Recombinant Mouse Troponin I, Cardiac Muscle (TNNI3) Protein (His-SUMO)

Name: Recombinant Mouse Troponin I, Cardiac Muscle (TNNI3) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-02669P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Mouse Troponin I, Cardiac Muscle (TNNI3) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P48787
Target Symbol	TNNI3
Synonyms	Tnni3; Troponin I; cardiac muscle; Cardiac troponin I
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	ADESSDAAGEPQPAPAPVRRRSSANYRAYATEPHAKKKSKISASRKLQLKTLMLQIAKQEMEREAEERRGEKGRVLRTRCQPLELDGLGFEELQDLCRQLHARVDKVDEERYDVEAKVTKNITEIADLTQKIYDLRGKFKRPTLRRVRISADAMMQALLGTRAKESLDLRAHLKQVKKEDIEKENREVGDWRKNIDALSGMEGRKKKFEG
Expression Range	2-211aa
Protein Length	Full Length of Mature Protein
Mol. Weight	40.1kDa
Research Area	Signal Transduction
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 I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity.
Protein Families	Troponin I family
Database References	KEGG: mmu:21954 STRING: 10090.ENSMUSP00000096458 UniGene: PMID: 29544221 Hyperphosphorylation of this serine199 in cTnI C terminus impacts heart function by depressing diastolic function at baseline and limiting systolic reserve under physiological stresses. Paradoxically, it preserves heart function after ischemia/reperfusion injury, potentially by decreasing proteolysis of cTnI. PMID: 28899987 The contributions of cardiac myosin binding protein C and troponin I phosphorylation to beta-adrenergic enhancement of in vivo cardiac function PMID: 26635197 The difference in myosin regulatory light chain phosphorylation between the ventricles of R21C(+/+) in cardiac troponin I mice likely contributes to observed differences in contractile force and the lower tension monitored in the LV of HCM mice PMID: 25961037 troponin I phosphorylation specifically alters the Ca(2+) sensitivity of isometric tension and the time course of relaxation in cardiac muscle myofibrils PMID: 25418306 Combined troponin I Ser-150 and Ser-23/24 phosphorylation sustains thin filament Ca(2+) sensitivity playing an adaptive role to preserve contraction during acidic ischemia. PMID: 24657721 these results indicate that the inability to enhance myofilament relaxation through cTnI phosphorylation predisposes the heart to abnormal diastolic function, reduced accessibility of cardiac reserves, dysautonomia, and hypertrophy. PMID: 24973218 Dominant negative TnI-TnT interface mutation decreases the binding affinity of cTnI for TnT, causes early ventricular remodeling, and blunts the beta-adrenergic response of cardiac myocytes. PMID: 24898585 R193H and R205H mutation increase the binding affinity of Troponin I for Troponin T and Troponin C. PMID: 24326031 Conclude that dilated cardiomyopathy-causing mutations in thin filament proteins abolish the relationship between myofilament Ca(2+) sensitivity and troponin I phosphorylation by PKA. PMID: 23539503 The pattern of cTnI post-translational modification depends on sex and hypertrophic cardiomyopathy genotype. PMID: 23352598 A new functional and pathological role of amino acid modifications in the N-terminal acidic domain of cardiac TnI has been found that is modified by phosphorylations at TnI(S23/S24). PMID: 22940544 Data show that cardiac TnI gene transition and the alternatively spliced cardiac TnT isoform switching occur in postnatal pulmonary vein. PMID: 23176202 Conclude that cTnI phosphorylation by AMPK may represent a novel mechanism of regulation of cardiac function. PMID: 22456184 Generation and functional characterization of knock-in mice harboring the cardiac troponin I-R21C mutation associated with hypertrophic cardiomyopathy. PMID: 22086914 Data suggest that AMPK emerges as a possibly important regulator of cardiac and skeletal contractility via phosphorylation of a preferred site adjacent to the inhibitory loop of the thin filament protein TnI. PMID: 21416543 Loss of troponin I leads to myofibril hypersensitivity to Ca(2+) causing impaired relaxation in restrictive cardiomyopathy. PMID: 20580639 the functional effect of cTnI mutation and its potential value in compensating for the cTnT abnormality PMID: 20551314 Ca(2+) binding to thin filaments reconstituted with either cTnI(wild-type) or pseudo-phosphorylated cTnI(S23D/S24D), cTnI(T144E), and cTnI(S23D/S24D/T144E) was determined. PMID: 20164197 Studies indicate that that immunization of genetically susceptible mice with troponin I but not troponin T induced a robust autoimmune response leading to marked inflammation and fibrosis in the myocardium. PMID: 19446498 calcium induces an extended conformation of the inhibitory region of troponin I in cardiac muscle troponin PMID: 11724531 regulation of myocyte twitch kinetics by beta-stimulation and by