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Rat Kinetochore Organization and Biogenesis

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Structural maintenance of chromosomes 2 (SMC2) and 4 (SMC4) proteins are subunits of the condensin complex, which enables chromosome condensation and maintains the compaction of chromosomes as they separate to opposite poles during anaphase (1-3). In addition to regulating chromosome condensation, condensin is a general regulator of chromosome architecture and may function to regulate gene expression and DNA repair. SMC proteins contain a hallmark bipartite ATPase domain of the ABC ATPase superfamily, which consists of an N-terminal Walker A motif nucleotide-binding domain and C-terminal Walker B motif catalytic domain that interact to form a functional ATPase (1-3). The two ATPase domains are connected by two coiled coil domains separated by a central hinge region that facilitates protein-protein interactions between partnering SMC proteins. In the case of the condensin complex, SMC2 and SMC4 interact to form a functional ATPase required for chromatin condensation; however, the mechanism by which this ATPase activity regulates chromsome architecture is still being determined. In addition to SMC proteins, condensin contains three auxiliary subunits, which function to regulate condensin ATPase activity. Higher eukaryotes contain two distinct condensin complexes (condensin I and II), both of which contain SMC2 and SMC4 (1-3). Condensin I also contains the auxiliary subunits CAP-D2, CAP-G and CAP-H, while condensin II contains the related auxiliary proteins CAP-D3, CAP-G2 and CAP-H2. The two condensin complexes show different localization patterns during the cell cycle and on chromosomes and both are required for successful mitosis, suggesting distinct functions for each complex (1-3).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Structural maintenance of chromosomes 2 (SMC2) and 4 (SMC4) proteins are subunits of the condensin complex, which enables chromosome condensation and maintains the compaction of chromosomes as they separate to opposite poles during anaphase (1-3). In addition to regulating chromosome condensation, condensin is a general regulator of chromosome architecture and may function to regulate gene expression and DNA repair. SMC proteins contain a hallmark bipartite ATPase domain of the ABC ATPase superfamily, which consists of an N-terminal Walker A motif nucleotide-binding domain and C-terminal Walker B motif catalytic domain that interact to form a functional ATPase (1-3). The two ATPase domains are connected by two coiled coil domains separated by a central hinge region that facilitates protein-protein interactions between partnering SMC proteins. In the case of the condensin complex, SMC2 and SMC4 interact to form a functional ATPase required for chromatin condensation; however, the mechanism by which this ATPase activity regulates chromsome architecture is still being determined. In addition to SMC proteins, condensin contains three auxiliary subunits, which function to regulate condensin ATPase activity. Higher eukaryotes contain two distinct condensin complexes (condensin I and II), both of which contain SMC2 and SMC4 (1-3). Condensin I also contains the auxiliary subunits CAP-D2, CAP-G and CAP-H, while condensin II contains the related auxiliary proteins CAP-D3, CAP-G2 and CAP-H2. The two condensin complexes show different localization patterns during the cell cycle and on chromosomes and both are required for successful mitosis, suggesting distinct functions for each complex (1-3).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Structural maintenance of chromosomes 2 (SMC2) and 4 (SMC4) proteins are subunits of the condensin complex, which enables chromosome condensation and maintains the compaction of chromosomes as they separate to opposite poles during anaphase (1-3). In addition to regulating chromosome condensation, condensin is a general regulator of chromosome architecture and may function to regulate gene expression and DNA repair. SMC proteins contain a hallmark bipartite ATPase domain of the ABC ATPase superfamily, which consists of an N-terminal Walker A motif nucleotide-binding domain and C-terminal Walker B motif catalytic domain that interact to form a functional ATPase (1-3). The two ATPase domains are connected by two coiled coil domains separated by a central hinge region that facilitates protein-protein interactions between partnering SMC proteins. In the case of the condensin complex, SMC2 and SMC4 interact to form a functional ATPase required for chromatin condensation; however, the mechanism by which this ATPase activity regulates chromsome architecture is still being determined. In addition to SMC proteins, condensin contains three auxiliary subunits, which function to regulate condensin ATPase activity. Higher eukaryotes contain two distinct condensin complexes (condensin I and II), both of which contain SMC2 and SMC4 (1-3). Condensin I also contains the auxiliary subunits CAP-D2, CAP-G and CAP-H, while condensin II contains the related auxiliary proteins CAP-D3, CAP-G2 and CAP-H2. The two condensin complexes show different localization patterns during the cell cycle and on chromosomes and both are required for successful mitosis, suggesting distinct functions for each complex (1-3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Structural maintenance of chromosomes 2 (SMC2) and 4 (SMC4) proteins are subunits of the condensin complex, which enables chromosome condensation and maintains the compaction of chromosomes as they separate to opposite poles during anaphase (1-3). In addition to regulating chromosome condensation, condensin is a general regulator of chromosome architecture and may function to regulate gene expression and DNA repair. SMC proteins contain a hallmark bipartite ATPase domain of the ABC ATPase superfamily, which consists of an N-terminal Walker A motif nucleotide-binding domain and C-terminal Walker B motif catalytic domain that interact to form a functional ATPase (1-3). The two ATPase domains are connected by two coiled coil domains separated by a central hinge region that facilitates protein-protein interactions between partnering SMC proteins. In the case of the condensin complex, SMC2 and SMC4 interact to form a functional ATPase required for chromatin condensation; however, the mechanism by which this ATPase activity regulates chromsome architecture is still being determined. In addition to SMC proteins, condensin contains three auxiliary subunits, which function to regulate condensin ATPase activity. Higher eukaryotes contain two distinct condensin complexes (condensin I and II), both of which contain SMC2 and SMC4 (1-3). Condensin I also contains the auxiliary subunits CAP-D2, CAP-G and CAP-H, while condensin II contains the related auxiliary proteins CAP-D3, CAP-G2 and CAP-H2. The two condensin complexes show different localization patterns during the cell cycle and on chromosomes and both are required for successful mitosis, suggesting distinct functions for each complex (1-3).

