Recombinant Mouse Troponin T, Cardiac Muscle (TNNT2) Protein (His&Myc)

Name: Recombinant Mouse Troponin T, Cardiac Muscle (TNNT2) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-07361P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Mouse Troponin T, Cardiac Muscle (TNNT2) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P50752
Target Symbol	TNNT2
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	SDAEEVVEEYEEEQEEEDWSEEEEDEQEEAVEEEEAGGAEPEPEGEAETEEANVEEVGPDEEAKDAEEGPVEDTKPKPSRLFMPNLVPPKIPDGERVDFDDIHRKRVEKDLNELQTLIEAHFENRKKEEEELISLKDRIEKRRAERAEQQRIRNEREKERQNRLAEERARREEEENRRKAEDEARKKKALSNMMHFGGYIQKQAQTERKSGKRQTEREKKKKILAERRKALAIDHLNEDQLREKAKELWQSIHNLEAEKFDLQEKFKQQKYEINVLRNRINDNQKVSKTRGKAKVTGRWK
Expression Range	2-301aa
Protein Length	Full Length of Mature Protein
Mol. Weight	43.1 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 T is the tropomyosin-binding subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity.
Protein Families	Troponin T family
Database References	KEGG: mmu:21956 STRING: 10090.ENSMUSP00000137093 UniGene: PMID: 28419739 Hypertrophic cardiomyopathy pathophysiology is "mutation specific" in mice models carrying TNNT2 E163R and R92Q mutations. PMID: 28735292 TnTA30V mutation attenuated Ca(2+)-activated maximal tension and length-mediated cross-bridge recruitment against alpha-myosin heavy chain but augmented these parameters against beta-myosin heavy chain, suggesting divergent contractile phenotypes. PMID: 27769999 The shift from cTnT exon 5 inclusion to exclusion during development was delayed in the heart of Ts65Dn mice due to Dyrk1A overexpression. PMID: 27049307 for hypertrophic cardiomyopathy (HCM)-causing mutations in TnT, Ca(2+)-sensitisation together with uncoupling in vitro is the usual response and both factors may contribute to the HCM phenotype PMID: 27036851 cardiomyopathy mutation (R97L) in mouse cardiac troponin T has an effect on the muscle length-mediated recruitment of crossbridges and is modified divergently by alpha- and beta-myosin heavy chain PMID: 26792537 Data indicate that high-sensitivity troponin T (hs-TnT) levels are influenced by myocardial dysfunction/heart failure (HF) in acute exacerbation of chronic obstructive lung disease (AECOPD), but provide independent prognostic information. PMID: 26754170 cTnT elevation emerged as a strong, independent predictor of 30-day mortality and remained a modest, but significant, predictor throughout 2 years post transcatheter aortic valve implantation. PMID: 26896474 MBPC and troponin-I phosphorylation modulate myofilament length-dependent activation PMID: 26453301 Data indicate that the troponin T Tnnt2(MerCreMer/+) mouse model also provides a useful tool to trace myocardial lineage during development. PMID: 26010701 TnT mutation F72L leads to contractile changes that are linked to dilated cardiomyopathy in the presence of MYH6 and hypertrophic cardiomyopathy in the presence of MYH7. PMID: 26342069 TNT increases slightly during low flux-hemodialysis. High-flux hemodialysis eliminates the biomarker and can mask increases caused by cardiac disease. PMID: 25744196 Mice carrying the Delta160E or E163R mutations exhibit sarcomeric disruption. PMID: 24480310 Cardiac muscle activation blunted by a mutation to the regulatory component, troponin T. PMID: 23897817 Study is the first to show that the interplay between the N terminus of cTnT and the overlapping ends of contiguous Tm effectuates different states of Tm on the actin filament. PMID: 23748972 We conclude that the observed clinical severity of the cTnT Delta160E mutation is caused by a combination of direct sarcomeric disruption coupled to a profound dysregulation of Ca(2+) homeostasis PMID: 23434821 Report two distinct functional regions within the N-terminus of cTnT with divergent roles in mediating cardiac contractile activation. PMID: 23207592 findings provide new evidence to demonstrate that R92 mutation effects on cardiac contractile function and dynamics are influenced by myosin heavy chain isoform PMID: 22884844 role of N-terminal extension of cardiac troponin T in cardiac thin filament PMID: 23009843 results showed dominantly negative effects of the coexistence of fast skeletal muscle TnT and cardiac TnT on contractile kinetics absent the influence of extracellular matrix; a dilatative remodeling at the cellular level was observed, supporting a pathological significance PMID: 22538236 Data sugget that knockdown or downregulation of CYP2E1 might be a therapeutic strategy to control the development of dilated cardiomyopathy (DCM) after mutations of cTnT(R141W) or other factors. PMID: 22665122 Correlation of molecular and functional effects of mutations in cardiac troponin T linked to familial