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TMOD1 encodes a member of the tropomodulin family. Additionally we are shipping Tropomodulin 1 Antibodies (64) and Tropomodulin 1 Kits (1) and many more products for this protein.
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The mutation reduced binding affinity for both Lmod2 (show LMOD2 Proteins) and Tmod1. The effect of the K15N mutation on Tpm1.1 binding to Lmod2 (show LMOD2 Proteins) and Tmod1 provides a molecular rationale for the development of familial dilated cardiomyopathies .
Study highlighted a novel TMOD1-mediated link between NF-kappaB (show NFKB1 Proteins) activation and MMP13 (show MMP13 Proteins) induction, which accounts in part for the NF-kappaB (show NFKB1 Proteins)-dependent malignant phenotype of TNBC.
Tmod1 and Tmod3 (show TMOD3 Proteins) showed somewhat different tropomyosin (show TPM2 Proteins)-binding site utilization.
The structures and biochemical analysis of structure-inspired mutants showed that one Tmod molecule interacts with three actin subunits at the pointed end, while also contacting two tropomyosin (show TPM2 Proteins) molecules on each side of the filament.
Tropomyosin (show TPM2 Proteins) requires an intact N-terminal coiled coil to interact with this protein
levels of TM1 (show TPM2 Proteins), TM2 (show TPM2 Proteins) and TM3 (show TPM1 Proteins) are reduced in human transitional cell carcinoma cells, but significantly upregulated by inhibition of the mitogen-activated protein kinase (show MAPK1 Proteins)-signaling pathway
The N-terminal "KRK ring" may participate in balancing electrostatic force with hydrophobic interaction in dimerization of TM and its binding to E-Tmod.
study identifies several amino acid residues on Tmod-1 that are important for its interaction with TM5 (a nonmuscle TM isoform)
TMOD1 expression was upregulated significantly (p<0.05) in OSCC.
RNAi depletion of Tmod1 from either wild-type or Tmod4 (show TMOD4 Proteins)(-/-) muscle fibers leads to thin filament elongation by approximately 15%.
The C-terminal extension of Lmod2 (show LMOD2 Proteins) and C terminal of Tmod1 are sufficient to produce a filament nucleator.
Calpain-mediated proteolysis of tropomodulin isoforms TMOD1 and TMOD4 (show TMOD4 Proteins) leads to thin filament elongation in dystrophic skeletal muscle.
Role of Tmod1 protein's leucine rich repeat domain in the formation of neurite-like processes
Tmod1 is involved in a functional synergy critical for regulating lens fiber cell geometry, transparency, and mechanical stiffness.
Tropomodulin 1 constrains fiber cell geometry during elongation and maturation in the lens cortex.
The Tmod1 deletion caused Tmod3 to leave its SR compartment, leading to mislocalization and destabilization of the Tmod3-gamma(cyto)-actin-sAnk1.5 complex.
Tmod1-null mice display a mild anemia with features resembling hereditary spherocytic elliptocytosis.
Erythrocyte tropomodulin isoforms with and without the N-terminal actin-binding domain.
This gene encodes a member of the tropomodulin family. The encoded protein is an actin-capping protein that regulates tropomyosin by binding to its N-terminus, inhibiting depolymerization and elongation of the pointed end of actin filaments and thereby influencing the structure of the erythrocyte membrane skeleton. Multiple transcript variants encoding the same protein have been found for this gene.
, tropomodulin 1
, erythrocyte tropomodulin