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Product listing: Securin (D2B6O) Rabbit mAb, UniProt ID O95997 #13445 to WIP1 (D4F7) Rabbit mAb, UniProt ID O15297 #11901

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Securin is a regulatory protein that contributes to mitotic checkpoint control, p53 activity, DNA repair, and cell migration. The securin protein prevents premature separation of sister chromatids by inhibiting the protease separase, which cleaves the cohesin complex at the onset of anaphase to allow for sister chromatid segregation (1,2). In mouse oocytes, securin regulates cyclin B stability and G2/M transition (3). Securin negatively affects the transcriptional activity of p53, preventing p53-regulated apoptosis (4). Research studies indicate that securin plays a role in microtubule nucleation, cell polarization, and cell migration (5). Additional research indicates that securin expression may be useful as a biomarker for human breast cancer (6-8). The pituitary tumor-transforming gene 1 (PTTG1) encodes for securin protein, while the highly homologous securin 2 protein is transcribed from the related PTTG2 gene. Securin 2 (PTTG2) protein lacks the ability to inhibit separase activity and may function primarily in cell adhesion and migration (9,10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: The Sestrin family of proteins, which comprises sestrin-1 (PA26), sestrin-2 (Hi95), and sestrin-3, plays an important role in regulating the cellular response to oxidative stress. Sestrin-1 and -2, both transcriptional targets of p53, have been shown to activate AMPK activity toward TSC2, ultimately resulting in the inhibition of mTOR (1). Thus, sestrin-1 and -2 link p53 signaling to the regulation of cellular growth (2). Sestrins have also been shown to function as modulators of cellular hydrogen peroxide concentration. Hydrogen peroxide is an important signaling molecule that is highly genotoxic and must therefore be tightly regulated (3). 2-Cys peroxiredoxins are metabolizing enzymes that maintain low cellular concentrations of hydrogen peroxide, but are hyperoxidized to an inactive state by a rapid increase in concentration (4) before quickly being reduced back to their active state by sestrins (5). This allows a hydrogen peroxide signal to temporarily circumvent the protective activity of 2-Cys peroxiredoxins, while minimizing oxidative damage.

$269
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, IHC-Leica® Bond™, Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: SLFN11 is a nuclear protein that belongs to the Schlafen (SLFN) family of genes involved in cell cycle regulation and growth inhibition (1, 2). Expression of SLFN11 predicts sensitivity of cancer cell lines to DNA-damaging agents (1, 3). Evidence suggests that in the presence of DNA-targeted therapies, SLFN11 is recruited to stressed replication forks where it blocks replication leading to cell death (4). SLFN11 is being explored as a predictive biomarker for response to DNA-targeted therapies (5).

$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: 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).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Immunoprecipitation, 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: 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).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: SMG-1 is a member of the phosphoinositide 3-kinase-related kinase (PIKK) family, which includes ATM, ATR, mTOR, DNA-PKcs, and TRRAP (1,2). Activated by DNA damage, SMG-1 has been shown to phosphorylate p53 and hUpf1 (SMG-2) (1-4). hUpf1 is a subunit of the surveillance complex that allows degradation of messenger RNA species containing premature termination codons (PTCs). This process, known as nonsense-mediated mRNA decay (NMD), prevents the translation of truncated forms of proteins that may result in gain of function or dominant negative species. NMD occurs under normal cellular conditions as well as in response to damage (5,6). SMG-1 has also been shown to affect cell death receptor signaling and to protect cells from extrinsically induced apoptotic cell death (7).

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

Application Methods: Chromatin IP, Immunofluorescence (Immunocytochemistry), Immunoprecipitation, 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).