hypertrophic cardiomyopathy PMID: 22334656 Pak1-knockout hearts have reduced recovery of myocardial performance after global I/R injury concomitant with changes in troponin-T and MLC2 phosphorylation and protein association. PMID: 22037191 One major and two minor alternatively spliced isoforms of troponin T have been purified from wild-type healthy adult mouse heart. PMID: 21639091 TCDD represses the expression of the cardiac development-specific Nkx2.5 homeobox transcription factor, of cardiac troponin-T and of alpha- and beta-myosin heavy chains. PMID: 20130022 Results indicated a pathogenic mechanism in which the coexistence of functionally different cTnT variants in cardiac muscle reduces myocardial efficiency due to desynchronized thin filament activation. PMID: 20418479 Cardiomyopathy-causing deletion K210 in cardiac troponin T alters phosphorylation propensity of sarcomeric proteins. PMID: 20079745 Studies show that the rat Tnnt2-rtTA;TetO-Cre mice transgenic line a valuable genetic tool for analysis of spatiotemporal gene function and cardiomyocyte lineage tracing during developmental and postnatal period. PMID: 20014345 Identification of a functionally critical protein kinase C phosphorylation residue PMID: 12832403 Transgenic mouse models expressing a missense mutation (R92Q) or a splice donor site mutation (trunc) in the cardiac troponin T (cTnT) showed that hypertrophic signaling is differentially affected by distinct mutations in cTnT. PMID: 15466629 Changes in thin filament structure caused by single amino acid substitutions lead to differences in the biophysical properties of cTnT and alter cardiomyopathy pathogenesis. PMID: 16326803 The mu-calpain-mediated proteolytic modification of TnT may act as an acute mechanism to adjust muscle contractility under stress conditions. PMID: 16981728 the hypervariable NH2-terminal region modulates the conformation and function of the TnT core structure to fine-tune muscle contractility. PMID: 17260966 Independent FHC-relted Tnt mutations exhibit specific alterations in myocellular and calcium kinetics. PMID: 17490679 R-92L and R-92W mutations in the TM-binding domain of cardiac TnT alter thin filament structure and flexibility sufficiently to cause severe defects in both whole heart energetics and contractile performance PMID: 17526570 Transgenic mice expressing chicken TNNT3 and cTNT in myocardium showed ventricular dysfunction and chronic myocardial hypertrophy and degeneration. PMID: 17959729 Plasma troponin T was at a similar level in beta1(-/-), beta1(+/+) and beta1(-/-) BM mice treated with 30 min ischaemia and 3 h reperfusion. PMID: 18296493 Differential interactions among the sarcomeric proteins containing cTnT-Q92 or cTnT-W141 are responsible for the contrasting phenotypes of hypertrophic cardiomyopathy or dilated cardiomyopathy, respectively. PMID: 18349139 Data found that fTnT normally associated with fast twitch skeletal muscle were present at significant levels in the thoracic aorta, and that fTnT transcripts were expressed in the smooth muscle layer of mouse blood vessels of all sizes PMID: 18548613 Absence of one Tnnt2 allele leads to a mild deficit in transcript but not protein, leading to a normal cardiac phenotype. PMID: 18612386 These findings indicate cTnT plays a critical role in sarcomere assembly during myofibrillogenesis in the embryonic heart, and that the membrane excitation and intracellular Ca(2+) handling systems develop independently of the contractile system. PMID: 18671960 The direct repeat and overlapping Troponin T GATA site are critical for the expression level and cardiac specificity. PMID: 18951515 Data indicate that UT-B deletion caused the dynamic expression regulation of TNNT2 and ANP, and these proteins may provide new clues to investigate the molecular events involved in cardiac conduction. PMID: 19132680 peak releases of TnT or TnT fragments from decomposition of a large number of myofibrils in acute myocardial infarction may breach the cellular protection of proteolytic degradation PMID: 19395545 cTnT mutations in the TNT1 domain result in mutation-specific effects and a different temporal onset of altered myocellular mechanics, Ca(2+) kinetics, and Ca(2+) homeostasis; may contribute to clinical variability in familial hypertrophic cardiomyopathy PMID: 19502551 Results describe the functional effects of N-terminal deletion and phosphorylation in cardiac troponin T on Ca(2+) dependence of myofilament isometric force production, isometric ATPase rate, and thin filament sliding speed. PMID: 19586048

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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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