$134
20 µl
$336
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Aurora kinases belong to a highly conserved family of mitotic serine/threonine kinases with three members identified among mammals: Aurora A, B, and C (1,2). Studies on the temporal expression pattern and subcellular localization of Aurora kinases in mitotic cells suggest an association with mitotic structure. Aurora kinase functional influences span from G2 phase to cytokinesis and may be involved in key cell cycle events such as centrosome duplication, chromosome bi-orientation and segregation, cleavage furrow positioning, and ingression (3). Aurora A is detected at the centrosomes, along mitotic spindle microtubules, and in the cytoplasm of mitotically proliferating cells. Aurora A protein levels are low during G1 and S phases and peak during the G2/M phase of the cell cycle. Phosphorylation of Aurora A at Thr288 in its catalytic domain increases kinase activity. Aurora A is involved in centrosome separation, maturation, and spindle assembly and stability. Expression of Aurora B protein also peaks during the G2/M phase of the cell cycle; Aurora B kinase activity peaks at the transition from metaphase to the end of mitosis. Aurora B associates with chromosomes during prophase prior to relocalizing to the spindle at anaphase. Aurora B regulates chromosome segregation through the control of microtubule-kinetochore attachment and cytokinesis. Expression of both Aurora A and Aurora B during the G2/M phase transition is tightly coordinated with histone H3 phosphorylation (4,5); research investigators have observed overexpression of these kinases in a variety of human cancers (2,4). Aurora C localizes to the centrosome from anaphase to cytokinesis and both mRNA and protein levels peak during G2/M phase. Although typical Aurora C expression is limited to the testis, research studies report overexpression of Aurora C is detected in various cancer cell lines (6).

$364
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 488 fluorescent dye and tested in-house for direct flow cytometric and immunofluorescent analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Phospho-Aurora A (Thr288)/Aurora B (Thr232)/Aurora C (Thr198) (D13A11) XP® Rabbit mAb #2914.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry

Background: Aurora kinases belong to a highly conserved family of mitotic serine/threonine kinases with three members identified among mammals: Aurora A, B, and C (1,2). Studies on the temporal expression pattern and subcellular localization of Aurora kinases in mitotic cells suggest an association with mitotic structure. Aurora kinase functional influences span from G2 phase to cytokinesis and may be involved in key cell cycle events such as centrosome duplication, chromosome bi-orientation and segregation, cleavage furrow positioning, and ingression (3). Aurora A is detected at the centrosomes, along mitotic spindle microtubules, and in the cytoplasm of mitotically proliferating cells. Aurora A protein levels are low during G1 and S phases and peak during the G2/M phase of the cell cycle. Phosphorylation of Aurora A at Thr288 in its catalytic domain increases kinase activity. Aurora A is involved in centrosome separation, maturation, and spindle assembly and stability. Expression of Aurora B protein also peaks during the G2/M phase of the cell cycle; Aurora B kinase activity peaks at the transition from metaphase to the end of mitosis. Aurora B associates with chromosomes during prophase prior to relocalizing to the spindle at anaphase. Aurora B regulates chromosome segregation through the control of microtubule-kinetochore attachment and cytokinesis. Expression of both Aurora A and Aurora B during the G2/M phase transition is tightly coordinated with histone H3 phosphorylation (4,5); research investigators have observed overexpression of these kinases in a variety of human cancers (2,4). Aurora C localizes to the centrosome from anaphase to cytokinesis and both mRNA and protein levels peak during G2/M phase. Although typical Aurora C expression is limited to the testis, research studies report overexpression of Aurora C is detected in various cancer cell lines (6).

