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Mediates B-cell B-cell interactions. Additionally we are shipping CD22 Antibodies (649) and CD22 Kits (32) and many more products for this protein.
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Thus, proximity labeling with tyramide appears to be a useful method to identify cis (show CISH Proteins)-ligands and to analyze their interaction with the lectins.
This combined approach suggests that the inhibitory function of CD22 is influenced by its nanoscale organization and is ensured by its fast diffusion enabling a "global BCR (show BCR Proteins) surveillance" at the plasma membrane.
results demonstrate that loss of high affinity CD22 ligands on GC B (show NPR2 Proteins)-cells occurs in both mice and humans through alternative mechanisms, unmasking CD22 relative to naive and memory B-cells
A noncatalytic role for CD45 (show PTPRC Proteins) in regulating tonic, but not antigen-mediated, B-cell antigen receptor (BCR (show BCR Proteins)) signaling through modulation of the function of the inhibitory coreceptor CD22, was identified.
CD22 is recruited to the immunological synapse by sialic acid ligands on the Ag-bearing cells, producing a tolerogenic signal involving Lyn (show LYN Proteins) and the proapoptotic factor BIM (show BCL2L11 Proteins) that promotes deletion of the B cell and failure of mice to develop Abs to the Ag upon subsequent challenge.
These data assign a key role to CCL22 (show CCL22 Proteins) in Treg recruitment in the protection of NOD mice against type 1 diabetes following the treatment with G-CSF (show CSF3 Proteins).
Thus, CD22 plays an essential role in controlling West Nile virus infection by governing cell migration and CD8 (show CD8A Proteins)(+) T cell responses.
that neither B cells nor CD22 are critical for the immediate antiinflammatory activity of IVIgs in mouse models of rheumatoid arthritis and ITP (show ITPA Proteins).
Increased red cell turnover in a line of CD22-deficient mice is caused by Gpi1c: a model for hereditary haemolytic anaemia.
novel expression pattern and tissue eosinophilia-regulating function for the "B cell-specific" inhibitory molecule CD22 on GI eosinophils.
This is the first time a NMR-based binding study of high affinity Siglec-2 (CD22) ligands in complex with whole Burkitt's lymphoma Daudi cells has been described.
Here the authors structurally characterize the ectodomain of CD22 and present its crystal structure with the bound therapeutic antibody epratuzumab, which gives insights into the mechanism of inhibition of B-cell activation (show BLNK Proteins).
hCD22 transgenic mice develop normal humoral responses in a peanut allergy oral sensitization model. Homing of B cells to Peyer's patches was partially rescued by expression of hCD22 compared with CD22(-/-) B cells, although not to wild-type levels.
Diabody-based (177)Lu-radioimmunoconjugate for CD22-directed radioimmunotherapy reduced disease burden in a non-Hodgkin lymphoma mouse model.
Siglec-1 (show SIGLEC1 Proteins) and Siglec-2 are potential biomarkers in autoimmune disease. (Review)
We aimed to screen exons 9-14 of the CD22 gene, which is a mutational hot spot region in B-precursor acute lymphoblastic leukemia (pre-B ALL) patients. Nine variants, of which two novel, were found. Novel variants were in introns 10 and 13. Gly745Asp (rs10406069) variant was missense and Cys790Arg (rs79438722) variant was silent.
Anti-CD22-magnetic nanoparticles-doxorubicin inhibited the proliferation of Raji cells, significantly increased the uptake of doxorubicin, and induced apoptosis.
MicroRNA-19a and CD22 Comprise a Feedback Loop for B Cell Response in Sepsis.
These results suggest that the in vivo mechanism of non-ligand-blocking epratuzumab may, in part, involve the unmasking of CD22 to facilitate the trans-interaction of B cells with vascular endothelium.
Mediates B-cell B-cell interactions. May be involved in the localization of B-cells in lymphoid tissues. Binds sialylated glycoproteins\; one of which is CD45. Preferentially binds to alpha-2,6-linked sialic acid. The sialic acid recognition site can be masked by cis interactions with sialic acids on the same cell surface. Upon ligand induced tyrosine phosphorylation in the immune response seems to be involved in regulation of B-cell antigen receptor signaling. Plays a role in positive regulation through interaction with Src family tyrosine kinases and may also act as an inhibitory receptor by recruiting cytoplasmic phosphatases via their SH2 domains that block signal transduction through dephosphorylation of signaling molecules.
B-cell receptor CD22
, B-lymphocyte cell adhesion molecule
, T-cell surface antigen Leu-14
, sialic acid-binding Ig-like lectin 2
, CD22 antigen
, sialic acid binding Ig-like lectin 2
, Sialic acid-binding Ig-like lectin 2