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Recombinant Rat Troponin T, cardiac muscle (Tnnt2)

Recombinant Rat Troponin T, cardiac muscle (Tnnt2)

Baculovirus
Mammalian cell

Code
MSDS	MSDS Datasheet
Size	Pls inquire
Source
Conjugate
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Product Details
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Target Background

Product Details

Purity

>85% (SDS-PAGE)

Target Names

Tnnt2

Uniprot NO.

P50753

Species

Rattus norvegicus (Rat)

Source

Yeast

Expression Region

2-299

Target Protein Sequence

SDAEEEVVE YEEEQEEEDW SEEEEDEQEE AVEEEDGEAE PDPEGEAEAE EDKAEEVGPD EEARDAEDGP VEDSKPKPSR LFMPNLVPPK IPDGERVDFD DIHRKRMEKD LNELQTLIEA HFENRKKEEE ELISLKDRIE KRRAERAEQQ RIRNEREKER QNRLAEERAR REEEENRRKA EDEARKKKAL SNMMHFGGYI QKAQTERKSG KRQTEREKKK KILAERRKVL AIDHLNEDQL REKAKELWQS IHNLEAEKFD LQEKFKQQKY EINVLRNRIN DNQKVSKTRG KAKVTGRWK
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.

Protein Length

Full Length of Mature Protein

Tag Info

N-terminal His-tagged/Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Storage

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.

Shelf Life

Notes

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

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Target Background

Function(From Uniprot)

Troponin T is the tropomyosin-binding subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity.

Gene References into Functions

Replacement of the functionally corresponding N-terminal end portion of rat fast skeletal cardiac muscle (RfsTnT) into cardiac muscle troponin T (RcTnT), the observed functional differences associate with a sequence variation. PMID:23357173
L48Q cTnC reduced crossbridge dependence of thin filament activation in cardiac muscle and changes in Ca(2+) sensitivity of force in response to changes in sarcomere length are at least partially dependent on properties of thin filament troponin. PMID:22865385
cTnC, cTnI, cTnT and cTm are not only present in myofilaments of ventricular cardiomyocytes in culture but are also within their nuclei; significantly, these four proteins appear between days 3 and 5 in both myofilaments and nuclei PMID:22364878
Early single cTnT measurement correlates with infarct size in rats, and a cutoff value of 5.1 mug/l provides good sensitivity and specificity to predict congestive heart failure with secondary pulmonary hypertension. PMID:20537565
The time course of cTnT elevation was temporally associated with evidence of increased lipid peroxidation in the rat heart. PMID:20711602
a novel role for cTnT as a dual-specificity sarcomeric A-kinase anchoring protein PMID:21056973
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
The mu-calpain-mediated proteolytic modification of TnT may act as an acute mechanism to adjust muscle contractility under stress conditions. PMID:16981728
Overexpression of heat shock protein 27 protects against ischaemia/reperfusion-induced cardiac dysfunction via stabilization of troponin I and T. PMID:18397962
Mdetabolic inhibition of cardiomyocytes induces a parallel release of intact Tnnt3 and its degradation products, starting only after onset of irreversible cardiomyocyte damage. PMID:18721805
Study demonstrate profound energetic alterations in DEL-TNT hearts, supporting the notion that inefficient cellular ATP utilization contributes to the pathogenesis of HCM. PMID:19189074