Description
Product Name: | Human TPM1 Recombinant Protein |
Product Code: | RPPB4989 |
Size: | 10µg |
Species: | Human |
Target: | TPM1 |
Synonyms: | Tropomyosin alpha-1 chain, Tropomyosin-1, Alpha-tropomyosin, TPM1, C15orf13, TMSA, CMD1Y, HTM-alpha. |
Source: | Escherichia Coli |
Physical Appearance: | Sterile Filtered clear solution. |
Formulation: | TPM1 0.5mg/ml protein solution contains 20mM Tris-HCl buffer pH-8, 1mM DTT, 0.1M NaCl & 20% glycerol. |
Stability: | Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles. |
Purity: | Greater than 90.0% as determined by SDS-PAGE. |
Amino Acid Sequence: | MGSSHHHHHH SSGLVPRGSH MDAIKKKMQM LKLDKENALD RAEQAEADKK AAEDRSKQLE DELVSLQKKL KGTEDELDKY SEALKDAQEKLELAEKKATD AEADVASLNR RIQLVEEELD RAQERLATAL QKLEEAEKAA DESERGMKVI ESRAQKDEEK MEIQEIQLKE AKHIAEDADRKYEEVARKLV IIESDLERAE ERAELSEGQV RQLEEQLRIM DQTLKALMAA EDKYSQKEDR YEEEIKVLSD KLKEAETRAE FAERSVTKLEKSIDDLEDEL YAQKLKYKAI SEELDHALND MTSM |
TPM1 is a member of the tropomyosin family which consists of a number of extremely conserved, extensively distributed 35-45 kDa actin-binding proteins that are involved in the contractile system of striated and smooth muscles and the cytoskeleton of non-muscle cells. Tropomyosin-1 is composed of 2 alpha-helical chains arranged as a coiled-coil. TPM1 is polymerized end to end alongside the two grooves of actin filaments and provides stability to the filaments. TPM1 binds to actin filaments in muscle and non-muscle cells. TPM1 also functions in association with the troponin complex to regulate the calcium-dependent interaction of actin and myosin during muscle contraction. In non-muscle cells TPM1 is implicated in stabilizing cytoskeleton actin filaments. Smooth muscle contraction is controlled by interaction with caldesmon. Alternatively spliced transcript variants encoding a range of isoforms have been described in smooth muscle and non-muscle cells. TPM1 Isoform 1 is expressed in adult and fetal skeletal muscle and cardiac tissues, with higher expression levels in the cardiac tissues, whereas Isoform 10 is expressed in adult and fetal cardiac tissues, but not in skeletal muscle.Mutations in the TPM1 gene are linked to type 3 familial hypertrophic cardiomyopathy.
TPM1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 304 amino acids (1-284 a.a.) and having a total molecular mass of 35kDa (Molecular weight on SDS-PAGE will appear higher). TPM1 is fused to a 20 amino acid His Tag at N-terminus and is purified by proprietary chromatographic techniques.
UniProt Protein Function: | TPM1: a cytoskeletal protein that binds to actin filaments in muscle and nonmuscle 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. Defects in TPM3 are a cause of nemaline myopathy type 1 (NEM1). Three alternatively spliced isoforms have been described. |
UniProt Protein Details: | Protein type:Motility/polarity/chemotaxis; Actin-binding; Motor Chromosomal Location of Human Ortholog: 15q22.1 Cellular Component: filamentous actin; sarcomere; cytoskeleton; stress fiber; cytosol; muscle thin filament tropomyosin Molecular Function:structural constituent of cytoskeleton; structural constituent of muscle; cytoskeletal protein binding; actin binding Biological Process: positive regulation of cell adhesion; wound healing; regulation of muscle contraction; in utero embryonic development; cytoskeleton organization and biogenesis; sarcomere organization; regulation of heart contraction; muscle filament sliding; muscle contraction; positive regulation of ATPase activity; positive regulation of stress fiber formation; ruffle organization and biogenesis; ventricular cardiac muscle morphogenesis; cell motility; negative regulation of cell migration; positive regulation of heart rate by epinephrine; cardiac muscle contraction Disease: Cardiomyopathy, Dilated, 1y; Cardiomyopathy, Familial Hypertrophic, 3 |
NCBI Summary: | This gene 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. The encoded protein 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. In smooth muscle and non-muscle cells, alternatively spliced transcript variants encoding a range of isoforms have been described. Mutations in this gene are associated with type 3 familial hypertrophic cardiomyopathy. [provided by RefSeq, Jul 2008] |
UniProt Code: | P09493 |
NCBI GenInfo Identifier: | 136092 |
NCBI Gene ID: | 7168 |
NCBI Accession: | P09493.2 |
UniProt Secondary Accession: | P09493,P09494, P10469, Q6DV89, Q6DV90, Q7Z6L8, Q86W64 Q96IK2, B7Z5T7, D9YZV2, D9YZV3, D9YZV8, |
UniProt Related Accession: | P09493 |
Molecular Weight: | 284 |
NCBI Full Name: | Tropomyosin alpha-1 chain |
NCBI Synonym Full Names: | tropomyosin 1 (alpha) |
NCBI Official Symbol: | TPM1�� |
NCBI Official Synonym Symbols: | CMH3; TMSA; CMD1Y; LVNC9; C15orf13; HTM-alpha�� |
NCBI Protein Information: | tropomyosin alpha-1 chain; alpha-tropomyosin; sarcomeric tropomyosin kappa; cardiomyopathy, hypertrophic 3 |
UniProt Protein Name: | Tropomyosin alpha-1 chain |
UniProt Synonym Protein Names: | Alpha-tropomyosin; Tropomyosin-1 |
Protein Family: | Tropomyosin |
UniProt Gene Name: | TPM1�� |
UniProt Entry Name: | TPM1_HUMAN |