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Mouse cardiac troponin Ⅰ(cTn-Ⅰ) ELISA kit

  • 中文名稱:
    小鼠心肌肌鈣蛋白(cTn-Ⅰ)酶聯免疫試劑盒
  • 貨號:
    CSB-E08421m
  • 規格:
    96T/48T
  • 價格:
    ¥3800/¥2500
  • 其他:

產品詳情

  • 產品描述:
    小鼠心肌肌鈣蛋白(cTn-Ⅰ)酶聯免疫試劑盒(CSB-E08421m)為雙抗夾心法ELISA試劑盒,定量檢測血清、血漿樣本中的TNNI3含量。TNNI3是一個重要靶點。它是心肌肌鈣蛋白I的編碼基因,在心肌收縮調控中起關鍵作用。研究圍繞其結構與功能,探索突變對心肌功能影響及疾病關聯機制,有望為心肌病等心臟疾病的診斷、治療提供新方向和靶點。試劑盒檢測范圍為15.6 pg/mL-1000 pg/mL,適用于多種科研場景,包括心血管疾病機制研究、心肌損傷動物模型驗證、心臟保護藥物療效評估以及環境毒理或藥理學實驗中心肌損傷程度的動態監測。為研究小鼠心臟病理生理變化、篩選心肌保護化合物提供可靠工具,廣泛應用于基礎醫學、藥理學及毒理學等領域的科研探索。本品僅用于科研,不用于臨床診斷,產品具體參數及操作步驟詳見產品說明書。
  • 別名:
    Tnni3 ELISA Kit; Troponin I ELISA Kit; cardiac muscle ELISA Kit; Cardiac troponin I ELISA Kit
  • 縮寫:
  • Uniprot No.:
  • 種屬:
    Mus musculus (Mouse)
  • 樣本類型:
    serum, plasma
  • 檢測范圍:
    15.6 pg/mL-1000 pg/mL
  • 靈敏度:
    3.9 pg/mL
  • 反應時間:
    1-5h
  • 樣本體積:
    50-100ul
  • 檢測波長:
    450 nm
  • 研究領域:
    Others
  • 測定原理:
    quantitative
  • 測定方法:
    Sandwich
  • 精密度:
    Intra-assay Precision (Precision within an assay): CV%<8%      
    Three samples of known concentration were tested twenty times on one plate to assess.  
    Inter-assay Precision (Precision between assays): CV%<10%      
    Three samples of known concentration were tested in twenty assays to assess.    
                 
  • 線性度:
    To assess the linearity of the assay, samples were spiked with high concentrations of mouse cTn-Ⅰ in various matrices and diluted with the Sample Diluent to produce samples with values within the dynamic range of the assay.
     SampleSerum(n=4)
    1:1Average %91
    Range %88-95
    1:2Average %101
    Range %97-105
    1:4Average %96
    Range %92-100
    1:8Average %86
    Range %82-88
  • 回收率:
    The recovery of mouse cTn-Ⅰ spiked to levels throughout the range of the assay in various matrices was evaluated. Samples were diluted prior to assay as directed in the Sample Preparation section.
    Sample Type Average % Recovery Range  
    Serum (n=5) 90 87-95  
    EDTA plasma (n=4) 92 88-96  
                 
                 
  • 標準曲線:
    These standard curves are provided for demonstration only. A standard curve should be generated for each set of samples assayed.
    pg/ml OD1 OD2 Average Corrected  
    1000 2.399 2.356 2.378 2.221  
    500 1.610 1.687 1.649 1.492  
    250 0.955 0.997 0.976 0.819  
    125 0.563 0.568 0.566 0.409  
    62.5 0.375 0.358 0.367 0.210  
    31.2 0.241 0.236 0.239 0.082  
    15.6 0.165 0.178 0.172 0.015  
    0 0.154 0.159 0.157    
  • 數據處理:
  • 貨期:
    3-5 working days

