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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 (53) and FERMT1 Proteins (5) and many more products for this protein.
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Kindlin-1 is mainly expressed in the cytoplasm of normal esophageal squamous epithelium and Esophageal cancer (EC) cells. Kindlin-1 expression is positively correlated with tumor cell differentiation and is higher in stage I tumors. Kindlin-1 expression is higher in non-smoker patients than in smoker patients, and in patients with a family history of EC.
Kindlin supports platelet GPIIB IIIA activation by interacting with paxillin (show PXN ELISA Kits).
we demonstrated that Kindlin-1 promotes CRC (show CALR ELISA Kits) progression by recruiting SARA (show ZFYVE9 ELISA Kits) and Smad3 (show SMAD3 ELISA Kits) to TbetaRI (show TGFBR1 ELISA Kits) and thereby activates TGF-beta (show TGFB1 ELISA Kits)/Smad3 (show SMAD3 ELISA Kits) signaling. Thus, Kindlin-1 is a novel regulator of TGF-beta (show TGFB1 ELISA Kits)/Smad3 (show SMAD3 ELISA Kits) signaling and may also be a potential target for CRC (show CALR ELISA Kits) therapeutics.
Sequence analysis of KIND1 exons in patient 1 revealed a commonly reported homozygous nonsense mutation in exon 6 (c.811C>T;p.R271X). Both Patients 2 and 3 had novel homozygous single nucleotide deletions
these data define a novel role for Kin1 in microtubule acetylation and stability
keratinocytes derived from KS patients are unable to undergo electrotaxis, and this defect is restored by overexpression of wild-type kindlin-1 but not a W612A mutation that prevents kindlin-integrin binding.
FERMT1 activates the beta-catenin (show CTNNB1 ELISA Kits) transcriptional activity to promote EMT (show ITK ELISA Kits) in CC metastasis.
KIND1 is important not only for keratinocyte proliferation but also for the suppression of UV-induced inflammation and DNA damage.
We show a direct relationship between kindlin-1 abundance and UV-B induced apoptosis in keratinocytes, whereas kindlin-2 (show FERMT2 ELISA Kits) overexpression has no compensatory effect.
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.
loss of Kindlin-1 leads to an imbalance in the cellular oxidative state, which renders Kindlin-1 deficient cells more prone to the effects of reactive oxygen species generated in response to oxidative stress
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 (show FERMT2 ELISA Kits) 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
Kindlin1 knockdown resulted in developmental delays, gross malformations of the gut (show GUSB ELISA Kits) and eventual lethality by tadpole stages.
The rof/kindlin-1 mutant zebrafish provides a unique model system to study epidermal adhesion mechanisms in vivo.
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.
UNC112 related protein 1
, fermitin family homolog 1
, kindlin 1
, kindlin syndrome protein
, unc-112-related protein 1
, UNC-112 related protein 1
, fermitin family member 1
, fermitin family homolog 1-like