Recombinant Human Caldesmon/CDM protein (ab114302)
Key features and details
- Expression system: Wheat germ
- Suitable for: WB, ELISA, SDS-PAGE
Description
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Product name
Recombinant Human Caldesmon/CDM protein -
Expression system
Wheat germ -
Accession
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Protein length
Full length protein -
Animal free
No -
Nature
Recombinant -
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Species
Human -
Predicted molecular weight
85 kDa including tags -
Amino acids
1 to 538
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Specifications
Our Abpromise guarantee covers the use of ab114302 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Applications
Western blot
ELISA
SDS-PAGE
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Form
Liquid -
Additional notes
This product was previously labelled as Caldesmon.
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Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
pH: 8.00
Constituents: 0.3% Glutathione, 0.79% Tris HCl
General Info
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Alternative names
- CAD
- CALD 1
- CALD1
see all -
Function
Actin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). Stimulates actin binding of tropomyosin which increases the stabilization of actin filament structure. In muscle tissues, inhibits the actomyosin ATPase by binding to F-actin. This inhibition is attenuated by calcium-calmodulin and is potentiated by tropomyosin. Interacts with actin, myosin, two molecules of tropomyosin and with calmodulin. Also play an essential role during cellular mitosis and receptor capping. -
Tissue specificity
High-molecular-weight caldesmon (isoform 1) is predominantly expressed in smooth muscles, whereas low-molecular-weight caldesmon (isoforms 2, 3, 4 and 5) are widely distributed in non-muscle tissues and cells. Not expressed in skeletal muscle or heart. -
Sequence similarities
Belongs to the caldesmon family. -
Domain
The N-terminal part seems to be a myosin/calmodulin-binding domain, and the C-terminal a tropomyosin/actin/calmodulin-binding domain. These two domains are separated by a central helical region in the smooth-muscle form. -
Post-translational
modificationsIn non-muscle cells, phosphorylation by CDK1 during mitosis causes caldesmon to dissociate from microfilaments. Phosphorylation reduces caldesmon binding to actin, myosin, and calmodulin as well as its inhibition of actomyosin ATPase activity. Phosphorylation also occurs in both quiescent and dividing smooth muscle cells with similar effects on the interaction with actin and calmodulin and on microfilaments reorganization. -
Cellular localization
Cytoplasm > cytoskeleton. Cytoplasm > myofibril. On thin filaments in smooth muscle and on stress fibers in fibroblasts (nonmuscle). - Information by UniProt
Protocols
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
Datasheets and documents
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Datasheet download
References (0)
ab114302 has not yet been referenced specifically in any publications.