival and proliferation .
The expression and function of BCMA are regulated by several mechanisms, including transcriptional and post-transcriptional regulation . The binding of BAFF and APRIL to BCMA triggers signaling pathways that regulate B cell survival and differentiation . Additionally, soluble BCMA (sBCMA), a cleaved form of the receptor, can be found in the serum and is often elevated in patients with multiple myeloma .
BCMA has emerged as a promising therapeutic target, particularly in the treatment of multiple myeloma . Anti-BCMA therapies, including monoclonal antibodies, antibody-drug conjugates, and chimeric antigen receptor (CAR) T-cell therapies, have shown significant efficacy in clinical trials . These therapies target BCMA-expressing cells, leading to their destruction and providing a potential treatment for refractory or relapsed multiple myeloma .
