TNNI3 Human, (1-210)
Greater than 90.0% as determined by both SDS-PAGE.
Description
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.
Product Specs
Troponin I (TnI) is a protein integral to the troponin complex, which plays a crucial role in the regulation of striated muscle contraction. Within this complex, TnI functions as the inhibitory subunit, preventing the interaction between actin and myosin, thus facilitating muscle relaxation. The TNNI3 gene specifically encodes the cardiac isoform of TnI, and its expression is restricted to cardiac muscle tissues. Genetic alterations in the TNNI3 gene have been linked to familial hypertrophic cardiomyopathy type 7 (CMH7) and familial restrictive cardiomyopathy (RCM), underscoring its importance in maintaining normal heart function.
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.
The TNNI3 protein solution is provided at a concentration of 0.25mg/ml. The storage buffer consists of 30% glycerol, 20mM Tris-HCl (pH 7.5), 0.1M NaCl, 0.1mM PMSF, and 1mM DTT.
The purity of the TNNI3 protein is greater than 90.0%, as determined by SDS-PAGE analysis.
MGSSHHHHHH SSGLVPRGSH MGSMADGSSD AAREPRPAPA PIRRRSSNYR AYATEPHAKK KSKISASRKL QLKTLLLQIA KQELEREAEERRGEKGRALS TRCQPLELAG LGFAELQDLC RQLHARVDKV DEERYDIEAK VTKNITEIAD LTQKIFDLRG KFKRPTLRRV RISADAMMQALLGARAKESL DLRAHLKQVK KEDTEKENRE VGDWRKNIDA LSGMEGRKKK FES
Product Science Overview
Cardiac Troponin-I is a critical protein in the regulation of cardiac muscle contraction. It is part of the troponin complex, which includes Troponin T and Troponin C, and plays a pivotal role in the calcium-mediated regulation of muscle contraction. The specific form, Human Recombinant Cardiac Troponin-I (1-210 a.a.), is a truncated version of the full-length protein, expressed in Escherichia coli for research and diagnostic purposes.
Troponin-I binds to actin in thin myofilaments to hold the actin-tropomyosin complex in place, preventing myosin from binding to actin in relaxed muscle . This inhibition is crucial for muscle relaxation and contraction cycles. The recombinant form, spanning amino acids 1 to 210, retains the essential functional domains necessary for its inhibitory role.
The recombinant Human Cardiac Troponin-I (1-210 a.a.) is typically expressed in Escherichia coli. This bacterial expression system is favored due to its simplicity, cost-effectiveness, and ability to produce large quantities of protein. The protein is then purified to a high degree of purity (>90%) using techniques such as SDS-PAGE .
Cardiac Troponin-I is a highly specific biomarker for myocardial injury. Its levels in the blood rise significantly within a few hours of myocardial infarction, making it an essential tool in the diagnosis of acute coronary syndromes . The recombinant form is used in various assays to detect and quantify Troponin-I levels in clinical samples.
Recombinant Human Cardiac Troponin-I (1-210 a.a.) is widely used in research to study the molecular mechanisms of cardiac muscle contraction and regulation. It is also employed in the development and validation of diagnostic assays for cardiac biomarkers.
