Date published: 2025-12-19

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spectrin α Activators

Spectrin α, a critical component of the cytoskeletal network, is regulated and activated by a diverse array of chemical compounds, each playing a unique role in enhancing its functionality. The interaction of Spectrin α with phosphatidylinositol 4,5-bisphosphate (PIP2) and calmodulin exemplifies its dynamic regulation; PIP2 directly influences Spectrin α's membrane association, enhancing its ability to maintain cellular integrity, while calmodulin binding, in a calcium-dependent manner, modulates Spectrin α's structural properties. Erythropoietin also plays a vital role, particularly in erythroid cells, by stabilizing and optimizing Spectrin α's functionality, essential for red blood cell deformability and survival. The presence of calcium ions further influences Spectrin α, especially in its interaction with calcium-binding proteins, thereby modulating its conformation and interactions within the cytoskeleton and membranes. Additionally, ATP binding to Spectrin α is critical for its conformational dynamics, which is essential for maintaining cell shape and membrane integrity.

Further exploring the regulators of Spectrin α, cyclic AMP (cAMP) through PKA-mediated phosphorylation, and Phorbol 12-myristate 13-acetate (PMA), as a PKC activator, play significant roles in modulating its activity. cAMP influences Spectrin α by altering its interaction with other cytoskeletal proteins, thereby enhancing its structural support role. On the other hand, PMA-induced phosphorylation can modify Spectrin α's interactions, further strengthening its contribution to the cytoskeletal framework. Magnesium ions, essential for ATP binding, and Nitric oxide, which modulates Spectrin α's flexibility and stress response, also contribute to its functional enhancement. Collectively, these compounds, through their specific and targeted effects on cellular and molecular pathways, facilitate the enhancement of Spectrin α's role in maintaining cellular shape, structural integrity, and adaptability to mechanical stress, underscoring its importance in cellular architecture and function.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

ADP

58-64-0sc-507362
5 g
$53.00
(0)

Binds to Spectrin α, involved in conformational changes, influencing flexibility and ability to maintain cell shape and membrane integrity.

Adenosine 3′,5′-cyclic monophosphate

60-92-4sc-217584
sc-217584A
sc-217584B
sc-217584C
sc-217584D
sc-217584E
100 mg
250 mg
5 g
10 g
25 g
50 g
$114.00
$175.00
$260.00
$362.00
$617.00
$1127.00
(1)

Through PKA-mediated phosphorylation, influences Spectrin α's function, potentially altering its interaction with other cytoskeletal proteins and enhancing its role in cellular structural support.

PMA

16561-29-8sc-3576
sc-3576A
sc-3576B
sc-3576C
sc-3576D
1 mg
5 mg
10 mg
25 mg
100 mg
$40.00
$129.00
$210.00
$490.00
$929.00
119
(6)

As a PKC activator, influences Spectrin α through phosphorylation, modifying its interaction with other cytoskeletal proteins and enhancing its structural role in the cell.