Use your antibodies-online credentials, if available.
Keine Produkte auf Ihrer Vergleichsliste.
Ihr Warenkorb ist leer.
Weitere Synonyme anzeigen
Wählen Sie die gewünschte Spezies
Knocking down of PLXNB2 with PLXNB2 siRNA results in repressed ovarian cancer cell proliferation and invasion, and decreased phosphorylation of AKT and ERK1/2
Study shows that plexin-B2 (PLXNB2) is the functional receptor for ANG in endothelial, cancer, neuronal, and normal hematopoietic and leukemic stem and progenitor cells.
Analysis of the interaction of Plexin-B1 and Plexin-B2 with Rnd family proteins shows lack of binding specificity.
plexin-B2 is a downstream target for Rnd3, which contributes to its cellular function.
Results show that decreased expression of Sema4D, plexin-B1 and -B2 was associated with local recurrence and poor prognosis of breast neoplasm.
Two related guanine nucleotide exchange factors (GEFs), PDZ-RhoGEF and leukemia-associated RhoGEF (LARG), use their PDZ domains to bind class B plexins and play critical roles in signaling.
Plexin-B2 promotes glioma invasion and vascularization
Blocking of CD100, plexin B1 and/or B2 in adhesion experiments have shown that both CD100 and plexins act as adhesion molecules involved in monocyte-endothelial cell binding.
In endometrial luminal epithelium, cadherin 6, desmoglein 2 and plexin b2 were surprisingly found in the apical as well as the lateral membrane domain; their knock-down compromised epithelial integrity.
High PLEXIN B2 expression is associated with high-grade gliomas.
Plexin B2 associates directly with two members of a recently identified family of Dbl homology/pleckstrin homology containing guanine nucleotide exchange factors for Rho, PDZ-RhoGEF, and Leukemia-associated Rho GEF (LARG).
cleavage by proprotein convertases is a novel regulatory step for semaphorin receptors localized at the cell surface.
Germinal center recruitment of follicular T helper cells requires Plexin B2.
Plexin-B1 and -B2 play redundant or compensatory roles during forebrain development to ensure proper neuronal production and neocortical expansion.
During kidney morphogenesis and repair, renal tubular epithelial cells lacking the transmembrane receptor Plexin-B2 or its semaphorin ligands fail to correctly orient the mitotic spindle
Data show that the Plexin B2 receptor interacts physically and functionally with Rnd3 and stimulates RhoA activity in migrating cortical neurons.
In contrast to the GAP domain mutants, Plexin-B2 transgenic mice defective in Rho guanine nucleotide exchange factor binding are viable and fertile but exhibit abnormal development of the liver vasculature
these results show that Plexin-B2 plays a role in postnatal neurogenesis and in the migration of subventricular zone-derived neuroblasts
Data an association between Plexin-B2 and Plexin-D1 with the negative regulation of IL-12/IL-23p40 in DCs.
In vitro blocking of plexin B2 or CD100 inhibited gamma-delta T cell activation.
Data show that Plexin-B2 functions in macrophages as a negative regulator of the GTPases Rac and Cdc42 and as a negative regulator of basal cell motility and wound healing.
deletion of Plexin B2 (Plxnb2), a semaphorin receptor that is expressed both in the pretubular aggregates and the ureteric epithelium in the developing kidney, results in renal hypoplasia and occasional double ureters
We have identified here Sema4C and Sema4G as candidate ligands for Plexin-B2
Plexin-B2 and Sema4C are potential regulators of the vascular and endocrine system.
Sema4D-plexin-B2 interactions regulate mechanisms underlying cell specification, differentiation, and migration during corticogenesis.
Plexin-B2 controls the balance between cell proliferation and differentiation in cerebellar granule cells.
Plexin-B2 is critically required for several developmental processes in vivo, including proliferation, migration, and pattern formation in the mouse forebrain and the cerebellum.
Members of the B class of plexins, such as PLXNB2 are transmembrane receptors that participate in axon guidance and cell migration in response to semaphorins (Perrot et al. (2002)
, differentially expressed in brain tumors