Recombinant Mouse Troponin I, cardiac muscle (Tnni3)

In Stock
Code CSB-EP341785MO
Size US$306
Order now
Image
  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

Have Questions? Leave a Message or Start an on-line Chat

Product Details

Purity
Greater than 90% as determined by SDS-PAGE.
Target Names
Tnni3
Uniprot No.
Research Area
Signal Transduction
Alternative Names
Tnni3; Troponin I; cardiac muscle; Cardiac troponin I
Species
Mus musculus (Mouse)
Source
E.coli
Expression Region
2-211aa
Target Protein Sequence
ADESSDAAGEPQPAPAPVRRRSSANYRAYATEPHAKKKSKISASRKLQLKTLMLQIAKQEMEREAEERRGEKGRVLRTRCQPLELDGLGFEELQDLCRQLHARVDKVDEERYDVEAKVTKNITEIADLTQKIYDLRGKFKRPTLRRVRISADAMMQALLGTRAKESLDLRAHLKQVKKEDIEKENREVGDWRKNIDALSGMEGRKKKFEG
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
40.1kDa
Protein Length
Full Length of Mature Protein
Tag Info
N-terminal 6xHis-SUMO-tagged
Form
Liquid or Lyophilized powder
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.
Buffer
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution
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°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
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.
Lead Time
3-7 business days
Notes
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.
Description

Troponin I, cardiac muscle (Tnni3) CSB-EP341785MO is a recombinant mouse full-length of mature Tnni3 protein containing amino acid residues of 2-211. It is produced in the E.coli cells through procaryotic expression and fused with a 6xHis-SUMO-tag at the N-terminus. And it has high purity of up to 90% determined by SDS-PAGE. Its predicted molecular weight is 40.11 kDa, but the actual observed molecular mass (46 kDa)via SDS-PAGE analysis is slightly higher due to post-transcriptional modifications such as glycosylation. This recombinant Tnni3 protein is in-stock, allowing for continuous sourcing and no intermediate waiting period for protein preparation. This Tnni3 protein not only acts as an immunogen for antibody production but also finds uses in the studies of Tnni3-mediated signal transduction.

Tnni3 is the inhibitory subunit of the cardiac troponin (cTn) complex that is a sensor of the intracellular Ca2+ levels and modulates the interaction between the thick and thin filaments during muscle contraction. It mainly blocks the interaction between actin and myosin in the absence of Ca2+ and tightly regulated by phosphorylation.

Customer Reviews and Q&A

 Customer Reviews

There are currently no reviews for this product.

Submit a Review here

Target Background

Function
Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity.
Gene References into Functions
  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

Show More

Hide All

Protein Families
Troponin I family
Database Links
icon of phone
Call us
301-363-4651 (Available 9 a.m. to 5 p.m. CST from Monday to Friday)
icon of address
Address
7505 Fannin St., Ste 610, Room 322 (CUBIO Innovation Center), Houston, TX 77054, USA
icon of social media
Join us with

Subscribe newsletter

Leave a message

* To protect against spam, please pass the CAPTCHA test below.
CAPTCHA verification
© 2007-2024 CUSABIO TECHNOLOGY LLC All rights reserved. 鄂ICP备15011166号-1
Place an order now

I. Product details

*
*
*
*

II. Contact details

*
*

III. Ship To

*
*
*
*
*
*
*

IV. Bill To

*
*
*
*
*
*
*
*