$293
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Transforming acid coiled-coil (TACC) proteins are a family of proteins characterized by a common coiled-coil motif of approximately 200 amino acids at the carboxy-terminal end (1). Three family members have been identified in humans: TACC1, TACC2, and TACC3. These proteins are thought to be involved in centrosomal microtubule assembly and have been mapped to chromosomal regions that are disrupted in some cancers (reviewed in 2). TACC3 has been shown to be upregulated in many cancer cell lines (3). When phosphorylated at Ser558 by Aurora A, mammalian TACC3 is localized to mitotic spindles and increases microtubule stability (4,5). For this reason, it has been suggested that monitoring the localization of phosphorylated TACC3 would be an effective way to determine the efficacy of Aurora A inhibitors that show promise as anti-cancer drugs (6,7). In addition, studies have shown that TACC3 could be useful as a prognostic marker for non-small cell lung cancer (8).

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

Application Methods: Western Blotting

Background: Translationally controlled tumor protein (TCTP/p23/HRF) is a ubiquitously expressed and highly conserved protein involved in various cellular processes, such as its role as a histamine releasing factor in chronic allergic disease (1). TCTP binds tubulin in a cell cycle dependent manner and is associated with the mitotic spindle (2). In addition, TCTP interacts with the actin cytoskeleton to regulate cell shape (3). In mitosis, TCTP is phosphorylated by PLK at Ser46, decreasing microtubule stability (4,5). TCTP interacts with the small GTPase Rheb, possibly acting as a GEF, thereby activating the TORC1 pathway and controlling cell growth and proliferation (6,7). TCTP has also been shown to be involved in apoptosis and cell stress (8-11). In cultured cells, reduction in TCTP expression can cause loss of the malignant phenotype (12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Topoisomerases are ubiquitous, conserved enzymes that remove DNA supercoils resulting from processes such as chromosome segregation, DNA replication, transcription, and repair (1). Topoisomerase inhibitors such as camptothecin and etoposide trap the enzyme as a DNA-bound intermediate, and these drugs are used to treat multiple human cancers (1,2). Tyrosyl-DNA-phosphodiesterases TDP1 and TDP2 function in the base excision repair (BER) and nonhomologous end joining (NHEJ) DNA repair pathways, respectively, and function in part in the repair of stalled topoisomerase-DNA complexes (3). Research has shown that inhibitors of tyrosyl-DNA-phosphodiesterases may act synergistically with topoisomerase inhibitors, allowing the potential for a more robust treatment of cancer (4,5). In small cell lung cancer, research suggests that TDP1 and topoisomerase 1 levels can predict sensitivity to topoisomerase 1 inhibitors (6).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Telomeric repeat-binding factor 2-interacting protein (TERF2IP, also known as RAP1) is a component of the Shelterin Complex, a multi-protein complex that binds and organizes telomeres into T-loop structures to prevent them from being recognized by the cell as DNA double stranded breaks (1,2). The Shelterin Complex is composed of TERF2IP, TIN2 and TPP2 proteins, in addition to three DNA binding proteins that function to recruit the complex to telomeres: TRF1 and TRF2 bind double-stranded TTAGGG repeats found at telomeres, while the POT1 protein binds single-stranded TTAGGG repeats found at the very end of the telomeres (2). Together, these proteins function to protect telomeres and ensure proper replication and processing of chromosome ends. Recent studies have shown that TERF2IP is dispensable for maintenance of telomere length, organization of telomeric chromatin, and regulation of telomeric transcription (3,4). However, TERF2IP is required for inhibition of homology-directed repair (HDR), which can create undesirable telomeric sister chromatid exchange (3,4). In addition to its role in telomere maintenance, TERF2IP is also found in the cytoplasm, where it functions as an IκB kinase (IKK) adaptor protein and regulates NF-κB-dependent gene expression (5). TERF2IP forms a complex with IKKs and is critical for proper recruitment of IKKs to and activation of the p65 subunit of NF-κB. Elevated levels of TERF2IP have been found in breast cancer cells with NF-κB hyperactivity, and knockdown of TERF2IP sensitizes these cells to apoptosis, further identifying TERF2IP as a potential cancer therapeutic target (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The transcription factor CP2 (TFCP2, LSF) is a ubiquitous nuclear protein that was initially shown to bind and activate the alpha-globin promoter in erythroid cells (1). Research studies show that TFCP2 functions as an oncogene in hepatocellular carcinoma (HCC) cells. Overexpression of TFCP2 is seen in HCC patient samples and cell lines; TFCP2 expression correlates with high tumor grade and poor prognosis (2). Forced expression of TFCP2 in less aggressive HCC cells results in highly aggressive, angiogenic and metastatic tumors, while inhibition of TFCP2 abrogates growth and metastasis of highly aggressive HCC cells (2). Additional studies show that TFCP2 acts downstream of Notch1 in HCC cells, where it mediates Notch pathway signaling during proliferation and invasion of hepatocellular carcinoma (3). TFCP2 functions as an oncogene as it upregulates multiple genes involved in angiogenesis, cell invasion, and chemoresistance, including osteopontin, metalloproteinase-9, fibronectin 1, tight junction protein 1, and thymidylate synthase (2-5). Factor quinolinone inhibitor 1 (FQI1) is a small molecule inhibitor of TFCP2 that inhibits TFCP2 DNA-binding activity, reduces expression of TFCP2 target genes, and rapidly induces cell death in TFCP2-overexpressing HCC cell lines (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: TIF1β is a member of the TIF1 (transcriptional intermediary factor 1) family, a group of transcriptional regulators that play key roles in development and differentiation. Members of this family are characterized by the presence of two conserved motifs – an N-terminal RING-B box-coiled-coil motif and a C-terminal PHD finger and bromodomain unit (1,2). TIF1β is a corepressor for KRAB (Kruppel associated box) domain containing zinc finger proteins. The KRAB domain containing zinc finger proteins are a large group of transcription factors that are vertebrate-specific, varied in their expression patterns between species, and thought to regulate gene transcription programs that control speciation (3,4).TIF1β has been shown to be essential for early embryonic development and spermatogenesis (6,5). It functions to either activate or repress transcription in response to environmental or developmental signals by chromatin remodeling and histone modification. The recruitment and association of TIF1β with heterochromatin protein (HP1) is essential for transcriptional repression, and for progression through differentiation of F9 embryonic carcinoma cells (6,7). TIF1β also plays a role in the DNA damage response. Phosphorylation of TIF1β on Ser842 occurs in an ATM-dependent manner in response to genotoxic stress and is thought to be essential for chromatin relaxation, which is in turn required for the DNA damage response (8).

