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FHL2 is an important prognostic factor in cervical cancer (CC) and that it plays a crucial oncoprotein role by promoting cell proliferation and inhibiting apoptosis in CC.
FHL2 and iASPP interacted with each other and co-localized in both nucleus and cytoplasm. Either FHL2 or iASPP silenced could reduce cell proliferation, induce cell cycle arrest at G0/G1 phase, and increase cell apoptosis.
FHL2 phosphorylation by FAK is a critical, mechanically dependent step in signaling from soft matrices to the nucleus to inhibit cell proliferation by increasing p21 expression.
FHL2 facilitates ovarian granulosa cell tumor progression via controlling AKT1 transcription.
we determined the molecular mechanism responsible for IER3 degradation, involving a ternary complex of IER3, MDM2 and FHL2, which may contribute to cervical tumor growth. Furthermore, we demonstrated that FHL2 serves as a scaffold for E3 ligase and its substrate during the ubiquitination reaction, a function that has not been previously reported for this protein
FHL2 interacts with ADAM-17 in normal, dysplastic and malignant colon epithelial cells. Colocalisation of these proteins is more frequent in malignant than in normal and dysplastic cells, suggesting a role for ADAM-17/FHL2 complex in the development of colorectal cancer.
FHL2 overexpression could enhance the differentiation and mineralization of human dental pulp cells
findings show that mAbp1 and FHL2 are novel binding partners that differentially regulate Rho GTPase signaling and MTLn3 breast cancer cell invasion
These results identify FHL2 as a novel gene associated with asthma severity in human.
FHL2 might interact with Runx2 to mediate mesenchymal cell differentiation at the early stages of tooth development and human dental pulp cell differentiation.
FHL2 overexpression could contribute to the growth, proliferation, invasiveness, and metastasis of human tongue squamous cell carcinoma.
KLF8-induced FHL2 activation is a novel and critical signaling mechanism underlying human colorectal cancer invasion and metastasis.
Studies indicate that the LIM-only protein FHL2 interactome is functionally involved in the cardiovascular system.
we conclude that FHL2 has both structural and functional protein-protein interactions with b-catenin in the podocyte nucleus and that FHL2 protein inhibition can mitigate Wnt/b-catenin-induced podocytopathy.
Describe the molecular network governing FHL2 expression, and FHL2-linked cancers and the underlying molecular machinery. Review.
Tumoral expression of nuclear cofactor FHL2 is associated with lymphatic metastasis in sporadic but not in hereditary nonpolyposis colorectal cancer-associated colorectal cancer.
results provide evidence for the importance of the focal adhesion protein FHL2 in pancreatic cancer cell survival, proliferation and radiosensitivity
FHL2 is down-regulated in HCM; both FHL2 wild type and variants partially protected phenylephrine- or endothelin-1-induced hypertrophy in cardiac myocytes
FHL2 downregulation has a role in the pathogenesis of myeloid malignancies.
HPV16 E6 oncoprotein interacted and impaired the subcellular distribution of FHL2.
Fhl2 anticipates the emerging inflammation and specifically the development of psoriatic arthritis by impeding the Adam17-mediated release of TNF
Loss of FHL2 is associated with liver fibrosis.
loss of Fhl2 leads to an altered immune response to myocardial ischemia, which results in smaller infarcts and better hemodynamic performance up to 21 days after myocardial ischemia reperfusion.
also found that phosphorylation of ERK1/2 is markedly attenuated in FHL2-KO lung
Overexpression of FHL2 alone had no effect on Erbin expression, but in the presence of MITF, Erbin expression was decreased.
these data identify a previously unrecognized role for FHL2 in the pathogenesis of pulmonary granulomatous inflammation
FHL2 serves as a protective factor and that, rather than promoting the pathology, the upregulation of FHL2 in RA occurs in frame of a regenerative attempt.
FHL2 regulates hematopoietic stem cell functions under transplantation-induced stress conditions.
The LIM-only protein FHL2 reduces vascular lesion formation involving inhibition of proliferation and migration of smooth muscle cells.
a database of genes that are regulated by FHL2 in liver
FHL2-deficient mice developed a severe and long-lasting lung pathology due to enhanced expression of tenascin C and impaired activation of inflammation-resolving macrophages.
Early Wnt/beta-catenin-dependent transcriptional activation mediated by FHL2 is important for the transition to and expansion of early cardiogenic mesodermal cells.
Deficiency of FHL2 reduced susceptibility to diethylnitrosamine-induced hepatocarcinogenesis, correlating with the activator function of FHL2 in NF-kappaB signaling.
Deficiency of FHL2 results in aggravation of murine liver fibrosis.
Ex vivo analysis showed decreased basal and Wnt3a-induced Wnt5a and Wnt10b mRNA expression in FHL2-deficient bone marrow cells, further indicating that this defect may contribute to the reduced osteoblast function in FHL2 deficient mice
The four and a half LIM-only protein 2 regulates liver homeostasis and contributes to carcinogenesis.
ROCK2 is essential for the development of cardiac hypertrophy and that up-regulation of FHL2 may contribute to the antihypertrophic phenotype that is observed in cardiac-specific ROCK2-deficient mice.
This gene encodes a member of the four-and-a-half-LIM-only protein family. Family members contain two highly conserved, tandemly arranged, zinc finger domains with four highly conserved cysteines binding a zinc atom in each zinc finger. This protein is thought to have a role in the assembly of extracellular membranes. Also, this gene is down-regulated during transformation of normal myoblasts to rhabdomyosarcoma cells and the encoded protein may function as a link between presenilin-2 and an intracellular signaling pathway. Multiple alternatively spliced variants, encoding the same protein, have been identified.
LIM domain protein DRAL
, aging-associated gene 11
, down-regulated in rhabdomyosarcoma LIM protein
, four and a half LIM domains protein 2
, skeletal muscle LIM-protein 3
, SLIM 3
, four and a half LIM domains 2
, four and half LIM domains protein 2