Recombinant Mouse Tropomyosin alpha-1 chain (Tpm1)

Code CSB-YP024104MO
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Source Yeast
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Code CSB-EP024104MO
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Source E.coli
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Code CSB-EP024104MO-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP024104MO
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Source Baculovirus
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Code CSB-MP024104MO
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Tpm1
Uniprot No.
Alternative Names
Tpm1; Tpm-1; Tpma; Tropomyosin alpha-1 chain; Alpha-tropomyosin; Tropomyosin-1
Species
Mus musculus (Mouse)
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
Protein Length
Full length protein
Tag Info
Tag type will be determined during the manufacturing process.
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.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
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.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

Customer Reviews and Q&A

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Target Background

Function
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
  1. Stress fibre formation and up-regulation of alpha-smooth muscle actin (alphaSMA) induced by TGFbeta2 could be reversed by Tpm1/2 knock-down by siRNA. PMID: 27976512
  2. The cMyBP-C hypertrophic cardiomyopathy variant L348P enhances thin filament activation through an increased shift in tropomyosin position. PMID: 26718724
  3. three-dimensional structure of F-actin at a resolution of 3.7 A in complex with tropomyosin at a resolution of 6.5 A, determined by electron cryomicroscopy PMID: 25470062
  4. data also identify a novel alphaTM1/Tmod1-based pathway stabilizing F-actin at cell-cell junctions, which may be required for maintenance of cell shapes during embryonic cardiac morphogenesis. PMID: 24500875
  5. This is the first study to demonstrate that decreasing phosphorylation of tropomyosin can rescue a hypertrophic cardiomyopathic phenotype. PMID: 23960072
  6. the link between flexibility of TM and its function in ejecting hearts. PMID: 23609439
  7. Tm pseudo-phosphorylation slows deactivation of the thin filament and muscle force relaxation dynamics in the absence of dynamic and steady-state effects on muscle activation. PMID: 23232082
  8. Tropomyosin dephosphorylation results in myocyte hypertrophy with increases in SERCA2a expression. PMID: 23148217
  9. The results identify a novel mode of myofilament desensitization to Ca(2+) associated with a DCM linked switch in TPM1-kappa. PMID: 21221740
  10. signaling by alpha-tropomyosin may have a role in familial hypertrophic cardiomyopathy PMID: 14519438
  11. A point mutation in alpha-TM causes a disease similar to familial hypertophic cardiomyopahy. PMID: 14575301
  12. PTB interacting protein raver1 regulates alpha-tropomyosin alternative splicing. PMID: 14633994
  13. the N terminus is a critical determinant of TM1 functions, which in turn determines the organization of stress fibers. PMID: 14722123
  14. charge changes at the carboxy-terminal of alpha-TM alter the functional characteristics of the heart at both the whole organ and myofilament levels. PMID: 14766940
  15. Two transgenic lines of mutated alpha-TM demonstrated alterations in myocardial contractility differently. PMID: 15486021
  16. Chronic activation of p38alpha MAPK directly depresses sarcomeric function in association with decreased phosphorylation of alpha-tropomyosin. PMID: 17234967
  17. Developed mouse model of familial hypertrophic cardiomyopathy with a mutation in the thin filament protein alpha-tropomyosin. PMID: 17416600

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Subcellular Location
Cytoplasm, cytoskeleton.
Protein Families
Tropomyosin family
Database Links

KEGG: mmu:22003

UniGene: Mm.121878

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