Recombinant Human Siglec-11 Fc Chimera Protein, CF

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When Recombinant Human Siglec‑11 Fc Chimera (Catalog # 3258-SL) is immobilized at 2 µg/mL (100 µL/well), it binds Biotinylated Recombinant Human Siglec‑15 Fc Chimera Avi-tag protein with an ED50 of 0.7-4.2 μg/mL.

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Binding Activity
Format
Carrier-Free

Order Details

Recombinant Human Siglec-11 Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human Siglec‑11 Fc Chimera is immobilized at 2 µg/mL (100 µL/well), it binds Biotinylated Recombinant Human Siglec‑15 Fc Chimera Avi-tag protein with an ED50 of 0.7-4.2 μg/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived human Siglec-11 protein
Human Siglec-11
Asn17-His543
(Glu84Ala & Lys145Gln)
Accession # AAK72907
IEGRMD Human IgG1
(Pro100-Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
Asn17
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
SIGLEC11
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Binding Activity
Theoretical MW
84.4 kDa (monomer).
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
110-135 kDa, reducing conditions
Publications
Read Publications using
3258-SL in the following applications:

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
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Siglec-11 Fc Chimera Protein, CF

  • sialic acid binding Ig-like lectin 11
  • sialic acid-binding Ig-like lectin 11
  • Sialic acid-binding lectin 11
  • Siglec11
  • Siglec-11

Background

Siglecs (sialic acid binding Ig-like lectins) are I-type lectins that belong to the immunoglobulin superfamily. They are characterized by anN-terminal Ig-like V-set domain which mediates sialic acid binding, followed by a varying numbers of Ig-like C2-set domains. Siglecs-3 and 5 - 13 constitute the CD33/Siglec-3 related group, which are defined by their sequence homology and differential expression in the hematopoietic system (1-3). Mature human Siglec-11 consists of a 534 amino acid (aa) extracellular domain (ECD), a 23 aa transmembrane segment, and a 114 aa cytoplasmic domain. The ECD contains one Ig-like V-set domain, and three Ig-like C2-set domains. The cytoplasmic domain contains two immunoreceptor tyrosine-based inhibitory motifs (ITIMs) (4). A splice variant of Siglec-11 has a deletion of nearly 100 aa in the extracellular juxtamembrane region. Among siglecs, the ECD of Siglec-11 is most closely related to that of Siglec-10 (82% aa sequence identity). The cytoplasmic domains of these proteins are only 20% identical. Siglec-11 is closely related to the pseudogenes Siglec-14 and Siglec-16 (4, 5). Human Siglec-11 shares 90%-96% aa sequence identity with Siglec-11 from great apes. Rodent orthologs of Siglec-11 have not been identified. In human, Siglec-11 is expressed in tissue macrophages, brain microglia, and inflammatory site monocytes (4). Strong microglial expression is specific to humans, as it is less prominent or absent in chimpanzees and orangutans (5). Siglec-11 forms 180 kDa disulfide-linked dimers. It shows a strong binding preference for sialic acid in alpha 2-8 linkage which is unusual for siglecs (4). A conserved arginine in the Ig-like V-set domain only partially contributes to Siglec-11 ligand recognition, in contrast to its being required in other siglecs (4). Tyrosine phosphorylation of the cytoplasmic region of Siglec-11 promotes association with the phosphatases SHP-1 and SHP-2 (4).

  1. Varki, A. and T. Angata (2006) Glycobiology 16:1R.
  2. Crocker, P.R. (2005) Curr. Opin. Pharmacol. 5:431.
  3. Crocker, P.R. (2002) Curr. Opin. Struct. Biol. 12:609.
  4. Angata, T. et al. (2002) J. Biol. Chem. 277:24466.
  5. Hayakawa, T. et al. (2005) Science 309:1693.

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Bioinformatics

Gene Symbol SIGLEC11
Uniprot