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Safety Information

T2400

Sigma-Aldrich

Tropomyosin from porcine muscle

lyophilized powder (contains Tris buffer salts)

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About This Item

CAS Number:
9067-56-5
MDL number:
MFCD00132526
UNSPSC Code:
12352202
NACRES:
NA.77

¥1,737.73

Please contact Customer Service for Availability

biological source

Porcine muscle

Quality Level

200

Assay

≥70% protein basis (biuret)

form

lyophilized powder (contains Tris buffer salts)

technique(s)

electrophoresis: suitable

storage temp.

−20°C

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This Item
A4414G2500C3400
Tropomyosin from porcine muscle lyophilized powder (contains Tris buffer salts)

T2400

Tropomyosin from porcine muscle

白蛋白 来源于猪血清 lyophilized powder, essentially globulin free, ≥99% (agarose gel electrophoresis)

A4414

白蛋白 来源于猪血清

明胶 来源于猪皮肤 gel strength 300, Type A

G2500

明胶 来源于猪皮肤

酪蛋白 来源于牛奶 powder

C3400

酪蛋白 来源于牛奶

assay

≥70% protein basis (biuret)

assay

≥99% (agarose gel electrophoresis)

assay

70-90% (biuret)

assay

87-94% protein basis

biological source

Porcine muscle

biological source

Porcine

biological source

Porcine skin

biological source

bovine milk

technique(s)

electrophoresis: suitable

technique(s)

cell culture | mammalian: suitable

technique(s)

cell culture | mammalian: suitable

technique(s)

activity assay: suitable, electrophoresis: suitable, immunocytochemistry: suitable

form

lyophilized powder (contains Tris buffer salts)

form

lyophilized powder

form

powder

form

powder

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

-

storage temp.

-

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200

General description

Tropomyosin is a member of the actin filament binding protein family.[1] It is a ubiquitous protein present in animals and fungi.[2] Tropomyosin is made up of two α-helical chains arranged as a coiled-coil. It exists over twenty isoforms,[3] in different eukaryotic cells like skeletal, cardiac, and smooth muscles, brain, platelets, fibroblasts, platelets, and other non-muscle cells.[4]

Application

Tropomyosin from porcine muscle has been used:

  • as a positive control in actin- α-tropomyosin (TPM1) co-sedimentation analysis and assay[5]
  • in analyzing the anti-adhesive properties of fish tropomyosins[6]
  • in far Western blot analysis[7]

Biochem/physiol Actions

Dimeric protein that assumes an α-helical coiled coil conformation. In the absence of Ca2+, inhibits muscle contractility by blocking the myosin binding sites on actin.
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.[2]
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

Regulatory Information

动植物源性产品

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    Certificates of Analysis (COA)

    Lot/Batch Number
    0000424189
    058H7834
    058H7834
    0000424189
    0000293825

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    A systematic nomenclature for mammalian tropomyosin isoforms
    Michael A G, et al.
    Journal of Muscle Research and Cell Motility, 147?153-147?153 (2015)
    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)
    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)
    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
    View All Related Papers

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