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Mediates B-cell B-cell interactions. Additionally we are shipping CD22 Proteins (31) and CD22 Kits (24) and many more products for this protein.
Showing 10 out of 657 products:
Mouse (Murine) Monoclonal CD22 Primary Antibody for FACS - ABIN370869
Symington, Subbarao, Mosier, Sprent: Lyb-8.2: A new B cell antigen defined and characterized with a monoclonal antibody. in Immunogenetics 1983
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Human Polyclonal CD22 Primary Antibody for WB - ABIN611291
Bartoli, Gu, Tsai, Venema, Brooks, Marrero, Caldwell: Vascular endothelial growth factor activates STAT proteins in aortic endothelial cells. in The Journal of biological chemistry 2000
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Horse (Equine) Polyclonal CD22 Primary Antibody for WB - ABIN611290
Bromberg, Darnell: The role of STATs in transcriptional control and their impact on cellular function. in Oncogene 2000
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Human Monoclonal CD22 Primary Antibody for ICC, FACS - ABIN1724888
Kawasaki, Rademacher, Paulson: CD22 regulates adaptive and innate immune responses of B cells. in Journal of innate immunity 2011
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Human Monoclonal CD22 Primary Antibody for ICC, FACS - ABIN1724887
Tuscano, Kato, Pearson, Xiong, Newell, Ma, Gandara, ODonnell: CD22 antigen is broadly expressed on lung cancer cells and is a target for antibody-based therapy. in Cancer research 2012
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Human Polyclonal CD22 Primary Antibody for ELISA, WB - ABIN1533134
Stamenkovic, Seed: The B-cell antigen CD22 mediates monocyte and erythrocyte adhesion. in Nature 1990
Human Monoclonal CD22 Primary Antibody for FACS - ABIN4896270
Jelicic, Cimbro, Nawaz, Huang, Zheng, Yang, Lempicki, Pascuccio, Van Ryk, Schwing, Hiatt, Okwara, Wei, Roby, David, Hwang, Kehrl, Arthos, Cicala, Fauci: The HIV-1 envelope protein gp120 impairs B cell proliferation by inducing TGF-β1 production and FcRL4 expression. in Nature immunology 2013
Human Monoclonal CD22 Primary Antibody for IHC (p) - ABIN118611
Tedder, Tuscano, Sato, Kehrl: CD22, a B lymphocyte-specific adhesion molecule that regulates antigen receptor signaling. in Annual review of immunology 1997
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 Antibodies) surveillance" at the plasma membrane.
results demonstrate that loss of high affinity CD22 ligands on GC B (show NPR2 Antibodies)-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 Antibodies) in regulating tonic, but not antigen-mediated, B-cell antigen receptor (BCR (show BCR Antibodies)) 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 Antibodies) and the proapoptotic factor BIM (show BCL2L11 Antibodies) 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 Antibodies) in Treg recruitment in the protection of NOD mice against type 1 diabetes following the treatment with G-CSF (show CSF3 Antibodies).
Thus, CD22 plays an essential role in controlling West Nile virus infection by governing cell migration and CD8 (show CD8A Antibodies)(+) 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 Antibodies).
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.
As a receptor for sIgM, CD22 induces a negative feedback loop for B-cell activation (show BLNK Antibodies)/
Diabody-based (177)Lu-radioimmunoconjugate for CD22-directed radioimmunotherapy reduced disease burden in a non-Hodgkin lymphoma mouse model.
Siglec-1 (show SIGLEC1 Antibodies) 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.
By using integrative genomics and analysing the relationships of COPD (show ARCN1 Antibodies) phenotypes with SNPs and gene expression in lung tissue, we identified CST3 (show CST3 Antibodies) and CD22 as potential causal genes for airflow obstruction.
study detected the expression of CD22 and CD72 (show CD72 Antibodies) on B cells of myasthenia gravis, compared to multiple sclerosis patient controls and healthy controls y
In the absence of functional CD22, B cells have a "hyperactivated" phenotype, CD22 dysfunction could contribute to the pathogenesis of autoimmune diseases. (Review)
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