Human FCRLB/FCRY Antibody

FCRLB, also known as FCRL2, FCRY, and FREB2, is a 60 kDa protein with sequence homology to classical Fc receptors. There are at least six type 1 transmembrane FCRL proteins and two that lack transmembrane segments. Each family member contains between three and nine immunoglobulin-like domains. FCRL proteins are differentially expressed within the B cell lineage and can either promote or inhibit B cell proliferation and activation (1, 2). According to R&D Systems testing, FCRLB binds to purified human IgG with high affinity. Human FCRLB shares 82% and 85% amino acid sequence identity with mouse and rat FCRLB, respectively. It contains a putative signal peptide, three immunoglobulin-like domains, and a mucin-like stalk that is rich in Pro, Ser, and Thr residues (1‑3). The stalk region also contains di-Leu motifs and an unpaired cysteine (1‑3). Alternative splicing generates isoforms with deletions in the putative signal peptide and substitutions and/or truncations in the third Ig-like domain (3). When expressed in transfectants, FCRLB is not secreted but shows a diffuse intracellular localization (3, 4). FCRLB is expressed at a low level in placenta and in B lineage cells of the germinal center (3, 4). It is upregulated in B cells by BAFF and LPS (5). Among non-hematopoietic cells, FCRLB is expressed in fibroblasts, melanocytes, and melanoma (3, 5). It is preferentially expressed in nonproliferating cells and at the onset of apoptosis (4, 5).