Human Siglec-2/CD22 Antibody Summary
Accession # CAA42006
This antibody functions as an ELISA detection antibody when paired with Mouse Anti-Human Siglec‑2/CD22 Monoclonal Antibody (Catalog # MAB19684).
This product is intended for assay development on various assay platforms requiring antibody pairs. We recommend the Human Siglec-2/CD22 DuoSet ELISA Kit (Catalog # DY1968-05) for convenient development of a sandwich ELISA.
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Human Siglec‑2/CD22 ELISA Standard Curve. Recombinant Human Siglec‑2/CD22 protein was serially diluted 2-fold and captured by Mouse Anti-Human Siglec‑2/CD22 Monoclonal Antibody ( Catalog # MAB19684) coated on a Clear Polystyrene Microplate (Catalog # DY990). Mouse Anti-Human Siglec‑2/CD22 Monoclonal Antibody (Catalog # MAB19683) was biotinylated and incubated with the protein captured on the plate. Detection of the standard curve was achieved by incubating Streptavidin-HRP (Catalog # DY998) followed by Substrate Solution (Catalog # DY999) and stopping the enzymatic reaction with Stop Solution (Catalog # DY994).
Preparation and Storage
- 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 (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 the identified Siglecs 5 to 11 (1-3). To date, no Siglec has been shown to recognize any cell surface ligand other than sialic acid, suggesting that interactions with glycans containing this carbohydrate are important in mediating the biological functions of Siglecs. Human Siglec-2, also known as B-cell antigen CD22 or B lymphocyte cell adhesion molecule (BL-CAM), is a B cell restricted glycoprotein that is expressed in the cytoplasm of progenitor B and pre-B cells and on the surface of mature B cells. Two distinct human Siglec-2/CD22 cDNAs that arise from differential RNA processing of the same gene have been isolated. The predominant Siglec-2/CD22 beta encodes an 847 amino acid (aa) polypeptide with a hydrophobic signal peptide, an N-terminal Ig-like V-type domain, six Ig-like C2-type domains, a transmembrane region and a cytoplasmic tail with 4 immunoreceptor tyrosine-based inhibition motifs (ITIMs) (4). The variant Siglec-2/CD22 alpha encodes a 647 aa polypeptide missing two Ig-like C2-type domains and has a truncated (23 aa) cytoplasmic tail (5). Siglec-2/CD22 is an adhesion molecule that preferentially binds alpha 2,6- linked sialic acid on the same (cis) or adjacent (trans) cells. Interaction of CD22 with trans ligands on opposing cells was found to be favored over the binding of ligands in cis (9). Besides its role as an adhesion molecule, Siglec-2/CD22 is a coreceptor that physically interacts with B cell receptor (BCR) and is rapidly phosphorylated upon BCR ligation. It negatively regulates BCR signals by recruiting tyrosine phosphatase SHP-1 to its ITIMs. Phosphorylated Siglec-2/CD22 can also interact with other intracellular effector proteins such as Syk, PLC gamma, PI3 kinase, and Grb-2, suggesting it may play a role in positive signaling (2, 7, 8).
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- Collins, B.E. et al. (2004) Proc. Natl. Acad. Sci. USA 101:6104.
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