Recombinant Human Siglec-2/CD22 Protein, Atto 488 Conjugate Summary
| Human Siglec-2/CD22|
Accession # CAA42006.1
Excitation Wavelength: 501 nm
Emission Wavelengh: 523 nm
|Formulation||Supplied as a 0.2 μm filtered solution in PBS with BSA as a carrier protein.|
|Shipping||The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Protect from light. Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
Fluorescent beads conjugated to anti-Human Siglec 2/CD22 Monoclonal Antibody (MAB1968) were stained with (A) Recombinant Human Siglec 2/CD22 Protein, Atto 488 Conjugate (Catalog # ATJ1968) or (B) unstained.
2 μg/lane of Recombinant Human Siglec-2/CD22 Protein, Atto 488 Conjugate (Catalog # ATJ1968) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 114-126 kDa adn 228-252 kDa, respectively.
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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