R&D Systems代理5197-SL-050 Recombinant Human Siglec-1 Protein, CF (50 UG)

2025-06-27

货号:5197-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, Ser20-Gln1641, with a C-terminal 6-His tag Accession #:Q9BZZ2 N-terminal Sequence Analysis:Ser20 Purity:>80%, by SDS-PAGE under reducing conditions and visualized by silver stain. Predicted Molecular Mass:173.9 kDa SDS-PAGE:175 kDa- 190 kDa, reducing conditions Activity:Measured by the ability of the immobilized protein to support the adhesion of human red blood cells. Kelm, S. et al. (1994) Current Biology 4:965.The ED50 for this effect is typically 0.6-3µg/mL. Formulation:Lyophilized from a 0.2 µm filtered solution in PBS.See Certificate of Analysis for details. Molecule Information: Siglec-1/CD169 Long Name: Sialic Acid Binding Ig-like Lectin 1 Aliases: CD169 Entrez Gene IDs: 6614 (Human); 20612 (Mouse); 311426 (Rat) 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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