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Human Response to Radiation

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: The cdc25 protein phosphatase family plays a critical role in activating cyclin-dependent kinases (CDKs) via dephosphorylation of conserved Thr14/Tyr15 inhibitory phosphorylation sites. While cdc25C is primarily responsible for activating CDK1 to overcome the G2/M checkpoint and allow mitotic entry, the primary substrate of cdc25A is CDK2, which, when active, allows progression through the G1/S and intra-S checkpoints (1). Abundance, subcellular localization and activity of cdc25A is tightly controlled by a variety of mechanisms, including phosphorylation, ubiquitination, and inhibitory binding to 14-3-3 proteins. During normal cell cycle progression, elevated c-Myc and E2F transcription factor levels lead to increased cdc25A expression (2). When conditions are favorable for DNA synthesis, cdc25A and CDK2 form an activation loop, wherein each activates the other enzyme (1). DNA damage, on the other hand, leads to multisite phosphorylation at inhibitory sites (Ser123, Ser177, Ser278, Ser292, and Thr506) by Chk1 and Chk2, which result in 14-3-3 binding and ubiquitin-mediated degradation (3,4).

$122
20 µl
$303
100 µl
$717
300 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Bcl-2 exerts a survival function in response to a wide range of apoptotic stimuli through inhibition of mitochondrial cytochrome c release (1). It has been implicated in modulating mitochondrial calcium homeostasis and proton flux (2). Several phosphorylation sites have been identified within Bcl-2 including Thr56, Ser70, Thr74, and Ser87 (3). It has been suggested that these phosphorylation sites may be targets of the ASK1/MKK7/JNK1 pathway and that phosphorylation of Bcl-2 may be a marker for mitotic events (4,5). Mutation of Bcl-2 at Thr56 or Ser87 inhibits its anti-apoptotic activity during glucocorticoid-induced apoptosis of T lymphocytes (6). Interleukin-3 and JNK-induced Bcl-2 phosphorylation at Ser70 may be required for its enhanced anti-apoptotic functions (7).

$327
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 analysis of human cells.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: Bcl-2 exerts a survival function in response to a wide range of apoptotic stimuli through inhibition of mitochondrial cytochrome c release (1). It has been implicated in modulating mitochondrial calcium homeostasis and proton flux (2). Several phosphorylation sites have been identified within Bcl-2 including Thr56, Ser70, Thr74, and Ser87 (3). It has been suggested that these phosphorylation sites may be targets of the ASK1/MKK7/JNK1 pathway and that phosphorylation of Bcl-2 may be a marker for mitotic events (4,5). Mutation of Bcl-2 at Thr56 or Ser87 inhibits its anti-apoptotic activity during glucocorticoid-induced apoptosis of T lymphocytes (6). Interleukin-3 and JNK-induced Bcl-2 phosphorylation at Ser70 may be required for its enhanced anti-apoptotic functions (7).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Bcl-2 exerts a survival function in response to a wide range of apoptotic stimuli through inhibition of mitochondrial cytochrome c release (1). It has been implicated in modulating mitochondrial calcium homeostasis and proton flux (2). Several phosphorylation sites have been identified within Bcl-2 including Thr56, Ser70, Thr74, and Ser87 (3). It has been suggested that these phosphorylation sites may be targets of the ASK1/MKK7/JNK1 pathway and that phosphorylation of Bcl-2 may be a marker for mitotic events (4,5). Mutation of Bcl-2 at Thr56 or Ser87 inhibits its anti-apoptotic activity during glucocorticoid-induced apoptosis of T lymphocytes (6). Interleukin-3 and JNK-induced Bcl-2 phosphorylation at Ser70 may be required for its enhanced anti-apoptotic functions (7).

