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TLN1 encodes a cytoskeletal protein that is concentrated in areas of cell-substratum and cell-cell contacts. Additionally we are shipping Talin 1 Antibodies (84) and Talin 1 Proteins (10) and many more products for this protein.
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CD90 (Thy1 (show THY1 ELISA Kits)) is a novel interactor of talin 1 in effector cells of autoimmune equine uveitis.
Both TLN-1 and TLN-2 (show TLN2 ELISA Kits) levels correlate with tumorigenicity in human HCC (show FAM126A ELISA Kits), indicating that these molecules constitute important molecular targets for the diagnosis and/or treatment of hepatocellular carcinoma .
TLN1 significantly increases in refractory glioblastoma multiforme
Applying correlative imaging to link live cell and fixed immunofluorescence data on a single cell basis, we related per cell talin-1 levels to per cell measures quantitatively defining an array of cellular properties.
Disruption of the RIAM/lamellipodin-integrin-talin complex markedly impairs cell migration.
Our data demonstrate that high expression of Talin-1 is associated with significantly poorer OS and poorer DMFS in NPC (show NPC1 ELISA Kits) and depletion of Talin-1 expression inhibited NPC (show NPC1 ELISA Kits) cell migration and invasion. Talin-1 may serve as novel prognostic biomarker in NPC (show NPC1 ELISA Kits).
The activation of vinculin (show VCL ELISA Kits) by stretched talin induces a positive feedback that reinforces the actin-talin-vinculin (show VCL ELISA Kits) association.
Data (including data from molecular dynamic simulations) suggest specific interactions between glycoprotein GPIIb/GPIIIa (show ITGB3 ELISA Kits) complex transmembrane/C-terminal domains and talin-1 in cell membrane environment during platelet activation.
Data suggest that anionic lipids (such as phosphatidylinositol phosphates) play crucial role in localization of peripheral membrane proteins (such as TLN1, auxilin-1, and PTEN [phosphatase and tensin homolog]). [review-like article]
Low levels of Talin-1 expression are correlated with increased invasion and migration in liver cancer.
Data indicate the role of vinculin (show VCL ELISA Kits) in inducing the talin mediated integrin activation.
These findings show that talin and kindlin cooperatively activate integrins leading to fibronectin (show FN1 ELISA Kits) binding and adhesion.
Binding of vinculin (show VCL ELISA Kits) to the R1-R3 region of the talin rod is important for focal adhesion stability.
Data indicate that talin mechanics are isoform specific so that expression of either talin-1 or talin-2 (show TLN2 ELISA Kits) modulates extracellular rigidity sensing.
Conformational activation of talin by PREL-1 (show APBB1IP ELISA Kits) triggers integrin-mediated cell adhesion.
Direct methylation of talin, a key regulatory molecule in cell migration, by Ezh2 disrupted the binding of talin to F-actin and thereby promoted the turnover of adhesion structures.
reduction of talin-beta3 integrin (show ITGB3 ELISA Kits) binding affinity results in decelerated alphaIIbbeta3 integrin activation and protection from arterial thrombosis without pathological bleeding
As talin engages F-actin, force exerted on the R2R3 helical bundles disrupts RIAM (show APBB1IP ELISA Kits) binding and exposes the vinculin (show VCL ELISA Kits) binding sites, which recruit vinculin (show VCL ELISA Kits) to stabilize the complex.
Talin1 has unique expression versus talin 2 (show TLN2 ELISA Kits) in the heart and modifies the hypertrophic response to pressure overload.
Talin1 and Rap1 are critical for resorptive function, and their selective inhibition in mature osteoclasts retards pathological bone loss.
Talin binding to the membrane-proximal NPxY is crucial for connecting alpha5beta1 to the actin cytoskeleton.
suggest that Tln1-mediated Itgbeta1b plays a crucial role in maintaining cardiac sarcomeric Z-disks and endothelial/endocardial cell integrity in zebrafish
This gene encodes a cytoskeletal protein that is concentrated in areas of cell-substratum and cell-cell contacts. The encoded protein plays a significant role in the assembly of actin filaments and in spreading and migration of various cell types, including fibroblasts and osteoclasts. It codistributes with integrins in the cell surface membrane in order to assist in the attachment of adherent cells to extracellular matrices and of lymphocytes to other cells. The N-terminus of this protein contains elements for localization to cell-extracellular matrix junctions. The C-terminus contains binding sites for proteins such as beta-1-integrin, actin, and vinculin.
, Talin 1