Human Siglec-2/CD22 Antibody Summary
Asp20-Arg687
Accession # CAA42006
Applications
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.
Scientific Data
Detection of Human Siglec‑2/CD22 by Western Blot. Western blot shows lysates of Daudi human Burkitt's lymphoma cell line. PVDF membrane was probed with 0.2 µg/mL of Mouse Anti-Human Siglec-2/CD22 Monoclonal Antibody (Catalog # MAB19681) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF018). A specific band was detected for Siglec-2/CD22 at approximately 140 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
Reconstitution Calculator
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.
Background: Siglec-2/CD22
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).
- Crocker, P.R. and A. Varki (2001) Trends Immunol. 22:337.
- Crocker, P.R. and A. Varki (2001) Immunology 103:137.
- Angata, T. et al. (2002) J. Biol. Chem. 277:24466.
- Wilson, G.L et al. (1991) J. Exp. Med. 173:137.
- Stamenkovic, I. and B. Seed (1990) Nature 345:74.
- Kelm, S. et al. (1994) Current Bio. 4:965.
- Ravetch, J.V. and L.L. Lanier (2000) Science 290:84.
- Wienands, Y.J. et al. (1999) J. Biol. Chem. 274:18769.
- Collins, B.E. et al. (2004) Proc. Natl. Acad. Sci. USA 101:6104.
Product Datasheets
Citation for Human Siglec-2/CD22 Antibody
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
1 Citation: Showing 1 - 1
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Modulation of CD22 Protein Expression in Childhood Leukemia by Pervasive Splicing Aberrations: Implications for CD22-Directed Immunotherapies
Authors: Sisi Zheng, Elisabeth Gillespie, Ammar S. Naqvi, Katharina E. Hayer, Zhiwei Ang, Manuel Torres-Diz et al.
Blood Cancer Discovery
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