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The protein encoded by ICAM2 is a member of the intercellular adhesion molecule (ICAM) family. Zusätzlich bieten wir Ihnen ICAM2 Antikörper (298) und ICAM2 Kits (44) und viele weitere Produktgruppen zu diesem Protein an.
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Human ICAM2 Protein expressed in Human Cells - ABIN2002587
Staunton, Dustin, Springer: Functional cloning of ICAM-2, a cell adhesion ligand for LFA-1 homologous to ICAM-1. in Nature 1989
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Mouse (Murine) ICAM2 Protein expressed in Human Cells - ABIN2008096
Fagerholm, Varis, Stefanidakis, Hilden, Gahmberg: alpha-Chain phosphorylation of the human leukocyte CD11b/CD18 (Mac-1) integrin is pivotal for integrin activation to bind ICAMs and leukocyte extravasation. in Blood 2006
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Human ICAM2 Protein expressed in HEK-293 Cells - ABIN2181239
Xu, Shin, Jaffrey: Global profiling of protease cleavage sites by chemoselective labeling of protein N-termini. in Proceedings of the National Academy of Sciences of the United States of America 2009
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Results indicate that the interaction of ICAM-2 with alpha-actinin (zeige ACTN1 Proteine) is critical to conferring an ICAM-2-mediated non-metastatic phenotype in neuroblastoma (zeige ARHGEF16 Proteine) cells.
ICAM-2 regulates endothelial barrier function and permeability through a pathway involving N-Cadherin, ERMs and Rac-1
These findings highlight novel roles for ICAM-2 in mediating luminal neutrophil crawling and the effect on subsequent levels of extravasation.
beta2 integrin-mediated neutrophil crawling on endothelial ICAM-1 and ICAM-2 is a prerequisite for transcellular neutrophil diapedesis across the inflamed BBB.
a sequential involvement of endothelial ICAM-1 and VCAM-1 in mediating shear-resistant T cell arrest, followed by endothelial ICAM-1 and ICAM-2 in mediating T cell crawling to sites permissive for diapedesis across BBB endothelium.
unique role for ICAM-1 (zeige ICAM1 Proteine) in intraluminal lymphocyte crawling but redundant roles for ICAM-1 (zeige ICAM1 Proteine) and ICAM-2 in lymphocyte diapedesis and interstitial motility
show that the sequential expression of CD40 (zeige CD40 Proteine) and Icam2 delineate a transition in the acquisition of the blood potential from hemangioblast to hemogenic endothelium leading to the formation of primitive and definitive hematopoietic progenitors.
Data report the crystal structure of the radixin (zeige RDX Proteine) FERM (4.1 and ERM (zeige ETV5 Proteine)) domain complexed with the intercellular adhesion molecule-2 (ICAM-2) cytoplasmic peptide.
ICAM-2 and ICAM-1 (zeige ICAM1 Proteine) have redundant functions in lymphocyte recirculation through lymph nodes, but ICAM-2 is not required for the migration of T effector cells into inflamed skin.
The 60 kDa protein, the murine homologue of ICAM-2 (CD102), recognized by the BF/32 antibody was widely expressed on lymphocytes
Both ICAM-2 and ICAM-1 (zeige ICAM1 Proteine) levels in plasma were markedly increased in Ankylosing Spondylitis Chinese patients compared to controls.
Soluble ICAM2 was higher in ADHD patients than in controls.
ICAM-1 (zeige ICAM1 Proteine) and ICAM-2 are involved in each step of neutrophil extravasation, and have redundant but also distinct functions. Analysis of the role of endothelial ICAM-1 (zeige ICAM1 Proteine) requires simultaneous consideration of ICAM-2.
with larger patient groups and preferably detailed histopathological and clinical evaluations, are needed to explain the severity of ICAM-1 (zeige ICAM1 Proteine), ICAM-2, and ICAM-3 (zeige ICAM3 Proteine) molecules in Barrett's esophagus
ICAM-2 was significantly more pronounced in plasma cell mastitis than in nonpathologic breast tissue. However, no significant differences in ICAM-2 immunoreactivity were detected between ductal epithelium of PCM (zeige PCMT1 Proteine) and non-PCM (zeige PCMT1 Proteine).
Reduced glycosylation of ICAM-2 significantly attenuated, but did not abolish, its ability to suppress metastatic properties of neuroblastoma (zeige ARHGEF16 Proteine) cells.
These findings suggested that the downregulated miR (zeige MLXIP Proteine)-125b expression was associated with proliferation and radioresistance mechanisms, probably through ICAM2 signalling.
Immune surveillance occurs during the early intraepithelial stages of human pancreatic carcinogenesis and is mediated by expression of CXCL17 (zeige CXCL17 Proteine) and ICAM2.
Although ICAM-2 colocalizes with moesin (zeige MSN Proteine) and F-actin in microvilli of unstimulated endothelial cells, it is not involved in RhoA (zeige RHOA Proteine) activation or cause stress fiber formation upon cross-linking.
ICAM-2 plays a role in the cellular interactions associated with xenograft rejection
pig and human ICAM-2 promoters exhibit many similarities
The protein encoded by this gene is a member of the intercellular adhesion molecule (ICAM) family. All ICAM proteins are type I transmembrane glycoproteins, contain 2-9 immunoglobulin-like C2-type domains, and bind to the leukocyte adhesion LFA-1 protein. This protein may play a role in lymphocyte recirculation by blocking LFA-1-dependent cell adhesion. It mediates adhesive interactions important for antigen-specific immune response, NK-cell mediated clearance, lymphocyte recirculation, and other cellular interactions important for immune response and surveillance. Several transcript variants encoding the same protein have been found for this gene.
intercellular adhesion molecule 2
, lymphocyte function-associated AG-1 counter-receptor