Recombinant Cynomolgus/Rhesus Siglec-3/CD33 Fc Protein, CF
Recombinant Cynomolgus/Rhesus Siglec-3/CD33 Fc Protein, CF Summary
Product Specifications
| Cynomolgus Monkey/Rhesus Macaque Siglec-3/CD33 (Met16-Gly248) Accession # XP_045235686.1 | IEGRMD | Human IgG1 (Pro100-Lys330) |
| N-terminus | C-terminus | |
Analysis
Product Datasheets
Carrier Free
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.
10885-SL
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
| Reconstitution | Reconstitute at 500 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.
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Scientific Data
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When Recombinant Cynomolgus Monkey/Rhesus Macaque Siglec-3/CD33 Fc Chimera (Catalog # 10885-SL) is immobilized at 1 µg/mL (100 µL/well), Recombinant Human Galectin-3BP/MAC-2BP (2226-GAB) binds with an ED50 of 0.15-1.20 µg/mL.
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2 μg/lane of Recombinant Cynomolgus Monkey/Rhesus Macaque Siglec‑3/CD33 Fc Chimera Protein (Catalog # 10885-SL) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 68-79 kDa and 140-160 kDa, respectively.
Reconstitution Calculator
Background: Siglec-3/CD33
Sialic acid-binding Ig-like lectin 3 (Siglec-3), also known myeloid cell surface antigen CD33 (CD33), is a I-type (Ig-type) lectin belonging to the sialoadhesin subclass of the immunoglobulin superfamily (1). Siglecs are characterized by an N-terminal Ig-like V-type domain, which mediates sialic acid binding, followed by varying numbers of Ig-like C2-type domains in the extracellular domain (ECD). Fourteen human and nine mouse Siglecs have been characterized and are divided into 2 families: CD33 related and evolutionarily conserved (1-3). Mature Siglec-3 consists of an ECD with one Ig-like V-type domain and one Ig-like C2 domain, a single transmembrane and a cytoplasmic tail containing two immunoreceptor tyrosine-based inhibitory motifs (ITIMs) (3). Within the ECD, cynomolgus/rhesus Siglec-3 shares 89% amino acid sequence identity with human Siglec-3. An isoform of Siglec-3 lacking the N-terminal V-type domain, generated by alternative splicing, has been identified in humans (4). Each Siglec family member has a distinct preference for binding the various types of sialylated glycans found on the surface of mammalian cells and they most likely evolved to regulate host immune responses via the recognition of self-glycans (6). Siglec-3 is a disulfide-linked homodimer expressed on neutrophils, monocytes, macrophages and dendritic cells (2). Siglec-3 may be implicated in the regulation of both the innate but also the adaptive immunity and human Siglec-3 continues to be a therapeutic target for the treatment of acute myeloid leukemia and is a high potential risk factor for Alzheimer's (5). Siglec-3's ligands have yet to be classified, however terminal epitope preferences are conserved between Siglec-3 and Siglec-9 when binding to glycans (7). R&D Systems in-house testing indicates that Siglec-3 binds to LGALS3BP, consistent with the demonstrated functional interactions between other members of these protein families (8).
- Bhattacherjee, A. et al. (2021) Mol. Neurodegener. 16:19.
- Murch, S. et al. (2020) Medical Hypotheses. 144:110168.
- Hernandez-Caselles, T. et al. (2019) J. Immunol. Res. 2019:6032141.
- Hernández-Caselles, T. et al. (2006) J Leukoc Biol. 79:46
- Malik, et al. (2013) J. Neurosci. 33:13320
- Paulson, J. et al. (2012) Ann. N. Y. Acad. Sci. 1253:37.
- Wang, S. et al. (2021) Front Mol. Biosci. 8:645999.
- Laubli, H. et al. (2014) J. Biol. Chem. 289:33481.
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