Recombinant Proteins

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TNNT1 Human

Slow Skeletal Troponin T Human Recombinant

TNNT1 Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 278 amino acids and having a molecular mass of 32948 Dalton.
Shipped with Ice Packs
Cat. No.
BT17452
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

TNNT2 Human

Cardiac Muscle Troponin T Recombinant Human

Recombinant Human Cardiac Muscle Troponin T, produced in E. coli, is a single, non-glycosylated polypeptide chain containing 297 amino acids with a molecular weight of 35.8 kDa. TNNT2 is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT17509
Source

Escherichia Coli.

Appearance
Sterile filtered colorless solution.

TNNT2 Human, His

Cardiac Muscle Troponin T Human Recombinant, His Tag

This product consists of a recombinant human TNNT2 protein produced in E. coli. It is a single, non-glycosylated polypeptide chain comprising 305 amino acids (specifically, amino acids 1-285). With a molecular weight of 36.4 kDa, the TNNT2 protein is fused to a 20 amino acid His Tag at the N-terminus. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT17602
Source
Escherichia Coli.
Appearance
The product is provided as a sterile, filtered solution that is colorless.

TNNT3 Human

Fast Skeletal Troponin T Human Recombinant

TNNT3 Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 261 amino acids and having a molecular mass of 30964 Dalton.
Shipped with Ice Packs
Cat. No.
BT17695
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

TnT Human

Cardiac Troponin T Human

This product consists of human cardiac troponin T, purified from human cardiac tissue. It has a molecular weight of roughly 35 kDa and is prepared through a multi-step process involving ion-exchange and affinity chromatography to ensure its purity.
Shipped with Ice Packs
Cat. No.
BT17781
Source
Human Cardiac Tissue.
Appearance
This product appears as a clear, colorless liquid solution that has been sterilized by filtration.

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 with a molecular weight of approximately 50 kDa. The molar ratio of cTnC to cTnI is 1:1. The purification process involves proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT17860
Source
Escherichia Coli.
Appearance
Sterile, colorless liquid formulation.

scIC2

Single Chain Cardiac Troponin I-C 2nd generation Recombinant

Recombinant Single Chain Cardiac Troponin I-C 2nd generation, produced in E. coli, is a single, non-glycosylated polypeptide chain (aa28-110-Linker-cTnC) with a molecular weight of 30 kDa. It's important to note that 1 mg of scIC2 corresponds to 0.82 mg of full-length human cardiac TNI in molar terms. The purification of scIC2 is achieved through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT16574
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless liquid formulation.

TNC Rabbit

Skeletal Muscle Troponin-C Rabbit

Rabbit Skeletal Muscle Troponin-C is a single polypeptide chain that has undergone glycosylation and possesses a molecular mass of 18kDa. It constitutes one of the three subunits forming the Troponin complex, an integral part of the thin filaments found in striated muscles. The purification of Skeletal muscle Troponin-C involves a multi-step process employing a combination of ion-exchange and affinity chromatography techniques.
Shipped with Ice Packs
Cat. No.
BT16644
Source
Rabbit Skeletal Muscle.
Appearance
The solution is colorless and has been sterilized through filtration.

TNNI1 Human

Troponin I Type 1 Human Recombinant

Recombinant human TNNI1, produced in E. coli, is a single polypeptide chain that lacks glycosylation. It consists of 207 amino acids, spanning from position 1 to 187, and possesses a molecular weight of 23.8 kDa. A 20-amino acid His-tag is fused to the N-terminus of TNNI1 to facilitate purification using specialized chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT16766
Source
Escherichia Coli.
Appearance
A clear solution that has been sterilized through filtration.

TNNI2 Human

Troponin I Type 2 Human Recombinant

Skeletal isoforms of Troponin I are potential markers for acute and chronic skeletal muscle injuries. Two forms of Troponin I, slow (21.6 kDa) and fast (21.2 kDa) skeletal, are present in skeletal muscles. Fast Skeletal Troponin I exhibits a migration pattern corresponding to approximately 26.5kDa on SDS-PAGE.
Shipped with Ice Packs
Cat. No.
BT16862
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless liquid formulation.
Definition and Classification

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 .

Biological Properties

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 .

Biological Functions

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.

Modes of Action

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 .

Regulatory Mechanisms

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 .

Applications

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 .

Role in the Life Cycle

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 .

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