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TMOD1 encodes a member of the tropomodulin family. Additionally we are shipping Tropomodulin 1 Proteins (10) and Tropomodulin 1 Kits (1) and many more products for this protein.
Showing 10 out of 61 products:
Human Polyclonal Tropomodulin 1 Primary Antibody for EIA, WB - ABIN955335
Kong, Kedes: Leucine 135 of tropomodulin-1 regulates its association with tropomyosin, its cellular localization, and the integrity of sarcomeres. in The Journal of biological chemistry 2006
Show all 5 references for ABIN955335
Human Polyclonal Tropomodulin 1 Primary Antibody for IF, WB - ABIN521003
Kan-o, Takeya, Taniguchi, Tanoue, Tominaga, Sumimoto: Expression and subcellular localization of mammalian formin Fhod3 in the embryonic and adult heart. in PLoS ONE 2012
The mutation reduced binding affinity for both Lmod2 (show LMOD2 Antibodies) and Tmod1. The effect of the K15N mutation on Tpm1.1 binding to Lmod2 (show LMOD2 Antibodies) 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 Antibodies) activation and MMP13 (show MMP13 Antibodies) induction, which accounts in part for the NF-kappaB (show NFKB1 Antibodies)-dependent malignant phenotype of TNBC.
Tmod1 and Tmod3 (show TMOD3 Antibodies) showed somewhat different tropomyosin (show TPM2 Antibodies)-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 Antibodies) molecules on each side of the filament.
Tropomyosin (show TPM2 Antibodies) requires an intact N-terminal coiled coil to interact with this protein
levels of TM1 (show TPM2 Antibodies), TM2 (show TPM2 Antibodies) and TM3 (show TPM1 Antibodies) are reduced in human transitional cell carcinoma cells, but significantly upregulated by inhibition of the mitogen-activated protein kinase (show MAPK1 Antibodies)-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)
RNAi depletion of Tmod1 from either wild-type or Tmod4 (show TMOD4 Antibodies)(-/-) muscle fibers leads to thin filament elongation by approximately 15%.
The C-terminal extension of Lmod2 (show LMOD2 Antibodies) and C terminal of Tmod1 are sufficient to produce a filament nucleator.
Calpain-mediated proteolysis of tropomodulin isoforms TMOD1 and TMOD4 (show TMOD4 Antibodies) 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.
Tmod1 is a novel regulator of skeletal muscle physiology.
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