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

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

Background: TIF1β is a member of the TIF1 (transcriptional intermediary factor 1) family, a group of transcriptional regulators that play key roles in development and differentiation. Members of this family are characterized by the presence of two conserved motifs – an N-terminal RING-B box-coiled-coil motif and a C-terminal PHD finger and bromodomain unit (1,2). TIF1β is a corepressor for KRAB (Kruppel associated box) domain containing zinc finger proteins. The KRAB domain containing zinc finger proteins are a large group of transcription factors that are vertebrate-specific, varied in their expression patterns between species, and thought to regulate gene transcription programs that control speciation (3,4).TIF1β has been shown to be essential for early embryonic development and spermatogenesis (6,5). It functions to either activate or repress transcription in response to environmental or developmental signals by chromatin remodeling and histone modification. The recruitment and association of TIF1β with heterochromatin protein (HP1) is essential for transcriptional repression, and for progression through differentiation of F9 embryonic carcinoma cells (6,7). TIF1β also plays a role in the DNA damage response. Phosphorylation of TIF1β on Ser842 occurs in an ATM-dependent manner in response to genotoxic stress and is thought to be essential for chromatin relaxation, which is in turn required for the DNA damage response (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The p53 tumor suppressor protein regulates the cellular response to multiple stresses, including DNA damage and oxidative stress. Activation of p53 can lead to cell cycle arrest and DNA repair, or apoptosis (1). Activated p53 transcription factor regulates the expression of multiple genes that regulate cell metabolism and the cell cycle. One p53-inducible gene is C12orf5, which encodes for a fructose-2,6-bisphosphatase known as TIGAR. TP53-inducible glycolysis and apoptosis regulator (TIGAR) protects cells from oxidative stress as it negatively regulates glycolysis and reduces the production of reactive oxygen species (ROS) in cells (2,3). Research studies demonstrate that knockdown of TIGAR expression induces autophagy and apoptosis (4,5), and its expression protects cells from ROS-related cell death (6,7). Additional studies show that TIGAR promotes cell cycle arrest and supports dephosphorylation of the retinoblastoma (Rb) protein (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Topoisomerase II Binding Protein 1 (TopBP1) contains eight BRCT domains, which facilitate interaction with various proteins, phosphopeptides, and DNA. Through these interactions, TopBP1 functions in the regulation of DNA replication, DNA repair, checkpoint control, and transcription (1). TopBP1 contacts the checkpoint kinase ATR and its binding partner ATRIP, and induces ATR and Chk1 activation in collaboration with claspin (2,3). Activation of ATR is dependent on recruitment of TopBP1 through the MRN (MRE11-RAD50-NBS1) complex, and the 911 (RAD9-RAD1-HUS1) complex is required for full activation (4). TopBP1 stabilizes Bloom syndrome helicase (BLM) during S phase of the cell cycle to suppress sister chromatin exchange and maintain genome stability (5).TopBP1 also regulates initiation of DNA replication along with the DNA replication factor treslin (6,7). TopBP1 has been shown to prevent replication associated DNA damage during neurogenesis (8), and to interact with mutant p53, mediating mutant p53 gain-of-function activity such as growth promotion and resistance to chemotherapeutic drugs (9). Phosphorylation of TopBP1 at Ser1159 by Akt regulates TopBP1 oligomerization and function in E2F1-dependent transcriptional regulation (10).

