Recombinant Proteins
Product List
Troponin-C Human
Cardiac Troponin-C Human Recombinant
Cardiac Troponin-C Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 181 amino acids (1-161) and having a molecular mass of 20.5 kDa.
Cardiac Troponin-C is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Troponin-C Protein
Cardiac Troponin-C Human
Troponin-C Human produced from Human Cardiac Tissue, having a molecular mass of 18kDa.
The Troponin-C is purified using a combination of ion-exchange and affinity chromatography steps.
Human cardiac tissue
Troponin-C2 Human
Troponin-C2 Human Recombinant
Troponin-C2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain of 160 amino acids having a molecular mass of 18.1kDa. The Recombinant Human Troponin-C2 is purified by proprietary chromatographic techniques.
scIC2
Single Chain Cardiac Troponin I-C 2nd generation Recombinant
1mg of scIC2 is equivalent to 0.82mg of full length human cardiac TNI on a molar basis.
The scIC2 is purified by proprietary chromatographic techniques.
TNC Rabbit
Skeletal Muscle Troponin-C Rabbit
Troponin-C is one of three subunits that form the Troponin complex of striated muscle thin filaments.
Skeletal muscle Troponin-C is purified using a combination of ion-exchange and affinity chromatography steps.
TNNI1 Human
Troponin I Type 1 Human Recombinant
TNNI2 Human
Troponin I Type 2 Human Recombinant
TNNI2 Human, His
Troponin I Type 2 Human Recombinant, His Tag
TNNI3 Human
Cardiac Troponin I Human Recombinant
The TNNI3 is purified by proprietary chromatographic techniques.
TNNI3 Human Chimeric
Cardiac Troponin-I Chimeric Human Recombinant
TNNI3 Human Chimeric produced in E.Coli is a single, non-glycosylated polypeptide chain (28-110 a.a.) and having a molecular mass of 29072 Dalton.
Sterile Filtered White lyophilized (freeze-dried) powder.
Introduction
Troponin is a complex of three regulatory proteins—troponin C (TnC), troponin I (TnI), and troponin T (TnT)—that are integral to muscle contraction in skeletal and cardiac muscle . These proteins are not found in smooth muscle. Troponin C binds calcium ions, troponin I inhibits actin-myosin interactions, and troponin T binds the troponin complex to tropomyosin .
Key Biological Properties: Troponin is essential for the regulation of muscle contraction. It is involved in the calcium-mediated regulation of the actin-myosin interaction .
Expression Patterns: Troponin is expressed in both skeletal and cardiac muscles, but the specific isoforms differ between these muscle types . For example, cardiac troponin I (cTnI) is exclusive to cardiac muscle after birth .
Tissue Distribution: Troponin is distributed in the thin filaments of muscle tissue, specifically within the sarcomere, the basic unit of muscle fiber .
Primary Biological Functions: Troponin plays a crucial role in muscle contraction by regulating the interaction between actin and myosin filaments . It acts as a switch that is activated by calcium ions to initiate muscle contraction .
Role in Immune Responses and Pathogen Recognition: While troponin’s primary function is related to muscle contraction, it does not have a direct role in immune responses or pathogen recognition.
Mechanisms with Other Molecules and Cells: Troponin interacts with calcium ions and tropomyosin to regulate muscle contraction . When calcium binds to troponin C, it induces a conformational change that moves tropomyosin away from myosin-binding sites on actin, allowing muscle contraction to occur .
Binding Partners: Troponin binds to tropomyosin and actin in the muscle thin filaments .
Downstream Signaling Cascades: The binding of calcium to troponin C triggers a cascade of events that lead to muscle contraction, including the activation of myosin ATPase activity .
Transcriptional Regulation: The expression of troponin genes is regulated at the transcriptional level by various transcription factors that respond to developmental and physiological cues .
Post-Translational Modifications: Troponin undergoes several post-translational modifications, including phosphorylation, which can affect its function and the regulation of muscle contraction .
Biomedical Research: Troponin is extensively studied in the context of muscle physiology and cardiac function .
Diagnostic Tools: Cardiac-specific troponins (cTnI and cTnT) are widely used as biomarkers for diagnosing myocardial infarction and other cardiac injuries . Elevated levels of these troponins in the blood indicate cardiac muscle damage .
Therapeutic Strategies: Understanding troponin’s role in muscle contraction has led to the development of drugs that target troponin for treating heart failure and other cardiac conditions .
Development: During embryonic development, slow skeletal TnI is expressed in cardiac tissue but is replaced by cardiac TnI after birth .
Aging and Disease: Changes in troponin levels and function are associated with various cardiac diseases, including cardiomyopathies and myocardial infarction . Elevated troponin levels can also be observed in chronic diseases and are used as prognostic markers .
