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Monoclonal Antibody Origin Recognition Complex

Also showing Monoclonal Antibody Nuclear Origin of Replication Recognition Complex

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: The origin recognition complex (ORC) is a highly conserved heterohexameric protein complex that associates with DNA at or near initiation of DNA replication sites. All six ORC subunits are essential for initiation of DNA replication (1-3), and ORC may be involved in regulation of gene expression in response to stress (4). ORC binding to DNA permits the ordered binding of other proteins such as cdc6 and MCMs to form pre-replication complexes (Pre-RCs). Pre-RCs form between telophase and early G1 phase of the cell cycle and are inactivated at the onset of DNA synthesis, allowing coordinated regulation of DNA replication and cell division (5). Modification of one or more of the six ORC subunits may be responsible for its inactivation during S phase, but the chromatin binding behavior of the ORC subunits during the cell division cycle is still under investigation (6-7).

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

Application Methods: Western Blotting

Background: The origin recognition complex (ORC) is a highly conserved heterohexameric protein complex that associates with DNA at or near initiation of DNA replication sites. All six ORC subunits are essential for initiation of DNA replication (1-3), and ORC may be involved in regulation of gene expression in response to stress (4). ORC binding to DNA permits the ordered binding of other proteins such as cdc6 and MCMs to form pre-replication complexes (Pre-RCs). Pre-RCs form between telophase and early G1 phase of the cell cycle and are inactivated at the onset of DNA synthesis, allowing coordinated regulation of DNA replication and cell division (5). Modification of one or more of the six ORC subunits may be responsible for its inactivation during S phase, but the chromatin binding behavior of the ORC subunits during the cell division cycle is still under investigation (6-7).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The origin recognition complex (ORC) is a highly conserved heterohexameric protein complex that associates with DNA at or near initiation of DNA replication sites. All six ORC subunits are essential for initiation of DNA replication (1-3), and ORC may be involved in regulation of gene expression in response to stress (4). ORC binding to DNA permits the ordered binding of other proteins such as cdc6 and MCMs to form pre-replication complexes (Pre-RCs). Pre-RCs form between telophase and early G1 phase of the cell cycle and are inactivated at the onset of DNA synthesis, allowing coordinated regulation of DNA replication and cell division (5). Modification of one or more of the six ORC subunits may be responsible for its inactivation during S phase, but the chromatin binding behavior of the ORC subunits during the cell division cycle is still under investigation (6-7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: The minichromosome maintenance (MCM) 2-7 proteins are a family of six related proteins required for initiation and elongation of DNA replication. MCM2-7 bind together to form the heterohexameric MCM complex that is thought to act as a replicative helicase at the DNA replication fork (1-5). This complex is a key component of the pre-replication complex (pre-RC) (reviewed in 1). Cdc6 and CDT1 recruit the MCM complex to the origin recognition complex (ORC) during late mitosis/early G1 phase forming the pre-RC and licensing the DNA for replication (reviewed in 2). Licensing of the chromatin permits the DNA to replicate only once per cell cycle, thereby helping to ensure that genetic alterations and malignant cell growth do not occur (reviewed in 3). Phosphorylation of the MCM2, MCM3, MCM4, and MCM6 subunits appears to regulate MCM complex activity and the initiation of DNA synthesis (6-8). CDK1 phosphorylation of MCM3 at Ser112 during late mitosis/early G1 phase has been shown to initiate complex formation and chromatin loading in vitro (8). Phosphorylation of MCM2 at serine 139 by cdc7/dbf4 coincides with the initiation of DNA replication (9). MCM proteins are removed during DNA replication, causing chromatin to become unlicensed through inhibition of pre-RC reformation. Studies have shown that the MCM complex is involved in checkpoint control by protecting the structure of the replication fork and assisting in restarting replication by recruiting checkpoint proteins after arrest (reviewed in 3,10).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Chromatin IP, Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: The minichromosome maintenance (MCM) 2-7 proteins are a family of six related proteins required for initiation and elongation of DNA replication. MCM2-7 bind together to form the heterohexameric MCM complex that is thought to act as a replicative helicase at the DNA replication fork (1-5). This complex is a key component of the pre-replication complex (pre-RC) (reviewed in 1). Cdc6 and CDT1 recruit the MCM complex to the origin recognition complex (ORC) during late mitosis/early G1 phase forming the pre-RC and licensing the DNA for replication (reviewed in 2). Licensing of the chromatin permits the DNA to replicate only once per cell cycle, thereby helping to ensure that genetic alterations and malignant cell growth do not occur (reviewed in 3). Phosphorylation of the MCM2, MCM3, MCM4, and MCM6 subunits appears to regulate MCM complex activity and the initiation of DNA synthesis (6-8). CDK1 phosphorylation of MCM3 at Ser112 during late mitosis/early G1 phase has been shown to initiate complex formation and chromatin loading in vitro (8). Phosphorylation of MCM2 at serine 139 by cdc7/dbf4 coincides with the initiation of DNA replication (9). MCM proteins are removed during DNA replication, causing chromatin to become unlicensed through inhibition of pre-RC reformation. Studies have shown that the MCM complex is involved in checkpoint control by protecting the structure of the replication fork and assisting in restarting replication by recruiting checkpoint proteins after arrest (reviewed in 3,10).

$336
100 µl
APPLICATIONS
REACTIVITY
Dog, Hamster, Human, Monkey, Mouse, Rat

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

Background: The minichromosome maintenance (MCM) 2-7 proteins are a family of six related proteins required for initiation and elongation of DNA replication. MCM2-7 bind together to form the heterohexameric MCM complex that is thought to act as a replicative helicase at the DNA replication fork (1-5). This complex is a key component of the pre-replication complex (pre-RC) (reviewed in 1). Cdc6 and CDT1 recruit the MCM complex to the origin recognition complex (ORC) during late mitosis/early G1 phase forming the pre-RC and licensing the DNA for replication (reviewed in 2). Licensing of the chromatin permits the DNA to replicate only once per cell cycle, thereby helping to ensure that genetic alterations and malignant cell growth do not occur (reviewed in 3). Phosphorylation of the MCM2, MCM3, MCM4, and MCM6 subunits appears to regulate MCM complex activity and the initiation of DNA synthesis (6-8). CDK1 phosphorylation of MCM3 at Ser112 during late mitosis/early G1 phase has been shown to initiate complex formation and chromatin loading in vitro (8). Phosphorylation of MCM2 at serine 139 by cdc7/dbf4 coincides with the initiation of DNA replication (9). MCM proteins are removed during DNA replication, causing chromatin to become unlicensed through inhibition of pre-RC reformation. Studies have shown that the MCM complex is involved in checkpoint control by protecting the structure of the replication fork and assisting in restarting replication by recruiting checkpoint proteins after arrest (reviewed in 3,10).