$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 cytometric analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Bcl-2 (124) Mouse mAb #15071.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: Bcl-2 exerts a survival function in response to a wide range of apoptotic stimuli through inhibition of mitochondrial cytochrome c release (1). It has been implicated in modulating mitochondrial calcium homeostasis and proton flux (2). Several phosphorylation sites have been identified within Bcl-2 including Thr56, Ser70, Thr74, and Ser87 (3). It has been suggested that these phosphorylation sites may be targets of the ASK1/MKK7/JNK1 pathway and that phosphorylation of Bcl-2 may be a marker for mitotic events (4,5). Mutation of Bcl-2 at Thr56 or Ser87 inhibits its anti-apoptotic activity during glucocorticoid-induced apoptosis of T lymphocytes (6). Interleukin-3 and JNK-induced Bcl-2 phosphorylation at Ser70 may be required for its enhanced anti-apoptotic functions (7).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 647 fluorescent dye and tested in-house for direct flow cytometric analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Bcl-2 (124) Mouse mAb #15071.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: Bcl-2 exerts a survival function in response to a wide range of apoptotic stimuli through inhibition of mitochondrial cytochrome c release (1). It has been implicated in modulating mitochondrial calcium homeostasis and proton flux (2). Several phosphorylation sites have been identified within Bcl-2 including Thr56, Ser70, Thr74, and Ser87 (3). It has been suggested that these phosphorylation sites may be targets of the ASK1/MKK7/JNK1 pathway and that phosphorylation of Bcl-2 may be a marker for mitotic events (4,5). Mutation of Bcl-2 at Thr56 or Ser87 inhibits its anti-apoptotic activity during glucocorticoid-induced apoptosis of T lymphocytes (6). Interleukin-3 and JNK-induced Bcl-2 phosphorylation at Ser70 may be required for its enhanced anti-apoptotic functions (7).

$262
3 nmol
300 µl
SignalSilence® Bcl-2 siRNA I from Cell Signaling Technology (CST) allows the researcher to specifically inhibit Bcl-2 expression using RNA interference, a method whereby gene expression can be selectively silenced through the delivery of double stranded RNA molecules into the cell. All SignalSilence® siRNA products from CST are rigorously tested in-house and have been shown to reduce target protein expression by western analysis.
REACTIVITY
Human

Background: Bcl-2 exerts a survival function in response to a wide range of apoptotic stimuli through inhibition of mitochondrial cytochrome c release (1). It has been implicated in modulating mitochondrial calcium homeostasis and proton flux (2). Several phosphorylation sites have been identified within Bcl-2 including Thr56, Ser70, Thr74, and Ser87 (3). It has been suggested that these phosphorylation sites may be targets of the ASK1/MKK7/JNK1 pathway and that phosphorylation of Bcl-2 may be a marker for mitotic events (4,5). Mutation of Bcl-2 at Thr56 or Ser87 inhibits its anti-apoptotic activity during glucocorticoid-induced apoptosis of T lymphocytes (6). Interleukin-3 and JNK-induced Bcl-2 phosphorylation at Ser70 may be required for its enhanced anti-apoptotic functions (7).

$262
3 nmol
300 µl
SignalSilence® Bcl-2 siRNA II allows the researcher to specifically inhibit Bcl-2 expression using RNA interference, a method whereby gene expression can be selectively silenced through the delivery of double stranded RNA molecules into the cell. All SignalSilence® siRNA products are rigorously tested in-house and have been shown to reduce target protein expression by western analysis.
REACTIVITY
Human

Background: Bcl-2 exerts a survival function in response to a wide range of apoptotic stimuli through inhibition of mitochondrial cytochrome c release (1). It has been implicated in modulating mitochondrial calcium homeostasis and proton flux (2). Several phosphorylation sites have been identified within Bcl-2 including Thr56, Ser70, Thr74, and Ser87 (3). It has been suggested that these phosphorylation sites may be targets of the ASK1/MKK7/JNK1 pathway and that phosphorylation of Bcl-2 may be a marker for mitotic events (4,5). Mutation of Bcl-2 at Thr56 or Ser87 inhibits its anti-apoptotic activity during glucocorticoid-induced apoptosis of T lymphocytes (6). Interleukin-3 and JNK-induced Bcl-2 phosphorylation at Ser70 may be required for its enhanced anti-apoptotic functions (7).

$115
20 µl
$269
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Bcl-2 exerts a survival function in response to a wide range of apoptotic stimuli through inhibition of mitochondrial cytochrome c release (1). It has been implicated in modulating mitochondrial calcium homeostasis and proton flux (2). Several phosphorylation sites have been identified within Bcl-2 including Thr56, Ser70, Thr74, and Ser87 (3). It has been suggested that these phosphorylation sites may be targets of the ASK1/MKK7/JNK1 pathway and that phosphorylation of Bcl-2 may be a marker for mitotic events (4,5). Mutation of Bcl-2 at Thr56 or Ser87 inhibits its anti-apoptotic activity during glucocorticoid-induced apoptosis of T lymphocytes (6). Interleukin-3 and JNK-induced Bcl-2 phosphorylation at Ser70 may be required for its enhanced anti-apoptotic functions (7).