endothelin-1 was altered in myocytes containing mutant cTnI PMID: 11934831 PKC-mediated phosphorylation of Ser(43) and Ser(45) of cTnI plays an important role in regulating force development in the intact myocardium PMID: 12003851 Troponin I serines 43/45 and regulation of cardiac myofilament function. PMID: 12181153 demonstration of novel site specificity of effects of protein kinase C phosphorylation on function and emphasize the complexity of modulation of the actin-myosin interaction by specific changes in the thin filament PMID: 12551921 the relationship between sarcomere length and myofilament lattice spacing in troponin I transgenic mice was markedly shifted downward to an overall decreased myofilament lattice spacing following protein kinase a treatment. PMID: 12562915 A primary role of PKC phosphorylation of cTnI may be to reduce the requirements of the contractile apparatus for both Ca2+ and ATP, thereby promoting efficient ATP utilisation during contraction. PMID: 12923217 autoantibodies to cTnI induce heart dysfunction and dilatation by chronic stimulation of Ca2+ influx in cardiomyocytes PMID: 14595408 PKC-dependent phosphorylation of TnI has important role in the modulation of cardiac function under basal as well as augmented states PMID: 14726296 cTnI has a pivotal role in the positive inotropic response of the murine heart to beta-adrenergic stimulation. PMID: 14966306 protein kinase C phosphorylation of cardiac troponin I plays a dominant role in depressing contractility PMID: 15507454 In conclusion, these data (alpha-chloralose-urethane) demonstrate that alpha-adrenergic-mediated force reduction is mediated through troponin I protein kinase C phosphorylation PMID: 15579573 removal of the N-terminal extension of cTnI enhances cardiac function by increasing the rate of myocardial relaxation and lowering left ventricular end diastolic pressure to facilitate ventricular filling PMID: 15611140 phosphorylation is driven by p90RSK PMID: 15840586 The Ca2+ binding properties of various assemblies of the regulatory components that contain one of the cardiomyopathy-related mutant cTnI. PMID: 16531415 Abnormal TnI phosphorylation observed in cardiac failure may explain exacerbated relaxation delay in response to increased afterload and contribute to blunted chronotropic reserve. PMID: 16936010 The cTnI-G203S mutation disrupts interactions with partner proteins, and results in intracellular Ca2+ dysregulation early in life, suggesting a pathogenic role in development of familial hypertrophic cardiomyopathy. PMID: 16950368 TnI deficiency impairs left ventricular relaxation, which leads to diastolic heart failure. PMID: 17526646 cTnI-Cre mice have delayed onset of Cre activity during early heart development PMID: 17540338 key role of cTnI in myocyte relaxation PMID: 17615373 The primary effect of protein kinase A phosphorylation of cardiac troponin I is reduced Ca(2+) sensitivity of force, whereas phosphorylation of cardiac myosin-binding protein C accelerates the kinetics of force development. PMID: 17641226 Changes in Ca(2+) affinity also support the idea that the equilibrium between states of actin-tropomyosin-troponin was shifted to the inactive state by mutations that mimic troponin I phosphorylation. PMID: 17872964 Thr144 in cardiac TnI modulates cardiac myofilament length-dependent activation. PMID: 17975107 Lys184 deletion in troponin I impairs relaxation kinetics and induces hypercontractility in murine cardiac myofibrils. PMID: 18096573 Simultaneous defects in MHC7 & TnI accelerate onset & progression of familial hypertrophic cardiomyopathy. Compared with single-mutant models, double-mutant mice develop severe disease & premature death, progressing directly to a dilated phenotype. PMID: 18362229 Impaired relaxation is the main manifestation in transgenic mice expressing a restrictive cardiomyopathy mutation, R193H, in cardiac TnI. PMID: 18408133 Removal of the N-terminal extension of cardiac troponin I as a functional compensation for impaired myocardial beta-adrenergic signaling PMID: 18815135 Transfer of troponin I-specific T cells can induce inflammation and fibrosis in wild-type mice, leading to deterioration of contractile function. Two sequence motifs of cTnI that induce inflammation and fibrosis in myocardium are characterized. PMID: 18955666 These results indicate that YY1 is a novel regulator of fetal TnI transcription in the heart. PMID: 19013134 the nNOS-PMCA4b complex regulates contractility via cAMP and phosphorylation of both PLB and cTnI. PMID: 19278978

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

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.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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