Recombinant Rat Tropomyosin alpha-1 chain (Tpm1)

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

Tpm1

Uniprot NO.

P04692

Species

Rattus norvegicus (Rat)

Source

Yeast

Expression Region

1-284

Target Protein Sequence

MDAIKKKMQM LKLDKENALD RAEQAEADKK AAEDRSKQLE DELVSLQKKL KGTEDELDKY SEALKDAQEK LELAEKKATD AEADVASLNR RIQLVEEELD RAQERLATAL QKLEEAEKAA DESERGMKVI ESRAQKDEEK MEIQEIQLKE AKHIAEDADR KYEEVARKLV IIESDLERAE ERAELSEGKC AELEEELKTV TNNLKSLEAQ AEKYSQKEDK YEEEIKVLSD KLKEAETRAE FAERSVTKLE KSIDDLEDEL YAQKLKYKAI SEELDHALND MTSI
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 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

Store at -20°C, for extended storage, conserve at -20°C or -80°C.

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.

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)

Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments.

Gene References into Functions

Transmission of stability information through the N-domain of tropomyosin is interrupted by a stabilizing mutation (A109L) in the hydrophobic core of the stability control region (residues 97-118). PMID:24362038
the link between flexibility of TM and its function in ejecting hearts. PMID:23609439
analysis of the pattern of of evolutionarily conserved basic and acidic residues that constitutes the binding interface of actin-tropomyosin PMID:23420843
The evolutionarily conserved residues are important for actomyosin regulation, a universal function of Tm that has a common structural basis and mechanism. PMID:23091026
troponin C (cTnC) and tropomyosin (cTm) are not only present in myofilaments of ventricular cardiomyocytes in culture but are also within their nuclei PMID:22364878
TPM1 may play an important role in the occurrence and development of liver fibrosis. PMID:22433308
The results were consistent with a mechanism in which the alpha-tropomyosin-actin interaction cooperatively affects actin to result in the generation of greater force and velocity. PMID:22041451
Data show that dual expression of two CM mutants, tropomyosin mutant A63V and cardiac troponin mutant R146G, were shown to additively slow myocyte relaxation beyond either mutant studied in isolation. PMID:20161772
A splicing silencer that regulates smooth muscle specific alternative splicing is active in multiple cell types. PMID:12177296
The stability and energetics of the tropomyosin coiled coil are important for actin affinity. PMID:14640678
analysis of tropomyosin bending and binding sites for actin PMID:16365313
Tm affects the conformation of actin so as to increase the area of hydrophobic interaction between actin and myosin molecules PMID:16980359
Results report the solution NMR structure of an overlap complex formed of model tropomyosin peptides. PMID:16999976
generic (interface instability) and specific periodic surface residues are essential for function PMID:18052203
The data suggest that end-to-end interactions of adjacent Tm molecules are strengthened when Tm is phosphorylated. PMID:18985725
A nonsense exon in the Tpm1 gene is silenced by hnRNP H and F PMID:19037011