Recombinant Proteins

p53
LBP
CEA
HLA
TCL
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NPM
MAF
Bax
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TPM1 Human

Tropomyosin-1 Human Recombinant

Recombinant human TPM1, expressed in E. coli, is a single, non-glycosylated polypeptide chain. This protein consists of 304 amino acids, with a sequence spanning from amino acid positions 1 to 284, resulting in a molecular mass of 35 kDa. However, it's important to note that the apparent molecular weight on SDS-PAGE may be higher. The recombinant TPM1 protein is engineered with a 20 amino acid His Tag fused to its N-terminus. Purification is achieved through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT18914
Source
Escherichia Coli.
Appearance
The product is a clear solution that has been sterilized by filtration.

TPM2 Human

Tropomyosin-2 Human Recombinant

Produced in E. coli, TPM2 is a single, non-glycosylated polypeptide chain consisting of 304 amino acids (1-284a.a.) with a molecular mass of 35.1 kDa. Note that the molecular weight on SDS-PAGE may appear higher. This TPM2 protein is fused to a 20 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18999
Source
Escherichia Coli.
Appearance
Clear, sterile-filtered solution.

TPM3 Human

Tropomyosin-3 Human Recombinant

This product consists of the human TPM3 protein, specifically amino acids 1 to 248. It has a His-tag attached to its N-terminus for purification purposes. Produced in E. coli, this recombinant protein is not glycosylated and has a molecular weight of 31.6 kDa. It is provided as a clear solution at a concentration of 0.5mg/ml.
Shipped with Ice Packs
Cat. No.
BT19087
Source
Escherichia Coli.
Appearance
A clear, sterile-filtered solution.

TPM4 Human

Tropomyosin-4 Human Recombinant

Produced in E. coli, TPM4 is a single, non-glycosylated polypeptide chain consisting of 268 amino acids (specifically, amino acids 1 to 248) and has a molecular weight of 30.7 kDa. The protein features a 20 amino acid His-tag fused to its N-terminus and undergoes purification through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT19180
Source
Escherichia Coli.
Appearance
The product is a sterile, filtered solution that appears colorless.
Definition and Classification

Tropomyosin is a two-stranded alpha-helical, coiled-coil protein found in many animal and fungal cells . It is a critical component of the actin cytoskeleton, playing a vital role in muscle contraction and stabilization of the cytoskeleton . Tropomyosins are categorized into two main groups: muscle tropomyosin isoforms and nonmuscle tropomyosin isoforms . Muscle isoforms regulate interactions between actin and myosin in muscle sarcomeres, while nonmuscle isoforms function in various cellular pathways .

Biological Properties

Tropomyosin is expressed in smooth and striated muscle tissues, including the heart, blood vessels, respiratory system, and digestive system . It is also found in nonmuscle cells, where it regulates the actin cytoskeleton . Tropomyosin isoforms exhibit tissue-specific expression patterns, with different isoforms present in various organs and body systems . For example, TPM3 gene expression can be detected in skeletal muscle, endothelial cells, and neurons .

Biological Functions

Tropomyosin’s primary function is to regulate muscle contraction by controlling the interaction between actin and myosin . It also plays a role in stabilizing the cytoskeleton in nonmuscle cells . Tropomyosin is involved in immune responses and pathogen recognition by modulating the actin cytoskeleton, which is crucial for cell motility and phagocytosis .

Modes of Action

Tropomyosin binds along the length of actin filaments, blocking myosin-binding sites in the absence of a nerve impulse . Upon calcium ion release, tropomyosin undergoes a conformational change, exposing the myosin-binding sites and allowing muscle contraction . Tropomyosin interacts with various actin-binding proteins, including troponin, caldesmon, and gelsolin, to regulate actin filament stability and function .

Regulatory Mechanisms

The expression and activity of tropomyosin are regulated through transcriptional and post-translational mechanisms . Alternative splicing of tropomyosin genes generates multiple isoforms with distinct functions . Post-translational modifications, such as phosphorylation, also play a role in modulating tropomyosin’s interaction with actin and other binding partners .

Applications

Tropomyosin has several applications in biomedical research, including its use as a biomarker for various cancers . It is also studied for its role in muscle diseases and as a potential therapeutic target for conditions involving cytoskeletal dysfunction . Tropomyosin’s involvement in actin dynamics makes it a valuable tool for understanding cell motility and morphology .

Role in the Life Cycle

Tropomyosin plays a crucial role throughout the life cycle, from development to aging and disease . During development, tropomyosin isoforms contribute to the formation and function of muscle tissues . In aging, changes in tropomyosin expression and function can lead to muscle weakness and other age-related conditions . Tropomyosin is also implicated in various diseases, including congenital myopathies and cancer .

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