Recombinant Human Troponin C, Slow Skeletal And Cardiac Muscles (TNNC1) Protein (His)

Name: Recombinant Human Troponin C, Slow Skeletal And Cardiac Muscles (TNNC1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-00870P
Price: 349.0 USD
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Size

100ug

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Product Overview

Description	Recombinant Human Troponin C, Slow Skeletal And Cardiac Muscles (TNNC1) Protein (His) is produced by our Baculovirus expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P63316
Target Symbol	TNNC1
Species	Homo sapiens (Human)
Expression System	Baculovirus
Tag	C-6His
Target Protein Sequence	MDDIYKAAVEQLTEEQKNEFKAAFDIFVLGAEDGCISTKELGKVMRMLGQNPTPEELQEMIDEVDEDGSGTVDFDEFLVMMVRCMKDDSKGKSEEELSDLFRMFDKNADGYIDLDELKIMLQATGETITEDDIEELMKDGDKNNDGRIDYDEFLEFMKGVE
Expression Range	1-161aa
Protein Length	Full Length
Mol. Weight	19.5 kDa
Research Area	Cardiovascular
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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	HGNC: 11943 OMIM: 191040 KEGG: hsa:7134 STRING: 9606.ENSP00000232975 UniGene: Hs.118845
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

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