Recombinant Mouse Siglec-E Fc Chimera Protein, CF

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Recombinant Mouse Siglec-E Fc Chimera Protein Binding Activity
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Product Details
Citations (3)
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Recombinant Mouse Siglec-E Fc Chimera Protein, CF Summary

Product Specifications

>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Measured by its binding ability in a functional ELISA. When Recombinant Mouse Siglec‑E Fc Chimera is immobilized at 2 μg/mL (100 μL/well), it binds to Recombinant Mouse Galectin-3 (HEK293-expressed) Protein (Catalog # 9039-GAB) with an ED50 of 0.08-0.8 μg/mL.
Mouse myeloma cell line, NS0-derived mouse Siglec-E protein
Mouse Siglec-E
Accession # AAH23280
N-terminus C-terminus
Accession #
N-terminal Sequence
No results obtained, N-sequencing might be blocked: Gln20 predicted
Structure / Form
Disulfide-linked homodimer
Predicted Molecular Mass
64.6 kDa (monomer)
75-95 kDa, reducing conditions

Product Datasheets

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Carrier Free

What does CF mean?

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.

What formulation is right for me?

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.
  • 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.

Scientific Data

Binding Activity Recombinant Mouse Siglec-E Fc Chimera Protein Binding Activity View Larger

When Recombinant Mouse Siglec-E Fc Chimera (Catalog # 5806-SL) is immobilized at 2 µg/mL (100 µL/well), Recombinant Mouse Galectin-3 (HEK293-expressed) Protein (Catalog # 9039-GAB) binds with an ED50 of 80-800 ng/mL.

Reconstitution Calculator

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Background: Siglec-E

Siglecs are sialic acid specific I‑type lectins that are characterized by an extracellular domain (ECD) with an N‑terminal Ig‑like V‑set domain followed by varying numbers of Ig‑like C2‑set domains (1, 2). Mouse Siglec‑E, also known as Myeloid Inhibitory Siglec (MIS), is an 80 ‑ 85 kDa member of the CD33‑related subfamily of Siglecs. It consists of a 335 amino acid (aa) ECD with one Ig‑like V‑set domain and two Ig‑like C2‑set domains, a 21 aa transmembrane segment, and a 93 aa cytoplasmic domain that contains two immunoreceptor tyrosine‑based inhibitory motifs (ITIM) (3, 4). Rodent and primate Siglec gene families have significantly diverged, and Siglec‑9 is the most likely human ortholog of mouse Siglec‑E (1). Within the ECD, mouse Siglec‑E shares 56% and 80% aa sequence identity with human Siglec‑9 and rat Siglec‑E, respectively. Siglec‑E is expressed as a heavily N‑glycosylated disulfide‑linked homodimer and shows binding preference for disialic acids in the alpha 2‑8 linkage (3, 5). It is expressed on the surface of several hematopoietic cell types including neutrophils, NK cells, monocytes, peritoneal macrophages and B1 cells, and splenic myeloid dendritic cells and marginal zone B cells (5). Tyrosine phosphorylation of the cytoplasmic ITIMs mediates the association of Siglec‑E with the phosphatases SHP‑1 and SHP‑2 (3, 4). Siglec‑E is up‑regulated and additionally phosphorylated following cellular stimulation by a variety of TLR agonists (6). Siglec‑E signaling negatively regulates the LPS‑induced production of TNF‑ alpha and IL‑6 by macrophages (4, 6). Its up‑regulation in macrophages parallels the development of endotoxin tolerance (6). Siglec‑E recognition of sialylated determinants on virulent T. cruzi contributes to the suppression of dendritic cell IL‑12 p40 production (7).

  1. Varki, A. and T. Angata (2006) Glycobiology 16:1R.
  2. Crocker, P.R. et al. (2007) Nat. Rev. Immunol. 7:255.
  3. Yu, Z. et al. (2001) Biochem. J. 353:483.
  4. Ulyanova, T. et al. (2001) J. Biol. Chem. 276:14451.
  5. Zhang, J.Q. et al. (2004) Eur. J. Immunol. 34:1175.
  6. Boyd, C.R. et al. (2009) J. Immunol. 183:7703.
  7. Erdmann, H. et al. (2009) Cell. Microbiol. 11:1600.
Long Name
Sialic Acid Binding Ig-like Lectin E
Entrez Gene IDs
83382 (Mouse)
Alternate Names
CD170;CD33L2;OBBP2;OB-BP2;Sialic acid-binding Ig-like lectin 5;SIGLEC5;SIGLEC-5; SiglecE; Siglec-E

Citations for Recombinant Mouse Siglec-E Fc Chimera Protein, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

3 Citations: Showing 1 - 3
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  1. CD22 blockade restores homeostatic microglial phagocytosis in ageing brains
    Authors: JV Pluvinage, MS Haney, BAH Smith, J Sun, T Iram, L Bonanno, L Li, DP Lee, DW Morgens, AC Yang, SR Shuken, D Gate, M Scott, P Khatri, J Luo, CR Bertozzi, MC Bassik, T Wyss-Coray
    Nature, 2019;0(0):.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Flow Cytometry
  2. Histone Deacetylase 3 Is Required for T Cell Maturation.
    Authors: Hsu F, Belmonte P, Constans M, Chen M, McWilliams D, Hiebert S, Shapiro V
    J Immunol, 2015;195(4):1578-90.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Flow Cytometry
  3. Broad and direct interaction between TLR and Siglec families of pattern recognition receptors and its regulation by Neu1.
    Authors: Chen, Guo-Yun, Brown, Nicholas, Wu, Wei, Khedri, Zahra, Yu, Hai, Chen, Xi, van de Vlekkert, Diantha, D'Azzo, Alessand, Zheng, Pan, Liu, Yang
    Elife, 2014;3(0):e04066.


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