Recombinant Mouse FCRL5/FcRH3 Protein, CF Summary
Measured by its ability to bind mouse IgG with an estimated KD <400 nM.
Met1-Ala496 with a C-terminal 6-His tag
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CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 100 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
Fc Receptor-Like 5 (FCRL5), also known as FcRH3 (FcRH5 in human), IRTA2, and CD307e, is a 90 ‑ 95 kDa member of the FCRL family of proteins whose amino acid (aa) sequence is reminiscent of that for classical Fc receptors. FCLR molecules are type 1 transmembrane proteins that contain from three to nine immunoglobulin-like domains. They are differentially expressed within the B cell lineage, and can either promote or inhibit B cell proliferation and activation (1, 2, 3). Mature mouse FCRL5 consists of a 470 aa extracellular domain (ECD), a 21 aa transmembrane segment, and a 79 aa cytoplasmic region. The ECD contains five Ig-like domains, while the cytoplasmic region possesses one ITAM-like motif and one immunotyrosine inhibitory motif (ITIM) (1, 3, 4). There are two major alleles for FCLR5 in mouse. The first was just described, and is found in BALB/c plus NZB mouse strains. The second is found in C57BL/6 mice, and differs by eleven scattered aa in the ECD. This creates one additional N-linked glycosylation site, and increases the SDS‑PAGE MW by 5 kDa (3). Alternate splicing of mouse FCRL5 generates at least one additional isoform that lacks the first Ig-like domain (aa 3 ‑ 90 of the mature molecule) (4). Human FCRL5, by contrast, contains up to nine Ig-like domains in a highly variable ECD, and over common regions, mouse and human FCRL5 share 49% aa sequence identity. CRL5 expression is restricted to mature B lineage cells in lymphoid tissues and blood, and is particularly noted to be expressed on T‑independent marginal zone and B1 B cells (3 - 8). Its ligation inhibits signaling through the B cell antigen receptor (9). Epstein-Barr virus transformation of B cells induces the up‑regulation of surface FCRL5 by a direct effect of its EBNA2 protein on FCRL5 gene transcription (10). FCRL5 on B cells functions as a receptor for the orthopoxvirus MHC class I-like protein OMCP (11). And based on the literature and R&D Systems testing, both mouse and human FCRL5 will bind to purified IgG with high affinity (5). In human, the FCRL5 gene maps to the 1q21 chromosomal locus, a common site of rearrangements in B cell malignancies. Notably, the FCRL5 protein is preferentially expressed in cell lines with 1q21 abnormalities, and is up‑regulated on tumor cells in some types of B cell malignancies (5, 7, 12 ‑ 14). In addition, soluble FCRL5 is elevated in the serum of many B cell leukemia patients (13, 15).
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