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Our studies identify Kindlin-2 as a stabilizing linker of endothelial AJs with the actin cytoskeleton, thereby re-enforcing the vascular barrier.
Kindlin-2 is a key protein that couples cell adhesion by activating integrins and the induction of membrane protrusions by activating Rac1 and supplying Rac1 with the Arp2 (show AICDA Proteins)/3 complex.
demonstration that Smurf1 (show SMURF1 Proteins) acts as a brake for integrin activation by controlling Kindlin-2 protein levels, a new mechanism that permits precise modulation of integrin-mediated cellular functions
Postnatal loss of Kindlin-2 from cardiac myocytes leads to progressive heart failure.
Data indicate that Kindlin-2 not only maintains the cardiac structure but also is required for cardiac function.
These findings show that talin and kindlin cooperatively activate integrins leading to fibronectin (show FN1 Proteins) binding and adhesion.
These studies uncover a previously unrecognized function for Kindlin-2 and a mechanism for regulation of the chondrocyte differentiation programme and chondrogenesis.
Taken together, our study suggests the suppressive roles of Kindlin-2 in the pathogenesis of colorectal carcinoma
Data suggest that kindlin-2 (Kind2/Fermt2) interacts with actin alpha 2 (Actn2 (show ACTN2 Proteins)) and integrin beta 1 (Itgb1 (show ITGB1 Proteins)) and co-localizes to cardiac sarcomere at Z-disc; knockdown of Kind2 leads to dissociation of Actn2 (show ACTN2 Proteins) and Itgb1 (show ITGB1 Proteins).
beta3/kindlin-2 interaction promotes outside-in alphaVbeta3 signaling selectively, with biological consequences in vivo [kindlin-2]
Results found Kindlin-2 expression upregulated in hepatocellular carcinoma (HCC (show FAM126A Proteins)) tissues and cell lines and it correlates with aggressive clinicopathological features and poor prognosis. Mechanistically, Kindlin-2 promotes HCC (show FAM126A Proteins) invasion, metastasis and epithelial-mesenchymal transition through Wnt (show WNT2 Proteins)/beta-catenin (show CTNNB1 Proteins) signaling.
Kindlin-2 is mainly expressed in the cytoplasm and nuclei of fibroblasts in the Esophageal cancer (EC) stroma. Kindlin-2 is upregulated in ECs compared with normal esophageal tissues. Kindlin-2 is more prevalent in poorly differentiated tumors. Kindlin-2 is expressed higher in EC smoker patients than non-smoker patients. Patients with a family history of EC show lower Kindlin-2 expression.
Long noncoding RNA-ATB functions as a molecular sponge for miR (show MLXIP Proteins)-200b and Kindlin-2.
Kindlin-2 is up-regulated in glioma cells and acts as an oncogene (show RAB1A Proteins). It is an independent risk factor for poor prognosis. The Kindlin-2/YB-1 (show YBX1 Proteins)/beta-catenin (show CTNNB1 Proteins) complex promotes EGFR (show EGFR Proteins) transcription and contributes to glioma progression. Kindlin-2 is a potential diagnostic and prognostic marker in glioma, and inhibition of Kindlin-2 may be a novel strategy for glioma treatment.
the rs17125944 polymorphism in FERMT2 gene might not be association with late-onset Alzheimer's disease in northern Han Chinese population
analysis of the Kindlin-2-RhoGDIalpha-Rac1 signaling axis that is critical for regulation of podocyte structure and function in vivo
Study found that FERMT2 (a beta3-integrin (show ITGB3 Proteins) co-activator) was significantly associated with a variation in cerebrospinal fluid Abeta (show APP Proteins) peptide levels in 2886 Alzheimer's disease cases.Under-expression of FERMT2 increases Abeta (show APP Proteins) peptide production by raising levels of mature APP (show APP Proteins) at the cell surface and facilitating its recycling
High kindlin 2 expression is associated with Breast Cancer.
Data suggest that the extreme C terminus of kindlin-2 is essential for interaction with and activation of integrin alphaIIBbeta3; these studies were conducted in macrophage cell line and erythroleukemia cell line.
We show a direct relationship between kindlin-1 (show FERMT1 Proteins) abundance and UV-B induced apoptosis in keratinocytes, whereas kindlin-2 overexpression has no compensatory effect.
Participates in the connection between ECM adhesion sites and the actin cytoskeleton and also in the orchestration of actin assembly and cell shape modulation. Recruits migfilin (FBLP1) protein to cell-ECM focal adhesion sites (By similarity).
fermitin family homolog 2
, mitogen inducible 2
, pleckstrin homology domain containing, family C (with FERM domain) member 1
, pleckstrin homology domain-containing family C member 1
, PH domain-containing family C member 1
, kindlin 2
, mitogen inducible gene 2 protein
, mitogen-inducible gene 2 protein
, pleckstrin homology domain containing, family C member 1