Immobilized Anti-Human Siglec-2 mAb at 2μg/ml (100 μl/well)can bind Human Siglec-2-Fc. The ED50 of Human Siglec-2-Fc is 24.05 ng/ml. (Regularly tested)

Siglec-2/CD22 Protein, Human, Recombinant (hFc) is expressed in HEK293 mammalian cells with C-Fc tag. The predicted molecular weight is 120-150 KDa and the accession number is P20273.

Human

HEK293 Cells

BL-CAM,SIGLEC2FLJ22814,CD22 antigenMGC130020,sialic acid binding Ig-like lectin 2,B-lymphocyte cell adhesion molecule,T-cell surface antigen Leu-14,Siglec-2,CD22,B-cell receptor CD22,CD22 molecule

Asp20-Arg687

Asp20-Arg687

Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Reconstitute the lyophilized protein in distilled water. The product concentration should not be less than 100 μg/ml. Before opening, centrifuge the tube to collect powder at the bottom. After adding the reconstitution buffer, avoid vortexing or pipetting for mixing.

Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.

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. 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. 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.