Recombinant Proteins
Product List
TNNI3 Human, (1-210)
Cardiac Troponin-I Human Recombinant (1-210 a.a.)
TNNI3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 233 amino acids (1-210 a.a) and having a molecular mass of 26.4 kDa.
TNNI3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
TNNI3 Human, His
Cardiac Troponin-I Human Recombinant, His Tag
Recombinant Human TNNI3 protein produced in E.Coli is a full length protein containing a total of 260 amino acids and fused to a 6 His Tag at C-terminus, migrating as a 27kDa band on SDS-PAGE.
Purified by proprietary chromatographic technique.
TNNT1 Human
Slow Skeletal Troponin T Human Recombinant
TNNT1 Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 278 a.a and having a molecular mass of 32948 Dalton.
Sterile Filtered White lyophilized (freeze-dried) powder.
TNNT2 Human
Cardiac Muscle Troponin T Recombinant Human
Cardiac Muscle Troponin T Human Recombinant produced in E.Coli is a single, non- glycosylated polypeptide chain containing 297 amino acids and having a molecular mass of 35.8kDa.
TNNT2 is purified by proprietary chromatographic techniques.
Escherichia Coli.
Sterile filtered colorless solution.
TNNT2 Human, His
Cardiac Muscle Troponin T Human Recombinant, His Tag
TNNT3 Human
Fast Skeletal Troponin T Human Recombinant
TNNT3 Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 261 a.a and having a molecular mass of 30964 Dalton.
Sterile Filtered White lyophilized (freeze-dried) powder.
TnT Human
Cardiac Troponin T Human
The Cardiac troponin-T is purified using a combination of ion-exchange and affinity chromatography steps.
Troponin C-I Human
Cardiac Troponin C-I Complex Human Recombinant
Recombinant Human Cardiac Troponin C-I complex produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of approximately 50kDa. The Molar ratio on cTnC to cTnI is 1:1.
The Cardiac Troponin C-I is purified by proprietary chromatographic techniques.
Troponin C-I-T Complex
Cardiac Troponin C-I-T Complex Human
Human Cardiac Troponin C-I-T Complex Protein produced in Human heart tissue having a molecular mass of approximately 75kDa.
Human cardiac tissue.
Sterile Filtered brown solution.
Troponin C-I-T Human
Cardiac Troponin C-I-T Complex Human Recombinant
Recombinant Human Cardiac Troponin C-I-T complex produced in E.Coli is a single, non-glycosylated, polypeptide chain having the Molar ratio on cTnC to cTnI to cTnT of 1:1:1. Mw is approximately 90kDa.
The Cardiac Troponin C-I-T complex is purified by proprietary chromatographic techniques
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 .
