Recombinant Human Caldesmon/CDM protein is a Human Full Length protein, in the 1 to 538 aa range, expressed in Wheat germ and suitable for SDS-PAGE, ELISA, WB.
Wheat germ
Tag free
SDS-PAGE, ELISA, WB
No
Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application ELISA | Reactivity Reacts | Dilution info - | Notes - |
Application WB | Reactivity Reacts | Dilution info - | Notes - |
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 plays an essential role during cellular mitosis and receptor capping. Involved in Schwann cell migration during peripheral nerve regeneration (By similarity).
CAD, CDM, CDM, CAD, CALD1, Caldesmon, CDM
Recombinant Human Caldesmon/CDM protein is a Human Full Length protein, in the 1 to 538 aa range, expressed in Wheat germ and suitable for SDS-PAGE, ELISA, WB.
Wheat germ
Tag free
SDS-PAGE, ELISA, WB
No
No
Human
pH: 8
Constituents: 0.79% Tris HCl, 0.3% Glutathione
Full Length
85.25 kDa
1 to 538
Recombinant
Liquid
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 plays an essential role during cellular mitosis and receptor capping. Involved in Schwann cell migration during peripheral nerve regeneration (By similarity).
Belongs to the caldesmon family.
In 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. CDK1-mediated phosphorylation promotes Schwann cell migration during peripheral nerve regeneration (By similarity).
Cytoskeleton, Stress fiber
Dry Ice
-80°C
-80°C
Upon delivery aliquot
Avoid freeze / thaw cycle
This product was previously labelled as Caldesmon.
This supplementary information is collated from multiple sources and compiled automatically.
Caldesmon also known as CDM CALD1 and h-caldesmon is a cytoskeletal protein with a molecular mass of approximately 93 to 120 kDa. This protein expresses itself abundantly in smooth muscle tissues yet it can also be found in non-muscle cells like fibroblasts and endothelial cells. Researchers often use specific caldesmon antibodies in immunohistochemistry allowing them to label various cellular components and providing insights into tissue composition. Due to its presence in muscle tissues caldesmon is essential for understanding muscle physiology and pathology.
Caldesmon interacts with actin and myosin to regulate actomyosin contractility. This protein plays a critical role in controlling the contraction and relaxation processes in smooth muscle cells. Caldesmon forms part of a complex that includes calmodulin and tropomyosin enhancing its ability to stabilize actin filaments. It functions by inhibiting the ATPase activity of myosin therefore influencing cellular motility and shape change mechanisms. Researchers continually study caldesmon to comprehend its interactome and its significance within the larger cellular structure.
Caldesmon participates in the regulation of the cytoskeletal dynamics vital for cell motility and structural integrity. In particular it is an important component of the contraction-relaxation cycle pathway in smooth muscle tissues. This protein has connections with pathways involving RhoA-Rho kinase where caldesmon modulates the phosphorylation levels influencing muscle contraction. Additionally proteins like tropomyosin and calmodulin modulate its activity especially under calcium-calmodulin-dependent pathways which further elucidates its regulatory importance.
Caldesmon has associations with conditions like certain types of cancers and cardiovascular diseases. Its expression levels and distribution provide valuable information in identifying smooth muscle tumors and other pathological conditions. In oncology for example h-caldesmon serves as a marker to distinguish leiomyosarcomas from other tumors. Moreover due to its involvement in smooth muscle contractility caldesmon links with proteins such as calmodulin and tropomyosin in diseases where abnormal contraction and cellular motility play significant roles. Understanding these connections is important for developing targeted treatments and improving diagnostic accuracy.
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12.5% SDS-PAGE image showing ab114302 Stained with Coomassie Blue.
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