$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. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Bcl-2 (124) Mouse mAb #15071.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: Bcl-2 exerts a survival function in response to a wide range of apoptotic stimuli through inhibition of mitochondrial cytochrome c release (1). It has been implicated in modulating mitochondrial calcium homeostasis and proton flux (2). Several phosphorylation sites have been identified within Bcl-2 including Thr56, Ser70, Thr74, and Ser87 (3). It has been suggested that these phosphorylation sites may be targets of the ASK1/MKK7/JNK1 pathway and that phosphorylation of Bcl-2 may be a marker for mitotic events (4,5). Mutation of Bcl-2 at Thr56 or Ser87 inhibits its anti-apoptotic activity during glucocorticoid-induced apoptosis of T lymphocytes (6). Interleukin-3 and JNK-induced Bcl-2 phosphorylation at Ser70 may be required for its enhanced anti-apoptotic functions (7).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: PNK (polynucleotide kinase) is a DNA repair enzyme that participates in single strand break repair and non-homologous end rejoining (NHEJ) for double strand breaks. PNK possesses a 5'-DNA kinase activity and a 3'-DNA phosphatase activity (1,2). It has three domains, a C-terminal kinase domain, a central phosphatase domain, and an N-terminal forkhead associated (FHA) domain that is responsible for protein-protein interactions. Reduction in expression of PNK by RNAi sensitizes cells to ionizing radiation and topoisomerase I inhibitors (3)

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Structural maintenance of chromosomes 1 (SMC1) protein is a chromosomal protein member of the cohesin complex that enables sister chromatid cohesion and plays a role in DNA repair (1,2). ATM/NBS1-dependent phosphorylation of SMC1 occurs at Ser957 and Ser966 in response to ionizing radiation (IR) as part of the intra-S-phase DNA damage checkpoint (3). SMC1 phosphorylation is ATM-independent in cells subjected to other forms of DNA damage, including UV light and hydroxyurea treatment (4). While phosphorylation of SMC1 is required for activation of the IR-induced intra-S-phase checkpoint, the precise mechanism is not well understood and may involve a conformational change that affects SMC1-SMC3 interaction (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Thioredoxin is a small redox protein found in many eukaryotes and prokaryotes. A pair of cysteines within a highly conserved, active site sequence can be oxidized to form a disulfide bond that is then reduced by thioredoxin reductase (1). Multiple forms of thioredoxin have been identified, including cytosolic thioredoxin 1 (TRX1) and mitochondrial thioredoxin 2 (TRX2). Thioredoxin participates in many cellular processes including redox signaling, response to oxidative stress, and protein reduction (1). A potential role of thioredoxin in human disorders such as cancer, aging, and heart disease is currently under investigation (2). Thioredoxin can play a key role in cancer progression, because it acts as a negative regulator of the proapoptotic kinase ASK1 (3). Changes in thioredoxin expression have been associated with meningococcal septic shock and acute lung injury (4,5).

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

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

Background: Methyl-CpG-binding protein 2 (MeCP2) is the founding member of a family of methyl-CpG-binding domain (MBD) proteins that also includes MBD1, MBD2, MBD3, MBD4, MBD5 and MBD6 (1-3). Apart from MBD3, these proteins bind methylated cytosine residues in the context of the di-nucleotide 5´-CG-3´ to establish and maintain regions of transcriptionally inactive chromatin by recruiting a variety of co-repressor proteins (2). MeCP2 recruits histone deacetylases HDAC1 and HDAC2, and the DNA methyltransferase DNMT1 (4-6). MBD1 couples transcriptional silencing to DNA replication and interacts with the histone methyltransferases ESET and SUV39H1 (7,8). MBD2 and MBD3 co-purify as part of the NuRD (nucleosome remodeling and histone de-acetylation) co-repressor complex, which contains the chromatin remodeling ATPase Mi-2, HDAC1 and HDAC2 (9,10). MBD5 and MBD6 have recently been identified and little is known regarding their protein interactions. MBD proteins are associated with cancer and other diseases; MBD4 is best characterized for its role in DNA repair and MBD2 has been linked to intestinal cancer (11,12). Mutations in the MeCP2 gene cause the neurologic developmental disorder Rett Syndrome (13). MeCP2 protein levels are high in neurons, where it plays a critical role in multiple synaptic processes (14). In response to various physiological stimuli, MeCP2 is phosphorylated on Ser421 and regulates the expression of genes controlling dendritic patterning and spine morphogenesis (14). Disruption of this process in individuals with altered MeCP2 may cause the pathological changes seen in Rett Syndrome.

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Structural maintenance of chromosomes 1 (SMC1) protein is a chromosomal protein member of the cohesin complex that enables sister chromatid cohesion and plays a role in DNA repair (1,2). ATM/NBS1-dependent phosphorylation of SMC1 occurs at Ser957 and Ser966 in response to ionizing radiation (IR) as part of the intra-S-phase DNA damage checkpoint (3). SMC1 phosphorylation is ATM-independent in cells subjected to other forms of DNA damage, including UV light and hydroxyurea treatment (4). While phosphorylation of SMC1 is required for activation of the IR-induced intra-S-phase checkpoint, the precise mechanism is not well understood and may involve a conformational change that affects SMC1-SMC3 interaction (3).

