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TMOD1 encodes a member of the tropomodulin family. Additionally we are shipping Tropomodulin 1 Antibodies (67) and Tropomodulin 1 Proteins (10) and many more products for this protein.
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Tmod1 function in mouse and human erythroblasts, was investigated.
The mutation reduced binding affinity for both Lmod2 and Tmod1. The effect of the K15N mutation on Tpm1.1 binding to Lmod2 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 ELISA Kits) activation and MMP13 (show MMP13 ELISA Kits) induction, which accounts in part for the NF-kappaB (show NFKB1 ELISA Kits)-dependent malignant phenotype of TNBC.
Tmod1 and Tmod3 (show TMOD3 ELISA Kits) showed somewhat different tropomyosin (show TPM2 ELISA Kits)-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 ELISA Kits) molecules on each side of the filament.
Tropomyosin (show TPM2 ELISA Kits) requires an intact N-terminal coiled coil to interact with this protein
levels of TM1 (show TPM2 ELISA Kits), TM2 (show TPM2 ELISA Kits) and TM3 (show TPM1 ELISA Kits) are reduced in human transitional cell carcinoma cells, but significantly upregulated by inhibition of the mitogen-activated protein kinase (show MAPK1 ELISA Kits)-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)
distinct F-actin organizations are present in small protrusions versus large paddles. Formation and/or maintenance of large paddle domains depends on a beta2-spectrin-actin network stabilized by Tmod1. alpha-Actinin (show ACTN1 ELISA Kits)-crosslinked F-actin bundles are enhanced in absence of Tmod1, indicating altered cytoskeleton organization.
TMOD1 expression was upregulated significantly (p<0.05) in OSCC.
RNAi depletion of Tmod1 from either wild-type or Tmod4(-/-) muscle fibers leads to thin filament elongation by approximately 15%.
The C-terminal extension of Lmod2 and C terminal of Tmod1 are sufficient to produce a filament nucleator.
Calpain-mediated proteolysis of tropomodulin isoforms TMOD1 and TMOD4 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.
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