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)
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
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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
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

  1. Rationally engineered TnC constructs corrected the abnormal Ca(2+) sensitivities of the thin filament, reconstituted actomyosin ATPase activity PMID: 22511780
  2. Molecular effects of cardiac troponin C mutations present in hypertrophic cardiomyopathy on calcium sensitivity and myofilament activation have been reported. PMID: 27133568
  3. 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
  4. 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
  5. 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
  6. 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
  7. 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
  8. contractility is constantly above normal in hearts made hypertrophic by TnC with the A8V mutation PMID: 26976709
  9. 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
  10. conclusive evidence that TNNC1 is an uncommon but definitive HCM-susceptibility gene PMID: 26304555
  11. Troponin C (TnC) and the N-terminal helix of Troponin I (TnI N-helix), which occurs in vivo during muscle contraction. PMID: 26111167
  12. FAK/CREB/TNNC1 has a role in mediating the effect of stromal MFAP5 on ovarian cancer metastatic potential PMID: 25277212
  13. Mutations in cTnC have been associated with hypertrophic or dilated cardiomyopathy.[review] PMID: 26232335
  14. 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
  15. in vitro characterisation of six cardiac Troponin C mutations causing hypertrophic and dilated cardiomyopathies (Review) PMID: 24744096
  16. The conformational dynamics of N-terminal lobe of TnC plays an important role in the regulation of cardiac muscle contraction. PMID: 25101951
  17. Data indicate that domain positioning impacts the effective concentration of cardiac isoform of troponin I (cTnI) presented to cardiac troponin C (cTnC). PMID: 25246568
  18. Toponin I, T, and C play crucial roles in muscle activity, connecting changes in intracellular Ca2+ concentration with generation of contraction. [review] PMID: 24490734
  19. Central helix point mutations decreased affinity of Ca2+ saturated cardiac TNC for TnI128-180. PMID: 24650606
  20. The structure of cardiac troponin C regulatory domain with bound Cd2+ reveals a closed conformation and unique ion coordination. PMID: 23633581
  21. Calcium induced regulation of skeletal troponin--computational insights from molecular dynamics simulations. PMID: 23554884
  22. calcium binding to the regulatory site of human cardiac troponin C PMID: 23111626
  23. Significance of troponin dynamics for Ca2+-mediated regulation of contraction and inherited cardiomyopathy. PMID: 23066014
  24. 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
  25. The study examines TNC for its ability of binding Ca2+ and furthermore determines the molecular contributions to Ca2+ binding kinetics. PMID: 22329450
  26. The L48Q mutation enhanced binding of both Ca(2+) and troponin I to cardiac troponin C. PMID: 22591429
  27. 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
  28. Cardiomyopathy-linked TnC mutations affect the response of reconstituted thin filaments to calcium upon cardiac troponin (Tn)I phosphorylation. PMID: 22489623
  29. Functional characterization of TNNC1 rare variants identified in dilated cardiomyopathy. PMID: 21832052
  30. strong cross-bridges potentiate the Ca(2+)-sensitizing effect of hypertrophic cardiomyopathy-cTnC mutants on the myofilament PMID: 21056975
  31. analysis of order and disorder in troponin C, T and I PMID: 20889975
  32. 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
  33. plasma levels are associated with degree of vascular obstruction in patients with pulmonary embolism PMID: 19492165
  34. Calcium binding properties of the carboxy terminal-domain sites might be important for the proper regulatory function of cardiac troponin C. PMID: 20459070
  35. Four private protein-altering variants were identified in troponin C type 1 in 4 probands. PMID: 20215591
  36. 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
  37. the dilated cardiomyopathy troponin C mutation lowers contractile force by reducing strong myosin-actin binding PMID: 20371872
  38. 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
  39. cardiac troponin switches between alternative sets of intramolecular interactions, similar to previous intermediate resolution x-ray data of skeletal muscle troponin PMID: 19920153
  40. 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
  41. 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
  42. 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
  43. C helix moves away from the D helix in a distinct Ca(2+)-dependent manner, while the B helix does not. PMID: 15628883
  44. Results describe the in situ structure of human cardiac troponin C. PMID: 15808858
  45. 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
  46. 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
  47. Results imply a hindered transduction of the protein kinase A phosphorylation signal from cardiac troponin I to troponin C. PMID: 16302972
  48. 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
  49. 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
  50. Suggest that TnC Ca(2+) binding properties modulate the rate of cardiac muscle contraction at submaximal levels of Ca(2+) activation. PMID: 17693547


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Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

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