cd 307

FcRH5 is a cell surface marker enriched on malignant plasma cells when compared to other hematologic malignancies and normal tissues. DFRF4539A is an anti-FcRH5 antibody-drug conjugated to monomethyl auristatin E (MMAE), a potent anti-mitotic agent. FcRH5 FcRL5 Protein (Primary Amine Labeling), Human, Recombinant (His), Biotinylated is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 92.38 kDa and the accession number is AAK93971.

FcRH5 is a cell surface marker enriched on malignant plasma cells when compared to other hematologic malignancies and normal tissues. DFRF4539A is an anti-FcRH5 antibody-drug conjugated to monomethyl auristatin E (MMAE), a potent anti-mitotic agent. FcRH5 FcRL5 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 92.38 kDa and the accession number is AAK93971.

Expression system: HEK293 Cells
Length: 27-496, Extracellular Domain
Activity: Not Tested

Expression system: HEK293 Cells
Length: 16-851, Extracellular Domain
Activity: ELISA

P-selectin glycoprotein ligand 1 is the high affinitycounter-receptor for P-selectin on expressed on activated endothelial cells and platelets. As such, it plays a critical role in the tethering of these cells to activated platelets or endothelia expressing P-selectin. As cell adhesion molecules, multiple studies have shown that PSGL-1 P-selectin interaction is required for the normal recruitment of leukocytes during inflammatory reactions, and also participates in hemostatic responses. PSGL-1 can also bind to other two members of the selectin family, E-selectin (endothelial) and L-selectin (leukocyte), but binds best to P-selectin.

Expression system: E. coli
Length: 18-573, Partial
Activity: Not Tested

Expression system: HEK293 Cells
Length: 1-303, Partial
Activity: Not Tested

Expression system: HEK293 Cells
Length: 1-395, Partial
Activity: Not Tested

Mouse Fc receptor-like protein 1 (FCRL1) is a single-pass type I membrane protein. It is expressed in B-cells at the various stages of differentiation. Mouse FCRL1 consists of a 203 amino acid (aa) extracellular domain (ECD) with two Ig‑like domains, a 21 aa transmembrane segment, and a 103 aa cytoplasmic domain with two immunotyrosine activation motifs (ITAMs). FCRL1 is likely not a receptor for immunoglobulin. It may function as an activating coreceptor in B-cells and B-cells differentiation.