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ICAM5 encodes a cytoskeletal protein that is concentrated in areas of cell-substratum and cell-cell contacts. Additionally we are shipping ICAM5 Antibodies (52) and ICAM5 Kits (20) and many more products for this protein.
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These findings suggested that Talin-1 (show TLN1 Proteins) protein was significantly upregulated in PCa (show FLVCR1 Proteins) tissues compared with that of BPH (show GLI3 Proteins) tissue and Talin-1 (show TLN1 Proteins) expression was an independent predictor for lymph node metastasis and biochemical recurrence of PCa (show FLVCR1 Proteins).
Serum talin-1 (show TLN1 Proteins) had 97.7% sensitivity.
Both TLN-1 (show TLN1 Proteins) and TLN-2 levels correlate with tumorigenicity in human HCC (show FAM126A Proteins), indicating that these molecules constitute important molecular targets for the diagnosis and/or treatment of hepatocellular carcinoma .
TLN1 (show TLN1 Proteins) 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 (show TLN1 Proteins) 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 (show TLN1 Proteins) is associated with significantly poorer OS and poorer DMFS in NPC (show NPC1 Proteins) and depletion of Talin-1 (show TLN1 Proteins) expression inhibited NPC (show NPC1 Proteins) cell migration and invasion. Talin-1 (show TLN1 Proteins) may serve as novel prognostic biomarker in NPC (show NPC1 Proteins).
The activation of vinculin (show VCL Proteins) by stretched talin induces a positive feedback that reinforces the actin-talin-vinculin (show VCL Proteins) association.
Data (including data from molecular dynamic simulations) suggest specific interactions between glycoprotein GPIIb/GPIIIa (show ITGB3 Proteins) complex transmembrane/C-terminal domains and talin-1 (show TLN1 Proteins) 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]
These findings show that talin and kindlin cooperatively activate integrins leading to fibronectin (show FN1 Proteins) binding and adhesion.
Data show that estradiol or bisphenol A decreased expression of luteinizing hormone beta (Lhb (show LHB Proteins)), follicle stimulating hormone beta (Fshb (show FSHB Proteins)), and intracellular adhesion molecule (show NCAM1 Proteins)-5 (Icam5) in females but only decreased expression of Icam5 in males.
Binding of vinculin (show VCL Proteins) 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 modulates extracellular rigidity sensing.
Conformational activation of talin by PREL-1 (show APBB1IP Proteins) 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.
This study revealed a similar expression of ICAM-5 in dendritic elements at P14 (show PCOLCE Proteins) and P28 (show GSTO1 Proteins); however, an increased prevalence of ICAM-5 was noted in dendritic protrusions at P28 (show GSTO1 Proteins) in the MMP-9 (show MMP9 Proteins) null animals
reduction of talin-beta3 integrin (show ITGB3 Proteins) binding affinity results in decelerated alphaIIbbeta3 integrin activation and protection from arterial thrombosis without pathological bleeding
Results suggest that the interaction between ICAM-5 and beta1 integrins is important in formation of functional synapses.
As talin engages F-actin, force exerted on the R2R3 helical bundles disrupts RIAM (show APBB1IP Proteins) binding and exposes the vinculin (show VCL Proteins) binding sites, which recruit vinculin (show VCL Proteins) to stabilize the complex.
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.
intercellular adhesion molecule 5
, intercellular adhesion molecule 3