Recombinant Mouse FCRL5/FcRH3 Protein, CF Summary
Details of Functionality |
Measured by its ability to bind mouse IgG with an estimated KD <400 nM. |
Source |
Mouse myeloma cell line, NS0-derived mouse FCRL5/FcRH5 protein Met1-Ala496 with a C-terminal 6-His tag |
Accession # |
|
N-terminal Sequence |
No results obtained: Gln27 predicted |
Protein/Peptide Type |
Recombinant Proteins |
Gene |
Fcrl5 |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<0.01 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
53.5 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
SDS-PAGE |
65-80 kDa, reducing conditions |
Packaging, Storage & Formulations
Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 100 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse FCRL5/FcRH3 Protein, CF
Background
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).
- Davis, R.S. (2007) Annu. Rev. Immunol. 25:525.
- Maltais, L.J. et al. (2006) Nat. Immunol. 7:431.
- Won, W-J. et al. (2006) J. Immunol. 177:6815.
- Davis, R.S. et al. (2004) Int. Immunol. 16:1343.
- Hatzivassiliou, G. et al. (2001) Immunity 14:277.
- Miller, I. et al. (2002) Blood 99:2662.
- Polson, A.G. et al. (2006) Int. Immunol. 18:1363.
- Vidal-Laliena, M. et al. (2005) Cell. Immunol. 236:6.
- Haga, C.L. et al. (2007) Proc. Natl. Acad. Sci. 104:9770.
- Mohan, J. et al. (2006) Blood 107:4433.
- Campbell, J.A. et al. (2010) J. Immunol. 185:28.
- Ise, T. et al. (2005) Clin. Cancer Res. 11:87.
- Ise, T. et al. (2007) Leukemia 21:169.
- Kazemi, T. et al. (2009) Cancer Immunol. Immunother. 58:989.
- Ise, T. et al. (2006) Clin. Chem. Lab. Med. 44:594.
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