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Rat Establishment of Chromosome Localization

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

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Frozen), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: Survivin is a 16 kDa anti-apoptotic protein highly expressed during fetal development and cancer cell malignancy (1). Survivin binds and inhibits caspase-3, controlling the checkpoint in the G2/M-phase of the cell cycle by inhibiting apoptosis and promoting cell division (2,3). This regulatory process requires the phosphorylation of survivin at Thr34 by p34 cdc2 kinase (4). Gene targeting using a Thr34 phosphorylation-defective survivin mutant, as well as antisense survivin, have been shown to inhibit tumor growth (5,6).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 488 fluorescent dye and tested in-house for direct flow cytometry and immunofluorescent analysis in human cells.The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Survivin (71G4B7) Rabbit mAb #2808.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

Background: Survivin is a 16 kDa anti-apoptotic protein highly expressed during fetal development and cancer cell malignancy (1). Survivin binds and inhibits caspase-3, controlling the checkpoint in the G2/M-phase of the cell cycle by inhibiting apoptosis and promoting cell division (2,3). This regulatory process requires the phosphorylation of survivin at Thr34 by p34 cdc2 kinase (4). Gene targeting using a Thr34 phosphorylation-defective survivin mutant, as well as antisense survivin, have been shown to inhibit tumor growth (5,6).

$305
50 tests
100 µl
Cell Signaling Technology antibody is conjugated to Alexa Fluor® 647 fluorescent dye and tested in-house for direct flow cytometric analysis of human cells. The unconjugated antibody, #2808 reacts with survivin from human, mouse, and rat. CST expects that Survivin (71G4E) Rabbit mAb (Alexa Fluor® 647 Conjugate) will also recognize survivin in these species.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry

Background: Survivin is a 16 kDa anti-apoptotic protein highly expressed during fetal development and cancer cell malignancy (1). Survivin binds and inhibits caspase-3, controlling the checkpoint in the G2/M-phase of the cell cycle by inhibiting apoptosis and promoting cell division (2,3). This regulatory process requires the phosphorylation of survivin at Thr34 by p34 cdc2 kinase (4). Gene targeting using a Thr34 phosphorylation-defective survivin mutant, as well as antisense survivin, have been shown to inhibit tumor growth (5,6).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Survivin (71G4B7) Rabbit mAb #2808.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry

Background: Survivin is a 16 kDa anti-apoptotic protein highly expressed during fetal development and cancer cell malignancy (1). Survivin binds and inhibits caspase-3, controlling the checkpoint in the G2/M-phase of the cell cycle by inhibiting apoptosis and promoting cell division (2,3). This regulatory process requires the phosphorylation of survivin at Thr34 by p34 cdc2 kinase (4). Gene targeting using a Thr34 phosphorylation-defective survivin mutant, as well as antisense survivin, have been shown to inhibit tumor growth (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Importins belong to the karyopherin family of nuclear transport proteins (1) and are divided into two subgroups: importin α and importin β. Importins mainly function in nuclear protein import and export (2,3). Importin β1 (also known as karyopherin β1, Kpnβ1, Kpnb1, or p97) plays a key role in the nuclear import process (1-3). Nuclear import via importin β1 association with adaptor importin α (also known as karyopherin α, or Kpnα) is an essential component of the classical nuclear localization signal (NLS) pathway (4). Importin α directly recognizes the NLS present in the cargo target, prompting complex formation with importin β1. The cargo:importin α:importin β1 complex is transported across the nuclear pore complex (NPC) into the nucleus, where it is dissociated by the binding of RanGTP (1-4). Nuclear import directly via importin β1 can also occur by importin β1 recognition of the cargo protein, bypassing importin α involvement. In both cases, the importin β1/target protein interaction is mediated through the binding of importin β1 HEAT repeats with the target protein sequences (either the cargo protein itself or importin α) (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Importins belong to the karyopherin family of nuclear transport proteins (1) and are divided into two subgroups: importin α and importin β. Importins mainly function in nuclear protein import and export (2,3). Importin β1 (also known as karyopherin β1, Kpnβ1, Kpnb1, or p97) plays a key role in the nuclear import process (1-3). Nuclear import via importin β1 association with adaptor importin α (also known as karyopherin α, or Kpnα) is an essential component of the classical nuclear localization signal (NLS) pathway (4). Importin α directly recognizes the NLS present in the cargo target, prompting complex formation with importin β1. The cargo:importin α:importin β1 complex is transported across the nuclear pore complex (NPC) into the nucleus, where it is dissociated by the binding of RanGTP (1-4). Nuclear import directly via importin β1 can also occur by importin β1 recognition of the cargo protein, bypassing importin α involvement. In both cases, the importin β1/target protein interaction is mediated through the binding of importin β1 HEAT repeats with the target protein sequences (either the cargo protein itself or importin α) (5).

