Recombinant Human Siglec-10 Fc Chimera Avi-tag Protein, CF Summary
Accession # Q96LC7.3
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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.
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 with Trehalose.|
|Reconstitution||Reconstitute at 250 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.
When Recombinant Human CD52 Fc Chimera Protein (9116-CD) is immobilized at 5 μg/mL (100 µL/well), the concentration of Biotinylated Recombinant Human Siglec‑10 Fc Chimera Avi-tag (Catalog # AVI2130) that produces 50% of the optimal binding response is found to be approximately 0.75-4.50 μg/mL.
2 μg/lane of Recombinant Siglec-10 Fc Chimera Avi-tag (Catalog # AVI2130) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 95-118 kDa and 190-236 kDa, respectively.
Sialic acid-binding Ig-like lectin 10 (Siglec-10), also known as Siglec-like protein 2, is an inhibitory I-type lectin of immune regulators belonging to the immunoglobulin superfamily. Siglecs can be divided into 2 classes: evolutionarily conserved Siglecs and CD33-related Siglecs (1). Siglec-10 falls within the CD33-related Siglecs class and has the closest sequence homology to Siglec-5 and Siglec-3 (2). The extracellular domain (ECD) of human Siglec-10 consists of one V-set domain that plays a role in specific sialoglycans recognition and four Ig-like C2-type domains, a single transmembrane domain and a cytoplasmic tail containing three immunoreceptor tyrosine-based inhibitory motifs (ITIMs) (3). Within the ECD, mature human Siglec-10 shares 63% amino acid sequence identity with mouse and rat Siglec-10. Siglec-10 is expressed on eosinophils, neutrophils, monocytes, and B cells (4, 6) with some splice variants predominating in particular cell types and tissue locations (5, 2, 7). It is upregulated on eosinophils in mouse models of allergic respiratory inflammation (8). Siglec-10 binds sialated proteins and lipids in alpha 2,3 or alpha 2,6 linkage and shows a preference for GT1b gangliosides (2, 9). This binding can be modulated by cis interactions of Siglec-10 with sialated molecules expressed on the same cell (2). When tyrosine phosphorylated, the cytoplasmic ITIMs interact with phosphatases SHP-1 and SHP-2 to propagate inhibitory signals (4, 7). Additionally, Siglec-10 has been shown to interact with soluble CD52 (10). This interaction inhibits the proliferation of activated T cells and the cytotoxic function of autoimmune CD8+ T cells in type 1 diabetes (11). Our Avi-tag Biotinylated Siglec-10 features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.
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- Forgione, R. et al. (2020) iScience. 23:101231.
- Whitney, G. et al. (2001) Eur. J. Biochem. 268:6083.
- Yousef, G.M. et al. (2001) Biochem. Biophys. Res. Commun. 284:900.
- Munday, J. et al. (2001) Biochem. J. 355:489.
- Kitzig, F. et al. (2002) Biochem. Biophys. Res. Commun. 296:355.
- Aizawa, H. et al. (2003) Genomics 82:521.
- Rapoport, E. et al. (2003) Bioorg. Med. Chem. Lett. 13:675.
- Toh, B.-H. et al. (2013) Cell. Mol. Immunol. 10:379.
- Bandala-Sanchez, E. et al. (2013) Nat. Immunol. 14:741.
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