| Reactivity | HuSpecies Glossary |
| Applications | Flow, CyTOF-ready |
| Clone | 219934 |
| Clonality | Monoclonal |
| Host | Mouse |
| Conjugate | Unconjugated |
| Concentration | LYOPH |
| Immunogen | Mouse myeloma cell line NS0-derived recombinant human Siglec-2/CD22 Asp20-Arg687 Accession # CAA42006 |
| Specificity | Detects human Siglec-2 in direct ELISAs. In direct ELISAs, no cross-reactivity with recombinant human Siglec-3, -5, -7, -9, -10, -F, or recombinant mouse Siglec‑11 is observed. |
| Source | N/A |
| Isotype | IgG1 |
| Clonality | Monoclonal |
| Host | Mouse |
| Gene | CD22 |
| Purity Statement | Protein A or G purified from hybridoma culture supernatant |
| Innovator's Reward | Test in a species/application not listed above to receive a full credit towards a future purchase. |
| Dilutions |
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| Publications |
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| Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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| Buffer | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. See Certificate of Analysis for details. *Small pack size (-SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS. |
| Preservative | No Preservative |
| Concentration | LYOPH |
| Reconstitution Instructions | Reconstitute at 0.5 mg/mL in sterile PBS. For liquid material, refer to CoA for concentration. |
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 V-type Ig-like domain which mediates sialic acid binding, followed by varying numbers of C2-type Ig-like domains (1, 2). Fourteen 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, plus 14 to 16 (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 and intestinal eosinophils (3,4). 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 V-type N-terminal Ig-like domain, six C2-type Ig-like domains, a transmembrane region and a cytoplasmic tail with 4 immunoreceptor tyrosine-based inhibition motifs (ITIMs) (5). The variant Siglec-2/CD22 alpha encodes a 647 aa polypeptide missing two C2-type Ig-like domains and has a truncated (23 aa) cytoplasmic tail (6). Siglec-2/CD22 is an adhesion molecule that preferentially binds alpha 2,6- linked sialic acid on the same (cis) or adjacent (trans) cells. 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 (3). It negatively regulates BCR signals by recruiting tyrosine phosphatase SHP-1 to its ITIMs, likely within large oligomeric complexes. Over aa 20-687, human and mouse share 59% aa sequence identity.
Secondary Antibodies |
Isotype Controls |
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Antigen-loss relapse after successful CAR-T therapy; What do we do now? By Jacqueline Carrico, BS, MD Tumor cell mechanisms driving tolerance to CAR-T Despite very promising results of CAR-T therapy in acute lymphoblastic leukemia, B-ALL, antigen-loss relapse has arisen as a major chall... Read full blog post. |
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