$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 unconjugated antibody #4545 reacts with keratins 4, 5, 6, 8, 10, 13 and 18 from human, rat and monkey. CST expects that Pan-Keratin (C11) Mouse mAb (Alexa Fluor® 488 Conjugate) will also recognize the same keratins in these species.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

Background: Keratins (cytokeratins) are intermediate filament proteins that are mainly expressed in epithelial cells. Keratin heterodimers composed of an acidic keratin (or type I keratin, keratins 9 to 23) and a basic keratin (or type II keratin, keratins 1 to 8) assemble to form filaments (1,2). Keratin isoforms demonstrate tissue- and differentiation-specific profiles that make them useful as research biomarkers (1). Research studies have shown that mutations in keratin genes are associated with skin disorders, liver and pancreatic diseases, and inflammatory intestinal diseases (3-6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Structural maintenance of chromosomes 1 (SMC1) protein is a chromosomal protein member of the cohesin complex that enables sister chromatid cohesion and plays a role in DNA repair (1,2). ATM/NBS1-dependent phosphorylation of SMC1 occurs at Ser957 and Ser966 in response to ionizing radiation (IR) as part of the intra-S-phase DNA damage checkpoint (3). SMC1 phosphorylation is ATM-independent in cells subjected to other forms of DNA damage, including UV light and hydroxyurea treatment (4). While phosphorylation of SMC1 is required for activation of the IR-induced intra-S-phase checkpoint, the precise mechanism is not well understood and may involve a conformational change that affects SMC1-SMC3 interaction (3).

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

Application Methods: Western Blotting

Background: The cohesin complex consists of a heterodimer between SMC1 (SMC1A or B) and SMC3, bound by additional RAD21 and STAG proteins (STAG1, 2, or 3) (1,2). These proteins form a ring-like structure that mediates the cohesion of two sister chromatids after DNA replication in S phase (1,2). RAD21 and STAG2 are phosphorylated by Polo-like kinase (PLK) during prophase, which leads to the dissociation of cohesin complexes from the chromosome arms; however, cohesin remains bound to centromeres until anaphase (3,4). RAD21 is cleaved by separin/ESPL1 in anaphase, which leads to dissociation of the remaining cohesin from centromeres, enabling sister chromatids to segregate during mitosis (5). RAD21 is also cleaved by caspase-3 and caspase-7 during apoptosis, resulting in a 64 kDa carboxy-terminal cleavage product that translocates to the cytoplasm and may help to trigger apoptosis (6,7). In addition to mediating cohesion of sister chromatids, the cohesin complex plays important roles in gene regulation and DNA repair, as SMC1 and SMC3 are both phosphorylated by ATM and ATR kinases upon DNA damage (1,2).

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

Application Methods: Western Blotting

Background: Wild-type p53 induced phosphatase 1 (WIP1)/protein phosphatase magnesium-dependent 1 delta (ppm1d) is a member of the PP2C family of serine/threonine protein phosphatases. WIP1 was initially identified as a p53 target gene, induced in response to ionizing radiation (1). Studies have shown that WIP1 is overexpressed in human cancers and is involved in the regulation of multiple DNA damage signaling pathways (reviewed in 2,3). WIP1 functions in returning cells to a homeostatic state following DNA damage (4,5), as well as in maintaining p53-dependent homeostasis under nonstress conditions (6). Researchers have shown that increased expression of WIP1 is associated with poor prognosis and lower survival rate in some human cancers (7,8). In contrast, overexpression of WIP1 in p53-negative tumor cells sensitizes them to chemotherapy-induced apoptosis while protecting normal tissue during treatment (9).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Structural maintenance of chromosomes 1 (SMC1) protein is a chromosomal protein member of the cohesin complex that enables sister chromatid cohesion and plays a role in DNA repair (1,2). ATM/NBS1-dependent phosphorylation of SMC1 occurs at Ser957 and Ser966 in response to ionizing radiation (IR) as part of the intra-S-phase DNA damage checkpoint (3). SMC1 phosphorylation is ATM-independent in cells subjected to other forms of DNA damage, including UV light and hydroxyurea treatment (4). While phosphorylation of SMC1 is required for activation of the IR-induced intra-S-phase checkpoint, the precise mechanism is not well understood and may involve a conformational change that affects SMC1-SMC3 interaction (3).