Recombinant Human TNNC1 Protein (N-6His)
Beta LifeScience
SKU/CAT #: BL-1643NP

BL-1643NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Recombinant Human TNNC1 Protein (N-6His)
Beta LifeScience
SKU/CAT #: BL-1643NP
Collections: Other recombinant proteins, Recombinant proteins
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.
Product Overview
Description | Recombinant Human Slow Skeletal And Cardiac Muscles is produced by our E.coli expression system and the target gene encoding Met1-Glu161 is expressed with a 6His tag at the N-terminus. |
Accession | P63316 |
Synonym | CMH7; TNNC1; TNNI3; Troponin I |
Gene Background | Troponin I, also known as TNI, is a 24 kDa component of a protein complex on striated muscle thin filaments.Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments. Troponin I inhibits the calcium-dependent muscle contraction mediated by Troponins C and T. The expression of cardiac Troponin I (TNNI3) is restricted to cardiac muscle, while TNNI1 and TNNI2 (encoded by distinct genes) are expressed in skeletal muscle. Mutations of cardiac Troponin I are associated with heriditary cardiomyopathy. Human cardiac Troponin I shares 93% amino acid sequence identity with mouse and rat cardiac Troponin I. |
Molecular Mass | 19.8 KDa |
Apmol Mass | 17-20 KDa, reducing conditions |
Formulation | Supplied as a 0.2 μm filtered solution of 20mM Tris-HCl, 100mM NaCl, 1mM DTT, 10% Glycerol, pH 8.0. |
Endotoxin | Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test. |
Purity | Greater than 95% as determined by reducing SDS-PAGE. (QC verified) |
Biological Activity | Not tested |
Reconstitution | |
Storage | Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles. |
Shipping | The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below. |
Usage | For Research Use Only |
Target Details
Target Function | Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments. |
Protein Families | Troponin C family |
Database References | |
Associated Diseases | Cardiomyopathy, dilated 1Z (CMD1Z); Cardiomyopathy, familial hypertrophic 13 (CMH13) |
Gene Functions References
- Rationally engineered TnC constructs corrected the abnormal Ca(2+) sensitivities of the thin filament, reconstituted actomyosin ATPase activity PMID: 22511780
- Molecular effects of cardiac troponin C mutations present in hypertrophic cardiomyopathy on calcium sensitivity and myofilament activation have been reported. PMID: 27133568
- Study shows that over-expression of MFAP5 and TNNC1 is correlated with cervical lymph node metastasis (CLNM), metastasis relapse-free survival and overall survival. These results propose that MFAP5 and TNNC1 may be potential markers for predicting occult cervical lymphatic metastasis and prognosis of oral tongue carcinoma. PMID: 27713166
- Our results (i) confirm that genetic backgrounds of hypertrophic cardiomyopathy and restrictive cardiomyopathy overlap and (ii) indicate that TNNC1 is a likely novel gene for autosomal recessive restrictive cardiomyopathy. PMID: 27604170
- Data suggest that modulation of structural dynamics far from the regulatory Ca2+-binding site is the underlying molecular mechanism for many TNNC1 mutations in patients with hypertrophic cardiomyopathies or familial hypertrophic cardiomyopathies; many mutations affect balance between open and closed conformations; troponin I switch peptide [TnI(SW)] switch peptide binds to TNNC1 and stabilizes the open TNNC1 conformation. PMID: 28533433
- Data suggest that mutations in troponin C (TnC) found in patients with hypertrophic cardiomyopathy (A8V, C84Y, and D145E) stabilize the active state of regulated actin (the actin-tropomyosin-troponin complex) to various extents; at a saturating Ca2+ concentration, all TnC mutants investigated increase the level of active M state compared to the wild type. PMID: 28530094
- There was no difference in the test characteristics of the HEART Pathway whether using cTnI or hs-cTnI, with both achieving 100% sensitivity and NPV. Use of hs-cTnT with the HEART Pathway was associated with one missed major adverse cardiac events. PMID: 28087371
- contractility is constantly above normal in hearts made hypertrophic by TnC with the A8V mutation PMID: 26976709
- We used nuclear magnetic resonance and circular dichroism to solve the structure and characterize the backbone dynamics and stability of the regulatory domain of cTnC with the L29Q mutation. PMID: 26341255
- conclusive evidence that TNNC1 is an uncommon but definitive HCM-susceptibility gene PMID: 26304555
- Troponin C (TnC) and the N-terminal helix of Troponin I (TnI N-helix), which occurs in vivo during muscle contraction. PMID: 26111167
- FAK/CREB/TNNC1 has a role in mediating the effect of stromal MFAP5 on ovarian cancer metastatic potential PMID: 25277212
- Mutations in cTnC have been associated with hypertrophic or dilated cardiomyopathy.[review] PMID: 26232335
- Data suggest that mutation A162H in switch region of troponin I induces transitory curved conformation and promotes contraction of troponin I bound to regulatory domain of troponin C; this is countered by residue E164 to ensure proper relaxation. PMID: 25996354
- in vitro characterisation of six cardiac Troponin C mutations causing hypertrophic and dilated cardiomyopathies (Review) PMID: 24744096
