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Human Polyclonal TLN1 Primary Antibody for ICC, IF - ABIN4357781
Philippe, Léger, Desvaux, Walch: Discs large 1 (Dlg1) scaffolding protein participates with clathrin and adaptator protein complex 1 (AP-1) in forming Weibel-Palade bodies of endothelial cells. in The Journal of biological chemistry 2013
Show all 3 Pubmed References
Human Monoclonal TLN1 Primary Antibody for IF, IHC (p) - ABIN2476678
Barlet-Bas, Cheval, Khadouri, Marsy, Doucet: Difference in the Na affinity of Na(+)-K(+)-ATPase along the rabbit nephron: modulation by K. in The American journal of physiology 1990
Show all 4 Pubmed References
Human Monoclonal TLN1 Primary Antibody for IHC (p), ELISA - ABIN520958
Lai, Hua, Tsai, Wan, Lin, Chen, Chiu, Chan, Tsai, Jinn-Chyuan Sheu: Talin-1 overexpression defines high risk for aggressive oral squamous cell carcinoma and promotes cancer metastasis. in The Journal of pathology 2011
Chicken Monoclonal TLN1 Primary Antibody for ICC, FACS - ABIN439404
Longo, Ioannidu, Scotto dAbusco, Superti, Misiano, Zanoni, Politi, Mazzola, Iosi, Mura, Scandurra: Improving Osteoblast Response In Vitro by a Nanostructured Thin Film with Titanium Carbide and Titanium Oxides Clustered around Graphitic Carbon. in PLoS ONE 2016
Mouse (Murine) Monoclonal TLN1 Primary Antibody for ELISA, ICC - ABIN4246336
Lagarrigue, Gingras, Paul, Valadez, Cuevas, Sun, Lopez-Ramirez, Goult, Shattil, Bergmeier, Ginsberg: Rap1 binding to the talin 1 F0 domain makes a minimal contribution to murine platelet GPIIb-IIIa activation. in Blood advances 2018
The N-terminal ABD1 of TLN blocks actin filament barbed-end elongation, whereas ABD2 and ABD3 do not show any activity.
Expression of ecotopic viral integration site 1 (EVI1) is positively correlated with talin1 (TLN1) in both chronic myeloid leukemia (CML)-chronic phase (CP) and CML-blast crisis (BC) cases.
Low TLN1 expression is associated with invasion and metastasis in Hepatocellular Carcinoma.
Calpain small subunit 1 (Capn4) overexpression increased the protein level of cleaved talin and and activated the focal adhesion kinase (FAK)/AKT/MAPK signaling in 786-O cells, while Capn4 silencing decreased the protein level of cleaved talin in Caki-1 cells.
Talin-1 induces proliferation and migration of vascular smooth muscle cells obtained from patients with thoracic aortic dissection.
Here, the authors show that cortical microtubule stabilization sites containing CLASPs, KIF21A, LL5beta and liprins are recruited to focal adhesions by the adaptor protein KANK1, which directly interacts with the major adhesion component, talin. Structural studies showed that the conserved KN domain in KANK1 binds to the talin rod domain R7.
Vinculin head-tail interaction is required on soft substrates to destabilize vinculin and talin in FAs, and to allow hMSCs branching. Another module involves paxillin and FAK, which soft substrates also destabilize, but independently of vinculin head-tail interaction. This multi-modularity may be key to allow a versatile response to complex biomechanical cues.
The central role of talin and vinculin in cell adhesions suggests that the disintegration of the tissue in atherosclerosis could be partially driven by downregulation of these genes, leading to loosening of cell-ECM interactions and remodeling of the tissue.
Application of these techniques to new talin biosensors reveals an intramolecular tension gradient across talin-1 that is established upon integrin-mediated cell adhesion. The tension gradient is actomyosin- and vinculin-dependent and sensitive to the rigidity of the extracellular environment
Our findings confirm the role of Talin-1 in carcinogenesis and provided a set of novel therapeutic targets for the treatment of hepatocellular carcinoma
These data show that TLN1 can act as a viral restriction factor that suppresses hepatitis B virus replication, and suggest that the HBx relieves this restriction by inducing TLN1 degradation.
The ERK pathway was responsible for these promoting effects of Talin1 knockdown in HCC cells.
This study showed that serum sTalin-1 levels were associated with a sustained increase in disability after MS attack but not with serum anti-Talin-1 antibody levels.
The Rap1-RIAM-talin axis of integrin activation and blood cell function
These findings suggested that Talin-1 protein was significantly upregulated in PCa tissues compared with that of BPH tissue and Talin-1 expression was an independent predictor for lymph node metastasis and biochemical recurrence of PCa.
Serum talin-1 had 97.7% sensitivity.
Both TLN-1 and TLN-2 levels correlate with tumorigenicity in human HCC, 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.
the Rap1-talin 1 F0 interaction has little effect on platelet GPIIb-IIIa activation and hemostasis and cannot account for the dramatic effects of loss of Rap1 activity on these platelet functions.
this study shows that Talin1 methylation is required for neutrophil infiltration during murine peritonitis
findings suggest that direct Rap1/Talin1 interaction is of particular importance in regulating the activity of different integrin classes expressed on platelets and neutrophils, which both depend on fast and dynamic integrin-mediated responses.
talin unfolding determines DLC1 downstream signalling and, consequently, cell mechanics.
Talin-F0 domain binds to Rap1b like canonical Rap1 effectors despite little sequence homology, and disruption of the binding strongly impairs integrin activation, cell adhesion, and cell spreading.
The mechanical response of talin-1 has been reported.
Loss of all Tln forms from the heart-muscle cell leads to myocyte instability and a dilated cardiomyopathy.
expression is markedly suppressed in pathologically activated osteoclasts
SKAP1 can affect the function of talin in T-cells needed for optimal T-cell/dendritic cell conjugation
talins are essential for kidney collecting duct development through mechanisms that extend beyond those requiring binding to the beta1 integrin subunit NPxY motif.
study describes a role for talin in maintaining the homeostasis and survival of the regulatory T (Treg) cell pool
High Talin expression is associated with epithelial to mesenchymal transition in mammary gland.
FAK sustained the active integrin conformation by maintaining talin association with Rab11 endosomes in a type I phosphatidylinositol phosphate kinase (PIPKIgamma)-dependent manner.
These findings show that talin and kindlin cooperatively activate integrins leading to fibronectin binding and adhesion.
Binding of vinculin to the R1-R3 region of the talin rod is important for focal adhesion stability.
Study suggests that phosphatidylinositol 4,5-bisphosphate can have an impact on integrin activation through interaction with talin and Arg995, in a manner which leads to a breakage of the Arg995-Asp723 salt bridge
Data indicate that talin mechanics are isoform specific so that expression of either talin-1 or talin-2 modulates extracellular rigidity sensing.
Mice engineered to express only talin1(L325R) in myeloid cells were protected from renal ischemia-reperfusion injury.
Conformational activation of talin by PREL-1 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.
suggest that Tln1-mediated Itgbeta1b plays a crucial role in maintaining cardiac sarcomeric Z-disks and endothelial/endocardial cell integrity in zebrafish
CD90 (Thy1) is a novel interactor of talin 1 in effector cells of autoimmune equine uveitis.
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.
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