R&D Systems代理5806-SL-050 Recombinant Mouse Siglec-E Fc Chimera Protein, CF (50 UG)

2025-06-25

货号:5806-SL-050

品牌:R&D Systems

规格:50ug

目录价:¥4490.00

市场价格:¥3592.00

会员价格:¥3592.00

  • 到货时间:3~4周

    金山科研平台,产品价格货期咨询微信:jinshanbio Source:Mouse myeloma cell line, NS0-derived Accession #:AAH23280 N-terminal Sequence Analysis:No results obtained, N-sequencing might be blocked: Gln20 predicted Structure:Disulfide-linked homodimer Purity:>95%, by SDS-PAGE under reducing conditions and visualized by silver stain. Predicted Molecular Mass:64.6 kDa (monomer) SDS-PAGE:75-95 kDa, reducing conditions Activity:Measured by its binding ability in a functional ELISA.

    When 0.5 µg/mL of Recombinant Mouse Siglec‑E Fc Chimera is immobilized onto a goat anti-mouse IgG Fc antibody coated plate, the concentration of biotinylated Neu5Ac alpha 2-6GalNAc alpha -Polyacrylamide that produces 50% of the optimal binding response is found to be approximately 20 - 80 ng/mL.

    Formulation:Lyophilized from a 0.2 µm filtered solution in PBS.See Certificate of Analysis for details. Molecule Information: Siglec-E Long Name: Sialic Acid Binding Ig-like Lectin E Entrez Gene IDs: 83382 (Mouse) Background: Siglecs Siglecs are I-type (Ig-type) lectins belonging to the Ig superfamily. They are characterized by an N-terminal, Ig-like V-type domain that mediates sialic acid binding, followed by varying numbers of Ig-like C2-type domains (2 to 17), a single transmembrane region, and a cytoplasmic tail. The siglecs can be broadly classified into two subgroups: Siglecs-1, -2, and -4, and a Siglec-3/CD33-related subgroup (Siglecs-3, and -5 through -13 in primates) defined by sequence similarity and clustered gene localization. They are widely expressed on hematopoietic cells, often in a cell-type-specific manner, and Siglec-4/MAG is a myelin component in Schwann cells and oligodendrocytes. Their ligands, sialic acids, are negatively charged monosaccharides found on cell-surface glycoproteins and glycolipids. Although Siglec functions continue to be defined, most have intracellular immunoreceptor tyrosine-based inhibitory motifs (ITIM), implicating them in the suppression of immunoreceptor signaling. They may also participate in cell/cell interactions or act as receptors for the entry of viral or bacterial pathogens.

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