- The conformational dynamics of N-terminal lobe of TnC plays an important role in the regulation of cardiac muscle contraction. PMID: 25101951
- Data indicate that domain positioning impacts the effective concentration of cardiac isoform of troponin I (cTnI) presented to cardiac troponin C (cTnC). PMID: 25246568
- Toponin I, T, and C play crucial roles in muscle activity, connecting changes in intracellular Ca2+ concentration with generation of contraction. [review] PMID: 24490734
- Central helix point mutations decreased affinity of Ca2+ saturated cardiac TNC for TnI128-180. PMID: 24650606
- The structure of cardiac troponin C regulatory domain with bound Cd2+ reveals a closed conformation and unique ion coordination. PMID: 23633581
- Calcium induced regulation of skeletal troponin--computational insights from molecular dynamics simulations. PMID: 23554884
- calcium binding to the regulatory site of human cardiac troponin C PMID: 23111626
- Significance of troponin dynamics for Ca2+-mediated regulation of contraction and inherited cardiomyopathy. PMID: 23066014
- a novel mutation in the TNNC1 gene is associated with HCM pathogenesis and may predispose to the pathogenesis of a fatal arrhythmogenic subtype of HCM PMID: 22815480
- The study examines TNC for its ability of binding Ca2+ and furthermore determines the molecular contributions to Ca2+ binding kinetics. PMID: 22329450
- The L48Q mutation enhanced binding of both Ca(2+) and troponin I to cardiac troponin C. PMID: 22591429
- The disease-related protein modifications alter Ca(2+) binding by influencing both the association and dissociation rates of thin filament Ca(2+) exchange. PMID: 22675533
- Cardiomyopathy-linked TnC mutations affect the response of reconstituted thin filaments to calcium upon cardiac troponin (Tn)I phosphorylation. PMID: 22489623
- Functional characterization of TNNC1 rare variants identified in dilated cardiomyopathy. PMID: 21832052
- strong cross-bridges potentiate the Ca(2+)-sensitizing effect of hypertrophic cardiomyopathy-cTnC mutants on the myofilament PMID: 21056975
- analysis of order and disorder in troponin C, T and I PMID: 20889975
- A region in cTnC associated with increased Ca(2+) sensitivity in skinned fibers was identified, an the F27W reporter mutation affected Ca(2+) sensitivity, maximal force, and ATPase activation of some mutants. PMID: 20566645
- plasma levels are associated with degree of vascular obstruction in patients with pulmonary embolism PMID: 19492165
- Calcium binding properties of the carboxy terminal-domain sites might be important for the proper regulatory function of cardiac troponin C. PMID: 20459070
- Four private protein-altering variants were identified in troponin C type 1 in 4 probands. PMID: 20215591
- After acute myocardial infarction, cTnI is present in serum as the ternary cTnT-cTnI-TnC (TIC) complex and binary cTnI-TnC (IC) complex. PMID: 20378771
- the dilated cardiomyopathy troponin C mutation lowers contractile force by reducing strong myosin-actin binding PMID: 20371872
- The intrinsic properties of TnC and its interactions with other contractile proteins play a crucial role in modulating the binding of calcium to TnC in increasingly complex biochemical systems. PMID: 20128626
- cardiac troponin switches between alternative sets of intramolecular interactions, similar to previous intermediate resolution x-ray data of skeletal muscle troponin PMID: 19920153
- Structure and dynamics of the C-domain of human cardiac troponin C in complex with the inhibitory region of human cardiac troponin I. PMID: 12732641
- Data suggest that activation of cardiac myofilaments is tightly coupled to the open state of the N-domain of cardiac troponin C, and that pathological effects of phosphorylation are influenced by mutations in cardiac troponin I. PMID: 15147183
- CTnI mutations mainly alter myocardial performance via changes in the Ca2+ -sensitivity of force development and in some cases alter the muscle relaxation kinetics. Review. PMID: 15524171
- C helix moves away from the D helix in a distinct Ca(2+)-dependent manner, while the B helix does not. PMID: 15628883
- Results describe the in situ structure of human cardiac troponin C. PMID: 15808858
- The crystal structure of troponin suggests that the Ca2+-binding to the regulatory TnC site displaces the N-terminal portion of TnI from actin/tropomyosin, thereby altering mobility/flexibility of the troponin/tropomyosin strand on the actin filament. PMID: 16157639
- Spin dipole-dipole interaction showed that in reconstituted muscle fibers both skeletal and cardiac TnC undergo Ca2+-induced structural change that is thought to be TnIreg movement. PMID: 16157641
- Results imply a hindered transduction of the protein kinase A phosphorylation signal from cardiac troponin I to troponin C. PMID: 16302972
- the mutation Gly159Asp causes a significant decrease in the rate of force production and a change in the relationship between the rate of force production and generated force in muscle PMID: 17021793
- in the presence of phosphorylated cTnI, cTnC-G159D specifically blunted phosphorylation induced decrease in Ca(2+)-sensitive tension development without altering cross-bridge cycling in cardiac myofilament PMID: 17446435
- Suggest that TnC Ca(2+) binding properties modulate the rate of cardiac muscle contraction at submaximal levels of Ca(2+) activation. PMID: 17693547