$293
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: The Ras family small GTPase Ran is involved in nuclear envelope formation, assembly of the mitotic spindle, and nuclear transport (1,2). TPX2, a target of active Ran (RanGTP), is a microtubule nucleating protein. TPX2 is inactive when bound to nuclear importin-alpha. RanGTP activity disrupts this interaction, relieving inhibition of TPX2 (3). TPX2 binding activates Aurora A kinase and promotes its localization to the mitotic spindle (4,5). DNA damage in mitosis leads to loss of interaction between Aurora A and TPX2 and inactivation of Aurora A kinase (6). TPX2 is highly expressed in pancreatic cancer cells, and knockdown of TPX2 expression in these cells is associated with increased sensitivity to paclitaxel (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: The Ras family small GTPase Ran is involved in nuclear envelope formation, assembly of the mitotic spindle, and nuclear transport (1,2). TPX2, a target of active Ran (RanGTP), is a microtubule nucleating protein. TPX2 is inactive when bound to nuclear importin-alpha. RanGTP activity disrupts this interaction, relieving inhibition of TPX2 (3). TPX2 binding activates Aurora A kinase and promotes its localization to the mitotic spindle (4,5). DNA damage in mitosis leads to loss of interaction between Aurora A and TPX2 and inactivation of Aurora A kinase (6). TPX2 is highly expressed in pancreatic cancer cells, and knockdown of TPX2 expression in these cells is associated with increased sensitivity to paclitaxel (7).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Telomeres, the linear ends of chromosomes, are organized into T-loops to prevent them from being recognized by the cell as DNA double stranded breaks (DSBs) (1). The telomeric repeat binding factor proteins TRF1 and TRF2 bind to double-stranded telomeres to allow formation of T-loops (2). A large number of proteins involved in the DNA damage response are found physically associated with TRF2 within telomeres (3). Interestingly, TRF2 can transiently localize to DNA damage-induced DSBs, but overexpression of TRF2 prevents ATM-dependent signaling (4). Phosphorylation of TRF2 at Ser323 has been reported in vivo, but no upstream kinase or role has been established for this phosphorylation site (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: TTK (Mps1, PYT) is a cell cycle regulated dual specificity kinase present in rapidly proliferating tissues and cell lines (1-3). TTK localizes to kinetochores and centromeres and is an essential component of the mitotic spindle checkpoint as well as centrosome duplication (4-6). The mitotic checkpoint inhibits entry into anaphase until all chromosomes are attached to the spindle; inhibition of this process leads to genomic instability and tumorigenesis. Phosphorylation of the BLM helicase at Ser144 by TTK maintains chromosome stability during mitosis (7). Small molecule inhibitors of TTK can block the spindle checkpoint response, thereby making TTK a potential therapeutic target (8,9).TTK also participates in the DNA damage response by directly phosphorylating and activating the cell cycle checkpoint kinase Chk2 at Thr68. Two targets phosphorylated by Chk2 are the cell cycle phosphatase cdc25 and the transcription factor p53. Inactivation of cdc25 phosphatase results in the accumulation of inactive cyclin B and cell cycle arrest following DNA damage. Phosphorylation of p53 by active Chk2 stabilizes the transcription factor and promotes cell cycle arrest and apoptosis in response to DNA damage (10).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Proliferating cell nuclear antigen (PCNA) is a member of the DNA sliding clamp family of proteins that assist in DNA replication (1). Crystal structure data suggests that a PCNA homotrimer ring can encircle and slide along the DNA double helix (2). Multiple proteins involved in DNA replication, DNA repair, and cell cycle control bind to PCNA rather than directly associating with DNA, thus facilitating fast processing of DNA (reviewed in 3). PCNA protein expression is a well-accepted marker of proliferation.

