Reactivity | HuSpecies Glossary |
Applications | Bioactivity |
Additional Information | Fc Chimera |
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Details of Functionality | Measured by flow cytometry for its ability to bind anti-Human Siglec-3/CD33 Monoclonal Antibody conjugated fluorescent beads. |
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Source | Mouse myeloma cell line, NS0-derived human Siglec-3/CD33 protein
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Accession # | |||||||
N-terminal Sequence | Asp18 |
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Structure / Form | Disulfide-linked homodimer, labeled with Atto 488 via amines Excitation Wavelength: 501 nm Emission Wavelenght: 523 nm |
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Protein/Peptide Type | Recombinant Proteins |
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Purity | >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
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Endotoxin Note | <1.0 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 53.4 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 | 67-80 kDa, under reducing conditions |
Storage | Protect from light. Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Supplied as a 0.2 μm filtered solution in PBS with BSA as a carrier protein. |
Purity | >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Siglecs (sialic acid binding Ig-like lectins) are I-type (Ig-type) lectins belonging to the Ig superfamily. They 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 (1, 2). Eleven human Siglecs have been cloned and characterized. They are sialoadhesin/CD169/Siglec-1, CD22/Siglec-2, CD33/Siglec-3, Myelin-Associated Glycoprotein (MAG/Siglec-4a) and Siglecs 5 to 11 (1 - 3). To date, no Siglec has been shown to recognized any cell surface ligand other than sialic acids, suggesting that interactions with glycans containing this carbohydrate are important in mediating the biological functions of Siglecs. Siglecs 5 to 11 share a high degree of sequence similarity with CD33/Siglec-3 both in their extracellular and intracellular regions. They are collectively referred to as CD33-related Siglecs. One remarkable feature of the CD33-related Siglecs is their differential expression pattern within the hematopoietic system (1, 2). This fact, together with the presence of two conserved immunoreceptor tyrosine-based inhibition motifs (ITIMs) in their cytoplasma tails, suggests that CD33-related Siglecs are involved in the regulation of cellular activation within the immune system. Human Siglec-3 is alternatively known as myeloid cell surface antigen CD33 and GP67. Human Siglec-3 cDNA encodes a 364 amino acid (aa) polypeptide with a hydrophobic signal peptide, an N-terminal Ig-like V-type domain, one Ig-like C2-type domains, a transmembrane region and a cytoplasmic tail (1, 4). Siglec-3 expression is restricted to cells of myelomonocytic lineage (2). It binds sialic acid preferring alpha 2,3- linkage over alpha 2,6- linkage (5). Studies indicated that Siglec-3 recruits SHP-1 and SHP-2 to its ITIMs (6, 7). When co-crosslinking with Fc gamma R1, Siglec-3 inhibits tyrosine phosphorylation and calcium mobilization, suggesting Siglec-3 can mediate inhibitory signals (7).
Harnessing Natural Killer Cell Activity for Anti-Tumor Immunotherapy By Victoria Osinski, PhDWhat’s “Natural” About Natural Killer (NK) Cells?For immunologists, the term cytotoxicity often conjures up images of an army of antigen specific CD8+ T cells deploying to ... Read full blog post. |
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