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Human Establishment of Meiotic Spindle Localization

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Nonmuscle myosin is an actin-based motor protein essential to cell motility, cell division, migration, adhesion, and polarity. The holoenzyme consists of two identical heavy chains and two sets of light chains. The light chains (MLCs) regulate myosin II activity and stability. The heavy chains (NMHCs) are encoded by three genes, MYH9, MYH10, and MYH14, which generate three different nonmuscle myosin II isoforms, IIa, IIb, and IIc, respectively (reviewed in 1). While all three isoforms perform the same enzymatic tasks, binding to and contracting actin filaments coupled to ATP hydrolysis, their cellular functions do not appear to be redundant and they have different subcellular distributions (2-5). The carboxy-terminal tail domain of myosin II is important in isoform-specific subcellular localization (6). Research studies have shown that phosphorylation of myosin IIa at Ser1943 contributes to the regulation of breast cancer cell migration (7).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Nonmuscle myosin is an actin-based motor protein essential to cell motility, cell division, migration, adhesion, and polarity. The holoenzyme consists of two identical heavy chains and two sets of light chains. The light chains (MLCs) regulate myosin II activity and stability. The heavy chains (NMHCs) are encoded by three genes, MYH9, MYH10, and MYH14, which generate three different nonmuscle myosin II isoforms, IIa, IIb, and IIc, respectively (reviewed in 1). While all three isoforms perform the same enzymatic tasks, binding to and contracting actin filaments coupled to ATP hydrolysis, their cellular functions do not appear to be redundant and they have different subcellular distributions (2-5). The carboxy-terminal tail domain of myosin II is important in isoform-specific subcellular localization (6). Research studies have shown that phosphorylation of myosin IIa at Ser1943 contributes to the regulation of breast cancer cell migration (7).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Nonmuscle myosin is an actin-based motor protein essential to cell motility, cell division, migration, adhesion, and polarity. The holoenzyme consists of two identical heavy chains and two sets of light chains. The light chains (MLCs) regulate myosin II activity and stability. The heavy chains (NMHCs) are encoded by three genes, MYH9, MYH10, and MYH14, which generate three different nonmuscle myosin II isoforms, IIa, IIb, and IIc, respectively (reviewed in 1). While all three isoforms perform the same enzymatic tasks, binding to and contracting actin filaments coupled to ATP hydrolysis, their cellular functions do not appear to be redundant and they have different subcellular distributions (2-5). The carboxy-terminal tail domain of myosin II is important in isoform-specific subcellular localization (6). Research studies have shown that phosphorylation of myosin IIa at Ser1943 contributes to the regulation of breast cancer cell migration (7).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: Actin nucleation, the formation of new actin filaments from existing filaments, affects actin filament structure during cell motility, division, and intracellular trafficking. An important actin nucleation protein complex is the highly conserved ARP2/3 complex, consisting of ARP2, ARP3, and ARPC1-5. The ARP2/3 complex promotes branching of an existing actin filament and formation of a daughter filament following activation by nucleation-promoting factors, such as WASP/WAVE or cortactin (1). The formation of podosomes, small cellular projections that degrade the extracellular matrix, is enhanced by ARP2/3 complex action. ARP2/3 competes with caldesmon, an actin binding protein shown to negatively affect podosome formation (2). Along with N-WASP, the ARP2/3 complex regulates nuclear actin filament nucleation and controls actin polymerization during transcription (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Bovine, Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Actin nucleation, the formation of new actin filaments from existing filaments, affects actin filament structure during cell motility, division, and intracellular trafficking. An important actin nucleation protein complex is the highly conserved ARP2/3 complex, consisting of ARP2, ARP3, and ARPC1-5. The ARP2/3 complex promotes branching of an existing actin filament and formation of a daughter filament following activation by nucleation-promoting factors, such as WASP/WAVE or cortactin (1). The formation of podosomes, small cellular projections that degrade the extracellular matrix, is enhanced by ARP2/3 complex action. ARP2/3 competes with caldesmon, an actin binding protein shown to negatively affect podosome formation (2). Along with N-WASP, the ARP2/3 complex regulates nuclear actin filament nucleation and controls actin polymerization during transcription (3).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
D. melanogaster, Hamster, Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Actin nucleation, the formation of new actin filaments from existing filaments, affects actin filament structure during cell motility, division, and intracellular trafficking. An important actin nucleation protein complex is the highly conserved ARP2/3 complex, consisting of ARP2, ARP3, and ARPC1-5. The ARP2/3 complex promotes branching of an existing actin filament and formation of a daughter filament following activation by nucleation-promoting factors, such as WASP/WAVE or cortactin (1). The formation of podosomes, small cellular projections that degrade the extracellular matrix, is enhanced by ARP2/3 complex action. ARP2/3 competes with caldesmon, an actin binding protein shown to negatively affect podosome formation (2). Along with N-WASP, the ARP2/3 complex regulates nuclear actin filament nucleation and controls actin polymerization during transcription (3).