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

Application Methods: Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: At least four distinct polo-like kinases exist in mammalian cells: PLK1, PLK2, PLK3, and PLK4/SAK (1). PLK1 apparently plays many roles during mitosis, particularly in regulating mitotic entry and exit. The mitosis promoting factor (MPF), cdc2/cyclin B1, is activated by dephosphorylation of cdc2 (Thr14/Tyr15) by cdc25C. PLK1 phosphorylates cdc25C at Ser198 and cyclin B1 at Ser133 causing translocation of these proteins from the cytoplasm to the nucleus (2-5). PLK1 phosphorylation of Myt1 at Ser426 and Thr495 has been proposed to inactivate Myt1, one of the kinases known to phosphorylate cdc2 at Thr14/Tyr15 (6). Polo-like kinases also phosphorylate the cohesin subunit SCC1, causing cohesin displacement from chromosome arms that allow for proper cohesin localization to centromeres (7). Mitotic exit requires activation of the anaphase promoting complex (APC) (8), a ubiquitin ligase responsible for removal of cohesin at centromeres, and degradation of securin, cyclin A, cyclin B1, Aurora A, and cdc20 (9). PLK1 phosphorylation of the APC subunits Apc1, cdc16, and cdc27 has been demonstrated in vitro and has been proposed as a mechanism by which mitotic exit is regulated (10,11).Substitution of Thr210 with Asp has been reported to elevate PLK1 kinase activity and delay/arrest cells in mitosis, while a Ser137Asp substitution leads to S-phase arrest (12). In addition, while DNA damage has been found to inhibit PLK1 kinase activity, the Thr210Asp mutant is resistant to this inhibition (13). PLK1 has been reported to be phosphorylated in vivo at Ser137 and Thr210 in mitosis; DNA damage prevents phosphorylation at these sites (14).

$260
200 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: At least four distinct polo-like kinases exist in mammalian cells: PLK1, PLK2, PLK3, and PLK4/SAK (1). PLK1 apparently plays many roles during mitosis, particularly in regulating mitotic entry and exit. The mitosis promoting factor (MPF), cdc2/cyclin B1, is activated by dephosphorylation of cdc2 (Thr14/Tyr15) by cdc25C. PLK1 phosphorylates cdc25C at Ser198 and cyclin B1 at Ser133 causing translocation of these proteins from the cytoplasm to the nucleus (2-5). PLK1 phosphorylation of Myt1 at Ser426 and Thr495 has been proposed to inactivate Myt1, one of the kinases known to phosphorylate cdc2 at Thr14/Tyr15 (6). Polo-like kinases also phosphorylate the cohesin subunit SCC1, causing cohesin displacement from chromosome arms that allow for proper cohesin localization to centromeres (7). Mitotic exit requires activation of the anaphase promoting complex (APC) (8), a ubiquitin ligase responsible for removal of cohesin at centromeres, and degradation of securin, cyclin A, cyclin B1, Aurora A, and cdc20 (9). PLK1 phosphorylation of the APC subunits Apc1, cdc16, and cdc27 has been demonstrated in vitro and has been proposed as a mechanism by which mitotic exit is regulated (10,11).Substitution of Thr210 with Asp has been reported to elevate PLK1 kinase activity and delay/arrest cells in mitosis, while a Ser137Asp substitution leads to S-phase arrest (12). In addition, while DNA damage has been found to inhibit PLK1 kinase activity, the Thr210Asp mutant is resistant to this inhibition (13). PLK1 has been reported to be phosphorylated in vivo at Ser137 and Thr210 in mitosis; DNA damage prevents phosphorylation at these sites (14).

$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).

$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).