Recombinant Proteins

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LBP
CEA
HLA
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MAF
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TNNI3 Human, (1-210)

Cardiac Troponin-I Human Recombinant (1-210 a.a.)

Recombinant Human TNNI3, expressed in E. coli, is a single, non-glycosylated polypeptide chain. This protein spans 233 amino acids, encompassing residues 1-210 of the TNNI3 sequence, with an additional 23 amino acid His-tag fused at the N-terminus. It possesses a molecular weight of 26.4 kDa and is purified to homogeneity using proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT17243
Source
Escherichia Coli.
Appearance
The product is a clear, colorless liquid solution that has been sterilized by filtration.

TNNI3 Human, His

Cardiac Troponin-I Human Recombinant, His Tag

Recombinant Human TNNI3 protein, expressed in E. coli, is a full-length protein encompassing 260 amino acids. A 6-His tag is fused at the C-terminus, resulting in a protein that migrates as a 27 kDa band on SDS-PAGE. The protein has been purified using a proprietary chromatographic technique.
Shipped with Ice Packs
Cat. No.
BT17342
Source
Escherichia Coli.
Appearance
Clear, sterile-filtered solution.

Troponin C-I-T Complex

Cardiac Troponin C-I-T Complex Human

This product consists of Human Cardiac Troponin C-I-T Complex Protein. It is produced in human heart tissue and has a molecular mass of approximately 75kDa.

Shipped with Ice Packs
Cat. No.
BT17944
Source

Human cardiac tissue.

Appearance

This product appears as a sterile filtered solution that is brown in color.

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 with a molar ratio of cTnC:cTnI:cTnT of 1:1:1. Its molecular weight is approximately 90 kDa. This complex is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18039
Source
Escherichia Coli.
Appearance
Sterile filtered, colorless liquid formulation.

Troponin-C Human

Cardiac Troponin-C Human Recombinant

Recombinant Human Cardiac Troponin-C, produced in E. coli, is a non-glycosylated polypeptide chain with 181 amino acids (1-161) and a molecular weight of 20.5 kDa. It consists of a single chain and is fused to a 20 amino acid His-tag at the N-terminus. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18109
Source
E.coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

Troponin-C Protein

Cardiac Troponin-C Human

Human Troponin-C, derived from human cardiac tissue, has a molecular mass of 18kDa. The purification process involves ion-exchange and affinity chromatography.
Shipped with Ice Packs
Cat. No.
BT18199
Source

Human cardiac tissue

Appearance
A sterile, filtered solution that is colorless.

Troponin-C2 Human

Troponin-C2 Human Recombinant

Recombinant human Troponin-C2 produced in E. coli is a single, non-glycosylated polypeptide chain of 160 amino acids with a molecular mass of 18.1 kDa. The recombinant human Troponin-C2 protein is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18256
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

TNNI2 Human, His

Troponin I Type 2 Human Recombinant, His Tag

Recombinant human TNNI2 protein, expressed in E. coli, is available as a single polypeptide chain. This protein consists of 202 amino acids, comprising residues 1-182 of the native TNNI2 sequence, along with a 20 amino acid His-tag fused at the N-terminus. It has a molecular mass of 23.5 kDa and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT16973
Source
E.coli.
Appearance
Clear, colorless solution, sterile-filtered.

TNNI3 Human

Cardiac Troponin I Human Recombinant

Recombinant Human TNNI3, produced in E.Coli, is a single, non-glycosylated polypeptide chain consisting of 210 amino acids. With a molecular mass of 24,016 Daltons, it is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT17081
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless liquid.

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.
Shipped with Ice Packs
Cat. No.
BT17168
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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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