protein

TPM1 Protein, Human (His)

HY-P74502

5 μg;10 μg;50 μg;100 μg

53;90;250;420 USD

TPM1 Protein, Human (His)

proteins

E. coli

5 μg;10 μg;50 μg;100 μg

53;90;250;420 USD

TPM1 encodes tropomyosin, a key actin-binding component in muscle contraction and cytoskeletal structure. It contains α-helical chains that form a coiled-coil structure that stabilizes actin filaments. TPM1 Protein, Human (His) is the recombinant human-derived TPM1 protein, expressed by E. coli , with N-His labeled tag. The total length of TPM1 Protein, Human (His) is 284 a.a., with molecular weight of ~35 kDa.

Human

TPM1 Protein, a member of the tropomyosin family, belongs to a highly conserved group of actin-binding proteins crucial for the contractile system in striated and smooth muscles, as well as the cytoskeleton of non-muscle cells. Comprising two alpha-helical chains arranged as a coiled-coil, tropomyosin polymerizes along the grooves of actin filaments, providing structural stability. This protein, a key alpha helical chain, serves as the predominant tropomyosin in striated muscle, where it collaborates with the troponin complex to regulate the calcium-dependent interaction between actin and myosin during muscle contraction. In smooth muscle and non-muscle cells, alternative splicing yields various isoforms. Mutations in the TPM1 gene are associated with type 3 familial hypertrophic cardiomyopathy and dilated cardiomyopathy 1Y. Moreover, TPM1 displays biased expression, with notable levels observed in the heart and prostate, along with nine other tissues, underscoring its importance in diverse physiological contexts.

Tropomyosin alpha-1 chain; Tropomyosin-1; TPM1; C15orf13; TMSA

Greater than 90% as determined by reducing SDS-PAGE.

Lyophilized from a 0.2 μm filtered solution of PBS, 10% Glycerol, pH 7.4.

Room temperature in continental US; may vary elsewhere.