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Recombinant Rabbit Tropomyosin alpha-1 chain (TPM1)

Recombinant Rabbit 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.

P58772

Species

Oryctolagus cuniculus (Rabbit)

Source

Mammalian cell

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

The results indicate that cross-linking significantly affects properties of Tpm and actin-myosin interaction and can explain, at least partly, the role of the interchain disulfide cross-linking of cardiac Tpm in human heart diseases. PMID:27856252
altered TM-actin contacts destabilized the thin filament and affected the actin-myosin interactions PMID:27480605
analysis of the thin filament associated with the R167H and K168E substitutions in tropomyosin Tpm1.1 PMID:27956029
We propose that TR100 acts to compromise the integrity of Tpm cables rather than prevent overlap complex formation. Our data suggests that TR100 is incorporated into the growing actin-Tpm co-polymer given that its effects cannot be observed on pre-formed Tpm3.1/actin filaments PMID:26804624
Maximal Ca(2+) activated force was the same in alphaalphaTm versus betabetaTm myofibrils, but betabetaTm myofibrils showed a marked slowing of relaxation and an impairment of regulation under resting conditions PMID:25380572
Tmod1 and Tmod3 showed somewhat different tropomyosin-binding site utilization. PMID:24922351
Thermal denaturation of rabbit cardiac alpha,alpha-tropomyosin is monitored at neutral pH and compared to shark tropomyosin, showing that amino acid substitutions predicted to be unfavorable in one temperature regime are desirable in another. PMID:21707054
The rotational motion of a spin label covalently bound to the side chain of a cysteine genetically incorporated into rabbit skeletal muscle tropomyosin, was measured. PMID:21575577
a computational search assessing electrostatic interactions for multiple azimuthal locations, z-positions, and pseudo-rotations of tropomyosin on F-actin was performed. PMID:21320445