| Product Name | TPM1, 1-284aa, Human |
|---|---|
| Description | TPM1 is a member of the tropomyosin family of highly conserved, widely distributed actin-binding proteins involved in the contractile system of striated and smooth muscles and the cytoskeleton of non-muscle cells. Tropomyosin is composed of two alpha-helical chains arranged as a coiled-coil. It is polymerized end to end along the two grooves of actin filaments and provides stability to the filaments. TPM1 is one type of alpha helical chain that forms the predominant tropomyosin of striated muscle, where it also functions in association with the troponin complex to regulate the calcium-dependent interaction of actin and myosin during muscle contraction. Recombinant human TPM1 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. |
| Synonyms | TPM1, CMD1Y, HTM-alpha, TMSA, Tropomyosin-1, Alpha-tropomyosin, Tropomyosin alpha-1 chain |
| Host | E. coli |
| Molecular Weight | 48.0 kDa(415aa), confirmed by MALDI-TOF |
| Amino Acid Sequence | MGSSHHHHHH SSGLVPRGSH MDAIKKKMQM LKLDKENALD RAEQAEADKK AAEDRSKQLE DELVSLQKKL KGTEDELDKY SEALKDAQEK LELAEKKATD AEADVASLNR RIQLVEEELD RAQERLATAL QKLEEAEKAA DESERGMKVI ESRAQKDEEK MEIQEIQLKE AKHIAEDADR KYEEVARKLV IIESDLERAE ERAELSEGQV RQLEEQLRIM DQTLKALMAA EDKYSQKEDR YEEEIKVLSD KLKEAETRAE FAERSVTKLE KSIDDLEDEL YAQKLKYKAI SEELDHALND MTSM |
| Tag | His-tag |
| Reactivity | Human |
| Applications | SDS-PAGE |
| Form | Liquid, in 20 mM Tris-HCl (pH 7.5) containing 10% Glycerol |
| Concentration | 1 mg/ml (determined by Bradford assay) |
| Purity | > 90% by SDS-PAGE |
| Storage | Can be stored at +4C short term (1-2 weeks). For long term storage, aliquot and store at -2°C or -7°C. Avoid repeated freezing and thawing cycles. |
| References | Lees-Miller JP.. (1991) Bioessays. 13(9):429-37. Perry SV. (2001) J Muscle Res Cell Motil. 22(1):5-49. |
| Background | TPM1 is a member of the tropomyosin family of highly conserved, widely distributed actin-binding proteins involved in the contractile system of striated and smooth muscles and the cytoskeleton of non-muscle cells. Tropomyosin is composed of two alpha-helical chains arranged as a coiled-coil. It is polymerized end to end along the two grooves of actin filaments and provides stability to the filaments. TPM1 is one type of alpha helical chain that forms the predominant tropomyosin of striated muscle, where it also functions in association with the troponin complex to regulate the calcium-dependent interaction of actin and myosin during muscle contraction. Recombinant human TPM1 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. |
| Supplier | ARP |
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