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The vaccinia-related kinase (VRK) proteins are a new group of Ser/Thr kinases in the human kinome. This mammalian kinase family comprises three members, VRK1, VRK2, and VRK3 (1-3). The VRK1 has autophosphorylation activity and phosphorylates several transcription factors, including p53 (4), ATF2 (5), and c-Jun (6). VRK2 is associated with the endoplasmic reticulum (7). VRK3 suppresses Erk activity through direct interaction and activation of the MAP kinase phosphatase VHR (8). Further functional and structural analysis of VRK proteins will elucidate important new aspects of cell regulation.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: The cohesin protein complex consists of a heterodimer between SMC1 (SMC1A or B) and SMC3, bound by additional RAD21 and STAG proteins (STAG1, 2, or 3). These proteins form a ring-like structure that mediates the cohesion of two sister chromatids after DNA replication in S phase (1,2). WAPL, also wings apart-like or WAPAL, is a chromatin-associated protein that binds to the cohesin protein complex and regulates its function and its interaction with chromatin (3,4). WAPL, through its interaction with cohesin, is important in the regulation of chromosome structure, cell cycle progression and appropriate chromosome segregation (5,6). Depletion of WAPL leads to segregation errors and DNA damage, and in p53 deficient cells leads to aneuploidy (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. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Wee1 (D10D2) Rabbit mAb #13084.
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Flow Cytometry

Background: Entry of all eukaryotic cells into mitosis is regulated by activation of cdc2 kinase. The critical regulatory step in activating cdc2 during progression into mitosis appears to be dephosphorylation of Tyr15 and Thr14 (1,2). Phosphorylation at Tyr15 and Thr14 and inhibition of cdc2 is carried out by Wee1 and Myt1 protein kinases, while Tyr15 dephosphorylation and activation of cdc2 is carried out by the cdc25 phosphatase (1,3,4). Hyperphosphorylation and inactivation of Myt1 in mitosis suggests that one or more kinases activated at the G2/M transition negatively regulates Myt1 activity. Kinases shown to phosphorylate Myt1 include cdc2, p90RSK, Akt, and Plk1 (5-8).

$115
20 µl
$269
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: Entry of all eukaryotic cells into mitosis is regulated by activation of cdc2 kinase. The critical regulatory step in activating cdc2 during progression into mitosis appears to be dephosphorylation of Tyr15 and Thr14 (1,2). Phosphorylation at Tyr15 and Thr14 and inhibition of cdc2 is carried out by Wee1 and Myt1 protein kinases, while Tyr15 dephosphorylation and activation of cdc2 is carried out by the cdc25 phosphatase (1,3,4). Hyperphosphorylation and inactivation of Myt1 in mitosis suggests that one or more kinases activated at the G2/M transition negatively regulates Myt1 activity. Kinases shown to phosphorylate Myt1 include cdc2, p90RSK, Akt, and Plk1 (5-8).

$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).