$364
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 555 fluorescent dye and tested in-house for immunofluorescent analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Phospho-Aurora A (Thr288)/Aurora B (Thr232)/Aurora C (Thr198) (D13A11) XP® Rabbit mAb  #2914.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry)

Background: Aurora kinases belong to a highly conserved family of mitotic serine/threonine kinases with three members identified among mammals: Aurora A, B, and C (1,2). Studies on the temporal expression pattern and subcellular localization of Aurora kinases in mitotic cells suggest an association with mitotic structure. Aurora kinase functional influences span from G2 phase to cytokinesis and may be involved in key cell cycle events such as centrosome duplication, chromosome bi-orientation and segregation, cleavage furrow positioning, and ingression (3). Aurora A is detected at the centrosomes, along mitotic spindle microtubules, and in the cytoplasm of mitotically proliferating cells. Aurora A protein levels are low during G1 and S phases and peak during the G2/M phase of the cell cycle. Phosphorylation of Aurora A at Thr288 in its catalytic domain increases kinase activity. Aurora A is involved in centrosome separation, maturation, and spindle assembly and stability. Expression of Aurora B protein also peaks during the G2/M phase of the cell cycle; Aurora B kinase activity peaks at the transition from metaphase to the end of mitosis. Aurora B associates with chromosomes during prophase prior to relocalizing to the spindle at anaphase. Aurora B regulates chromosome segregation through the control of microtubule-kinetochore attachment and cytokinesis. Expression of both Aurora A and Aurora B during the G2/M phase transition is tightly coordinated with histone H3 phosphorylation (4,5); research investigators have observed overexpression of these kinases in a variety of human cancers (2,4). Aurora C localizes to the centrosome from anaphase to cytokinesis and both mRNA and protein levels peak during G2/M phase. Although typical Aurora C expression is limited to the testis, research studies report overexpression of Aurora C is detected in various cancer cell lines (6).

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

Application Methods: Flow Cytometry, Immunoprecipitation, Western Blotting

Background: Aurora A (AIK) is a cell cycle-regulated Ser/Thr protein kinase that is overexpressed in many tumor cell lines (1-3). Phosphorylation of Aurora A at Thr288 within the kinase activation loop results in a significant increase in its activity and may target the protein for proteasomal degradation during mitosis (4). The closely-related kinase Aurora B (AIM1) has been implicated in multiple mitotic events (5), and siRNA silencing of Aurora B expression results in reduced histone H3 phosphorylation, aberrant chromosome alignment/segregation, and altered survivin localization (6).

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

Application Methods: Western Blotting

Background: Rac and Cdc42 are members of the Rho-GTPase family. In mammals, Rac exists as three isoforms, Rac1, Rac2 and Rac3, which are highly similar in sequence. Rac1 and Cdc42, the most widely studied of this group, are ubiquitously expressed. Rac2 is expressed in cells of hematopoietic origin, and Rac3, while highly expressed in brain, is also found in many other tissues. Rac and Cdc42 play key signaling roles in cytoskeletal reorganization, membrane trafficking, transcriptional regulation, cell growth and development (1). GTP binding stimulates the activity of Rac/Cdc42, and the hydrolysis of GTP to GDP through the protein's intrinsic GTPase activity, rendering it inactive. GTP hydrolysis is aided by GTPase activating proteins (GAPs), while exchange of GDP for GTP is facilitated by guanine nucleotide exchange factors (GEFs). Another level of regulation is achieved through the binding of RhoGDI, a guanine nucleotide dissociation inhibitor, which retains Rho family GTPases, including Rac and Cdc42, in their inactive GDP-bound state (2,3).

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

Application Methods: Western Blotting

Background: Rac and Cdc42 are members of the Rho-GTPase family. In mammals, Rac exists as three isoforms, Rac1, Rac2 and Rac3, which are highly similar in sequence. Rac1 and Cdc42, the most widely studied of this group, are ubiquitously expressed. Rac2 is expressed in cells of hematopoietic origin, and Rac3, while highly expressed in brain, is also found in many other tissues. Rac and Cdc42 play key signaling roles in cytoskeletal reorganization, membrane trafficking, transcriptional regulation, cell growth and development (1). GTP binding stimulates the activity of Rac/Cdc42, and the hydrolysis of GTP to GDP through the protein's intrinsic GTPase activity, rendering it inactive. GTP hydrolysis is aided by GTPase activating proteins (GAPs), while exchange of GDP for GTP is facilitated by guanine nucleotide exchange factors (GEFs). Another level of regulation is achieved through the binding of RhoGDI, a guanine nucleotide dissociation inhibitor, which retains Rho family GTPases, including Rac and Cdc42, in their inactive GDP-bound state (2,3).

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

Application Methods: Western Blotting

Background: Rac and Cdc42 are members of the Rho-GTPase family. In mammals, Rac exists as three isoforms, Rac1, Rac2 and Rac3, which are highly similar in sequence. Rac1 and Cdc42, the most widely studied of this group, are ubiquitously expressed. Rac2 is expressed in cells of hematopoietic origin, and Rac3, while highly expressed in brain, is also found in many other tissues. Rac and Cdc42 play key signaling roles in cytoskeletal reorganization, membrane trafficking, transcriptional regulation, cell growth and development (1). GTP binding stimulates the activity of Rac/Cdc42, and the hydrolysis of GTP to GDP through the protein's intrinsic GTPase activity, rendering it inactive. GTP hydrolysis is aided by GTPase activating proteins (GAPs), while exchange of GDP for GTP is facilitated by guanine nucleotide exchange factors (GEFs). Another level of regulation is achieved through the binding of RhoGDI, a guanine nucleotide dissociation inhibitor, which retains Rho family GTPases, including Rac and Cdc42, in their inactive GDP-bound state (2,3).