T2400
Tropomyosin from porcine muscle
lyophilized powder (contains Tris buffer salts)
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About This Item
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biological source
Porcine muscle
Quality Level
Assay
≥70% protein basis (biuret)
form
lyophilized powder (contains Tris buffer salts)
technique(s)
electrophoresis: suitable
storage temp.
−20°C
General description
Tropomyosin is a member of the actin filament binding protein family. It is a ubiquitous protein present in animals and fungi. Tropomyosin is made up of two α-helical chains arranged as a coiled-coil. It exists over twenty isoforms, in different eukaryotic cells like skeletal, cardiac, and smooth muscles, brain, platelets, fibroblasts, platelets, and other non-muscle cells.
Application
Tropomyosin from porcine muscle has been used:
- as a positive control in actin- α-tropomyosin (TPM1) co-sedimentation analysis and assay
- in analyzing the anti-adhesive properties of fish tropomyosins
- in far Western blot analysis
Biochem/physiol Actions
Tropomyosin is associated with the actin cytoskeleton and plays a role in stabilizing and regulating the interactions of actin with other actin-binding proteins. It also plays a role in muscle contraction by regulating the interactions of actin with myosin.
Tropomyosin together with troponin, regulates the binding of myosin to actin. Tropomyosin is a dimeric coiled-coil protein forming continuous polymers along the myosin-binding groove of actin. Various tropomyosin isoforms help confer structure and function to actins in the cytoskeleton and striated muscle function. Dimeric protein that assumes an α-helical coiled-coil conformation. In the absence of Ca2+, it inhibits muscle contractility by blocking the myosin binding sites on actin.
Analysis Note
SDS electrophoresis shows two major bands.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Vertebrate tropomyosin: distribution, properties and function
Perry S V, et al.
Journal of Muscle Research and Cell Motility, 5?49-5?49 (2001)
The molecular basis for tropomyosin isoform diversity
James P L M, et al.
Bioessays (1991)
A novel alpha-tropomyosin mutation associates with dilated and non-compaction cardiomyopathy and diminishes actin binding
Judith B A, et al.
Biochimica et Biophysica Acta - Molecular Cell Research, 1833(4), 833-839 (2013)
A systematic nomenclature for mammalian tropomyosin isoforms
Michael A G, et al.
Journal of Muscle Research and Cell Motility, 147?153-147?153 (2015)
G Reese et al.
International archives of allergy and immunology, 119(4), 247-258 (1999-09-04)
Among food allergens, crustaceans, such as shrimp, crab, crawfish and lobster, are a frequent cause of adverse food reactions in allergic individuals. The major allergen has been identified as the muscle protein tropomyosin. This molecule belongs to a family of
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