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FERMT1 encodes a member of the fermitin family, and contains a FERM domain and a pleckstrin homology domain. Additionally we are shipping FERMT1 Antibodies (49) and FERMT1 Proteins (5) and many more products for this protein.
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The rof/kindlin-1 mutant zebrafish provi (show ILK ELISA Kits)des a unique model system to study epidermal adhesion mechanisms in vivo.
These results indicate that Kindlin-1 is essential in EGF (show EGF ELISA Kits)-induced re-epithelialization in skin wound healing and provide additional rationale for the clinical application of EGF (show EGF ELISA Kits) in the treatment of acute wounds.
By modulating its affinity with kindlin, beta3 integrin (show ITGB3 ELISA Kits) may be able to locate near the cell edge where it can control beta1 integrin activation and clustering.
Kindlin-1 is highly expressed in epithelial tissues derived from ectoderm and endoderm. Kindlin-1 was also found highly expressed in endoderm/ectoderm-derived tissues in embryos.
Kindlin-1 controls keratinocyte adhesion through beta1-class integrins and proliferation and differentiation of cutaneous epithelial stem cells via TGF-beta (show TGFB1 ELISA Kits) activation and Wnt (show WNT2 ELISA Kits)-beta-catenin (show CTNNB1 ELISA Kits) signal inhibition.
Kindlin-1 and Kindlin-2 have opposite roles in lung cancers
Kindlin-1 in mice gives rise to skin atrophy and an intestinal epithelial dysfunction with similarities to human ulcerative colitis.
Kindlin-1 and -2 directly bind the C-terminal region of beta integrin cytoplasmic tails and exert integrin-specific activation effects
KS is caused by mutations in the FERMT1 gene. Including the present, more than 60 mutations in FERMT1 have been identified since 2003. In spite of the expanding FERMT1 mutation database, there seems to be a lack of a clear genotype-phenotype correlation in KS
A nonsense mutation in Exon 5 of KIND1 Gene in an Iranian Family may lead to incomplete and non-functional protein products and is pathogenic and has meaningful implications for the diagnosis of patients with Kindler syndrome.
we show that a certain number of KS patients may harbor FERMT1 transcriptional regulatory mutations which are not routinely detected.
Kindlin-1 is highly expressed in epithelial tissues derived from ectoderm and endoderm, whereas Kindlin-2 is mainly expressed in mesoderm-derived tissues. Likewise, Kindlin-1 was also found highly expressed in endoderm/ectoderm-derived tissues in embryos.
FERMT1 mutation causing Kindler syndrome.
our data suggest that Kindlin-1 could play an important role in hepatocellular carcinoma and might serve as a promising prognostic marker and potential target for hepatocellular carcinoma therapy.
A spectrum of FERMT1 mutations in 13 Iranian families with a diagnosis of Kindler syndrome have been ascertained.
We identified a novel mutation in FERMT1. These data are in agreement with the fact that the majority of KS-causing mutations in FERMT1 lead to premature termination of translation and to loss of kindlin-1 function in Kindler sysndrome
C-terminal LIM (show PDLIM5 ELISA Kits) domains of migfilin (show FBLIM1 ELISA Kits) dictate its focal adhesion localization, and these domains mediate an interaction with kindlin in vitro and in cells, demonstrating that kindlin is important for normal migfilin (show FBLIM1 ELISA Kits) dynamics.
Kindlin1 knockdown resulted in developmental delays, gross malformations of the gut (show GUSB ELISA Kits) and eventual lethality by tadpole stages.
This gene encodes a member of the fermitin family, and contains a FERM domain and a pleckstrin homology domain. The encoded protein is involved in integrin signaling and linkage of the actin cytoskeleton to the extracellular matrix. Mutations in this gene have been linked to Kindler syndrome.
fermitin family member 1
, fermitin family homolog 1
, fermitin family homolog 1-like
, unc-112-related protein 1
, UNC112 related protein 1
, kindlin 1
, kindlin syndrome protein
, UNC-112 related protein 1