引用文獻

產品評價

平均分:
5.0分 - 1 個評價

樣品類型:血清

樣品信息:小鼠

稀釋比:其他 5倍

產品評價: 我用CSBE08421m檢測心梗后心衰小鼠ctnI值,產品效果穩定

By 陶老師

靶點詳情

  • 功能:
    Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity.
  • 基因功能參考文獻:
    1. Pim-1 is a novel kinase that phosphorylates cTnI primarily at Ser23/24 and Ser150 in cardiomyocytes, which in turn may modulate myofilament function under a variety of physiological and pathophysiological conditions. PMID: 29544221
    2. 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
    3. The contributions of cardiac myosin binding protein C and troponin I phosphorylation to beta-adrenergic enhancement of in vivo cardiac function PMID: 26635197
    4. 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
    5. troponin I phosphorylation specifically alters the Ca(2+) sensitivity of isometric tension and the time course of relaxation in cardiac muscle myofibrils PMID: 25418306
    6. 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
    7. 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
    8. 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
    9. R193H and R205H mutation increase the binding affinity of Troponin I for Troponin T and Troponin C. PMID: 24326031
    10. 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
    11. The pattern of cTnI post-translational modification depends on sex and hypertrophic cardiomyopathy genotype. PMID: 23352598
    12. 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
    13. Data show that cardiac TnI gene transition and the alternatively spliced cardiac TnT isoform switching occur in postnatal pulmonary vein. PMID: 23176202
    14. Conclude that cTnI phosphorylation by AMPK may represent a novel mechanism of regulation of cardiac function. PMID: 22456184
    15. Generation and functional characterization of knock-in mice harboring the cardiac troponin I-R21C mutation associated with hypertrophic cardiomyopathy. PMID: 22086914
    16. 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
    17. Loss of troponin I leads to myofibril hypersensitivity to Ca(2+) causing impaired relaxation in restrictive cardiomyopathy. PMID: 20580639
    18. the functional effect of cTnI mutation and its potential value in compensating for the cTnT abnormality PMID: 20551314
    19. 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
    20. 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
    21. calcium induces an extended conformation of the inhibitory region of troponin I in cardiac muscle troponin PMID: 11724531
    22. regulation of myocyte twitch kinetics by beta-stimulation and by endothelin-1 was altered in myocytes containing mutant cTnI PMID: 11934831
    23. 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
    24. Troponin I serines 43/45 and regulation of cardiac myofilament function. PMID: 12181153
    25. 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
    26. 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
    27. 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
    28. autoantibodies to cTnI induce heart dysfunction and dilatation by chronic stimulation of Ca2+ influx in cardiomyocytes PMID: 14595408
    29. PKC-dependent phosphorylation of TnI has important role in the modulation of cardiac function under basal as well as augmented states PMID: 14726296
    30. cTnI has a pivotal role in the positive inotropic response of the murine heart to beta-adrenergic stimulation. PMID: 14966306
    31. protein kinase C phosphorylation of cardiac troponin I plays a dominant role in depressing contractility PMID: 15507454
    32. 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
    33. 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
    34. phosphorylation is driven by p90RSK PMID: 15840586
    35. The Ca2+ binding properties of various assemblies of the regulatory components that contain one of the cardiomyopathy-related mutant cTnI. PMID: 16531415
    36. 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
    37. 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
    38. TnI deficiency impairs left ventricular relaxation, which leads to diastolic heart failure. PMID: 17526646
    39. cTnI-Cre mice have delayed onset of Cre activity during early heart development PMID: 17540338
    40. key role of cTnI in myocyte relaxation PMID: 17615373
    41. 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
    42. 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
    43. Thr144 in cardiac TnI modulates cardiac myofilament length-dependent activation. PMID: 17975107
    44. Lys184 deletion in troponin I impairs relaxation kinetics and induces hypercontractility in murine cardiac myofibrils. PMID: 18096573
    45. 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
    46. Impaired relaxation is the main manifestation in transgenic mice expressing a restrictive cardiomyopathy mutation, R193H, in cardiac TnI. PMID: 18408133
    47. Removal of the N-terminal extension of cardiac troponin I as a functional compensation for impaired myocardial beta-adrenergic signaling PMID: 18815135
    48. 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
    49. These results indicate that YY1 is a novel regulator of fetal TnI transcription in the heart. PMID: 19013134
    50. the nNOS-PMCA4b complex regulates contractility via cAMP and phosphorylation of both PLB and cTnI. PMID: 19278978

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  • 蛋白家族:
    Troponin I family
  • 數據庫鏈接:


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