Detects human Siglec‑10 in direct ELISAs and Western blots. In direct ELISAs and Western blots, approximately 5% cross‑reactivity with recombinant human (rh) Siglec-5 is observed and less than 1% cross-reactivity with rhSiglec-2, rhSiglec-3, rhSiglec-7, rhSiglec-9, and recombinant mouse Siglec-F is observed.
Polyclonal Goat IgG
Mouse myeloma cell line NS0-derived recombinant human Siglec-10 Met17-Thr546 Accession # Q96LC7
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied as a 0.2 µm filtered solution in PBS.
<0.10 EU per 1 μg of the antibody by the LAL method.
Recombinant Human Siglec‑10 Fc Chimera (Catalog # 2130-SL)
2.5 µg/106 cells
Blockade of Receptor-ligand Interaction
In a functional ELISA, 1-4 µg/mL of this antibody will block 50% of the binding of 1.5 μg/mL of biotinylated 6’‑Sialyllactose-Polyacrylamide to immobilized Recombinant Human Siglec-10 Fc Chimera (Catalog # 2130-SL) coated at 5 µg/mL (100 µL/well). At 30 μg/mL, this antibody will block >90% of the binding.
Ready to be labeled using established conjugation methods. No BSA or other carrier proteins that could interfere with conjugation.
Please Note: Optimal dilutions should be determined by each laboratory for each application.
are available in the Technical Information section on our website.
Detection of Siglec‑10 in Human B Cells by Flow Cytometry.
Human whole blood CD19+ B cells were stained with Goat Anti-Human Siglec‑10 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF2130, filled histogram) or isotype control antibody (Catalog # AB‑108‑C, open histogram), followed by Phycoerythrin-conjugated Anti-Goat IgG Secondary Antibody (Catalog # F0107).
Preparation and Storage
Reconstitute at 0.2 mg/mL in sterile PBS.
Reconstitution Buffer Available
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
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.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Siglecs (sialic acid binding Ig-like lectins) are I-type lectins that belong to the immunoglobulin superfamily. They are characterized by an N‑terminal Ig-like V-type domain which mediates sialic acid binding, followed by a varying number of Ig-like C2-type domains. Siglecs 5‑11 constitute the CD33/Siglec-3 related group, and are differentially expressed in the hematopoietic system (1‑3). Siglec-G is the apparent ortholog of human Siglec-10 (4). The human Siglec-10 cDNA encodes a 697 amino acid (aa) precursor that includes a 16 aa signal sequence, a 534 aa extracellular domain (ECD), a 21 aa transmembrane segment, and a 126 aa cytoplasmic domain. The ECD contains one Ig-like V‑type domain and four Ig-like C2-type domains, while the cytoplasmic domain contains two immunoreceptor tyrosine-based inhibitory motifs (ITIM) (5‑8). Five splice variants of human Siglec-10 differ in their deletions within the ECD. A potentially secreted sixth variant contains the Ig-like V-type domain followed by a 45 aa substitution (5‑7, 9). Within the ECD, human Siglec-10 is most closely related to Siglec-5 (42% aa sequence identity). It shares 63% aa sequence identity with mouse Siglec-G. Siglec-10 is expressed on eosinophils, neutrophils, monocytes, and B cells (5, 8) with some splice variants predominating in particular cell types and tissue locations (6, 7, 9). It is up‑regulated on eosinophils in mouse models of allergic respiratory inflammation (10). Siglec-10 binds sialated proteins and lipids in alpha 2,3 or alpha 2,6 linkage and shows a preference for GT1b gangliosides (7, 11). This binding can be modulated by cis interactions of Siglec-10 with sialated molecules expressed on the same cell (7). When tyrosine phosphorylated, the cytoplasmic ITIMs interact with phosphatases SHP-1 and SHP-2 to propagate inhibitory signals (5, 9).
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