|Overview||N-terminal GST-tagged recombinant human, full length cofilin 1|
|Application||Cofilin 1 primarily used in Kinase Assays.|
|Safety Information according to GHS|
|Storage and Shipping Information|
|Storage Conditions||1 year at -20°C|
|Material Size||150 µg|
|Cofilin 1 - D8JN060AU||D8JN060AU|
|Cofilin 1 - D8JN060U-B||D8JN060U-B|
|Cofilin 1 - D8JN060U-C||D8JN060U-C|
|Cofilin 1 - D8JN060U-D||D8JN060U-D|
|Reference overview||Pub Med ID|
|High serum leptin is an independent risk factor for non-response patients with low viremia to antiviral treatment in chronic hepatitis C.|
Yuichiro Eguchi,Toshihiko Mizuta,Tsutomu Yasutake,Akitaka Hisatomi,Ryuichi Iwakiri,Iwata Ozaki,Kazuma Fujimoto
World journal of gastroenterology : WJG 12 2006
To determine whether body weight and/or serum leptin were independent predictors of response to antiviral treatment in patients with chronic hepatitis C.
|Regulation of the neuronal actin cytoskeleton by ADF/cofilin.|
Sarmiere, Patrick D and Bamburg, James R
J. Neurobiol., 58: 103-17 (2004) 2004
Actin and microtubules are major cytoskeletal elements of most cells including neurons. In order for a cell to move and change shape, its cytoskeleton must undergo rearrangements that involve breaking down and reforming filaments. Many recent reviews have focused on the signaling pathways emanating from receptors that ultimately affect axon growth and growth cone steering. This particular review will address changes in the actin cytoskeleton modulated by the family of actin dynamizing proteins known as actin depolymerizing factor (ADF)/cofilin or AC proteins. Though much is known about inactivation of AC proteins through phosphorylation at ser3 by LIM or TES kinases, new mechanisms of regulation of AC have recently emerged. A novel phosphatase, slingshot (SSH), and the 14-3-3 family of regulatory proteins have also been found to affect AC activity. The potential role of AC proteins in modulating the actin organizational changes that accompany neurite initiation, axonogenesis, growth cone guidance, and dendritic spine formation will be discussed.
|Signal transduction cascades underlying de novo protein synthesis required for neuronal morphogenesis in differentiating neurons.|
Tojima, Takuro and Ito, Etsuro
Prog. Neurobiol., 72: 183-93 (2004) 2004
Differentiating neurons must acquire many unique morphological and functional characteristics in creating the precise neural circuits of the mature nervous system. The phenomenon of 'neuronal differentiation' includes a special set of simple, separate processes, that is, neuritogenesis, neurite outgrowth, pathfinding, targeting and synaptogenesis. All of these processes are critically dependent on the reorganization of actin cytoskeleton by many actin-binding proteins that function downstream of Rho-family GTPases. Furthermore, de novo synthesis of key proteins are critically involved in the reorganization of actin cytoskeleton during neuronal differentiation. In this article, we review recent progresses in the general mechanisms that control actin dynamics by various actin-binding proteins in differentiating neurons, including a series of recent studies from our laboratory on de novo synthesis of several key proteins that are essential for actin reorganization induced by second messengers. We demonstrated that dual regulation of cyclic AMP and Ca2+ determines cofilin (an actin-binding protein) phosphorylation states and LIM kinase 1 (a cofilin kinase) expression level during neuritogenesis.
|Regulation of actin filament dynamics by actin depolymerizing factor/cofilin and actin-interacting protein 1: new blades for twisted filaments.|
Biochemistry, 42: 13363-70 (2003) 2003
Actin depolymerizing factor (ADF)/cofilin enhances turnover of actin filaments by severing and depolymerizing filaments. A number of proteins functionally interact with ADF/cofilin to modulate the dynamics of actin filaments. Actin-interacting protein 1 (AIP1) has emerged as a conserved WD-repeat protein that specifically enhances ADF/cofilin-induced actin dynamics. Interaction of AIP1 with actin was originally characterized by a yeast two-hybrid system. However, biochemical studies revealed its unique activity on ADF/cofilin-bound actin filaments. AIP1 alone has negligible effects on actin filament dynamics, whereas in the presence of ADF/cofilin, AIP1 enhances filament fragmentation by capping ends of severed filaments. Studies in model organisms demonstrated that AIP1 genetically interacts with ADF/cofilin and participates in several actin-dependent cellular events. The crystal structure of AIP1 revealed its unique structure with two seven-bladed beta-propeller domains. Thus, AIP1 is a new class of actin regulatory proteins that selectively enhances ADF/cofilin-dependent actin filament dynamics.
|Regulation of cortical actin networks in cell migration.|
Suetsugu, Shiro and Takenawa, Tadaomi
Int. Rev. Cytol., 229: 245-86 (2003) 2003
The actin cytoskeleton is a primary determinant of cell shape and motility. Studies on actin regulatory proteins are now coupled with studies of the signal transduction that directs actin cytoskeleton reorganization, and we have gained insights into how external stimuli such as chemoattractants drive changes in actin cytoskeleton. Chemoattractants regulate actin regulatory proteins such as the Arp2/3 complex through WASP family proteins, ADF/cofilin downstream of LIM-kinase, and various other phosphoinositide-dependent or -independent pathways. Through branching of actin filaments, Arp2/3 complex-dependent actin polymerization is suffcient to generate the force necessary for protrusion.