Recombinant Human Troponin C, slow skeletal and cardiac muscles (TNNC1)

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中文名稱：

人TNNC1重組蛋白
貨號：

CSB-EP024009HU
說明書：

MSDS Datasheet
規格：

￥1536
圖片：
(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
其他：

產品詳情
產品評價
相關產品
靶點詳情

產品詳情

純度：

Greater than 90% as determined by SDS-PAGE.
基因名：

TNNC1
Uniprot No.：

P63316
種屬：

Homo sapiens (Human)
蛋白長度：

Full Length
來源：

E.coli
分子量：

21.0 kDa
表達區域：

1-161aa
氨基酸序列

MDDIYKAAVEQLTEEQKNEFKAAFDIFVLGAEDGCISTKELGKVMRMLGQNPTPEELQEMIDEVDEDGSGTVDFDEFLVMMVRCMKDDSKGKSEEELSDLFRMFDKNADGYIDLDELKIMLQATGETITEDDIEELMKDGDKNNDGRIDYDEFLEFMKGVE
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.
蛋白標簽：

N-terminal 6xHis-tagged
產品提供形式：

Liquid or Lyophilized powder Warning: in_array() expects parameter 2 to be array, null given in /www/web/cusabio_cn/public_html/caches/caches_template/default/content/show_product_protein.php on line 662
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
緩沖液：

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose.
復溶：

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
儲存條件：

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
保質期：

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
貨期：

3-7 business days
注意事項：

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA：

Please contact us to get it.

產品評價

靶點詳情

功能：

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.
基因功能參考文獻：
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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相關疾病：

Cardiomyopathy, dilated 1Z (CMD1Z); Cardiomyopathy, familial hypertrophic 13 (CMH13)
蛋白家族：

Troponin C family
數據庫鏈接：

HGNC: 11943

OMIM: 191040

KEGG: hsa:7134

STRING: 9606.ENSP00000232975

UniGene: Hs.118845