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Product listing: Ku70 (V540) Antibody, UniProt ID P12956 #4104 to Phospho-ATRIP (Ser224) Antibody, UniProt ID Q8WXE1 #5161

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: Ku is a heterodimeric protein composed of two subunits (Ku70 and Ku80) originally identified by researchers as autoantigens associated with several autoimmune diseases including scleroderma, polymyositis, and systemic lupus erythematosus (1). Ku is an abundant, ubiquitously expressed nuclear protein that binds to and stabilizes the ends of DNA at telomeres or double-stranded DNA breaks (2-5). The Ku70/Ku80 heterodimer has ATP-dependent DNA helicase activity and functions as the DNA-binding regulatory component of DNA-dependent protein kinase (DNA-PK) (6-8). The assembly of the DNA-PK complex at DNA ends is required for nonhomologous end-joining (NHEJ), one mechanism involved in double-stranded DNA break repair and V(D)J recombination (8). DNA-PK has been shown to phosphorylate many proteins, including p53, serum response factor, c-Jun, c-Fos, c-Myc, Oct-1, Sp-1, and RNA polymerase II (1,8). The combined activities of Ku70/Ku80 and DNA-PK implicate Ku in many cellular functions, including cell cycle regulation, DNA replication and repair, telomere maintenance, recombination, and transcriptional activation.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: Ku is a heterodimeric protein composed of two subunits (Ku70 and Ku80) originally identified by researchers as autoantigens associated with several autoimmune diseases including scleroderma, polymyositis, and systemic lupus erythematosus (1). Ku is an abundant, ubiquitously expressed nuclear protein that binds to and stabilizes the ends of DNA at telomeres or double-stranded DNA breaks (2-5). The Ku70/Ku80 heterodimer has ATP-dependent DNA helicase activity and functions as the DNA-binding regulatory component of DNA-dependent protein kinase (DNA-PK) (6-8). The assembly of the DNA-PK complex at DNA ends is required for nonhomologous end-joining (NHEJ), one mechanism involved in double-stranded DNA break repair and V(D)J recombination (8). DNA-PK has been shown to phosphorylate many proteins, including p53, serum response factor, c-Jun, c-Fos, c-Myc, Oct-1, Sp-1, and RNA polymerase II (1,8). The combined activities of Ku70/Ku80 and DNA-PK implicate Ku in many cellular functions, including cell cycle regulation, DNA replication and repair, telomere maintenance, recombination, and transcriptional activation.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: The Large tumor suppressor (LATS) proteins (LATS1, LATS2) are serine/threonine kinases that belong to the NDR family (1). The Drosophila homolog (warts) was first identified as a tumor suppressor protein that plays a role in the maintenance of ploidy. Human LATS1 was shown to localize to the centrosome and the mitotic spindle and control G2/M transition by negatively regulating cdc2 kinase activity (2,3). LATS1 is also reported to play a role in the G1 tetraploidy checkpoint, via control of p53 expression (4). LATS1 affects cytokinesis by regulating actin polymerization through negative modulation of LIMK1 (5). LATS1 also binds the phosphorylated form of zyxin, a regulator of actin filament assembly. This interaction promotes localization of zyxin to the mitotic spindle, suggesting a role for actin regulatory proteins during mitosis (6). Decreased expression of LATS1 is associated with breast tumor aggressiveness (7), and mutations perturbing LATS1 have been associated with human sarcomas and ovarian sarcomas (8,9). LATS1 knockout mice develop soft-tissue sarcomas, ovarian stromal cell tumor, and display a high sensitivity to carcinogenic treatments (10). LATS1 and LATS2 have also been identified as key members of the Hippo signaling pathway, a conserved kinase cascade that functions to regulate cell growth and apoptosis (11). Phosphorylation of LATS by Mammalian Sterile-20-like proteins (e.g., MST1) results in LATS-mediated phosphorylation of the transcriptional co-activators YAP and TAZ (12, 13). LATS-mediated phosphorylation of YAP and TAZ promotes their cytoplasmic sequestration and association with 14-3-3 proteins, and subsequent proteasomal degradation, leading to downregulation of YAP/TAZ target genes that promote cell growth (11, 14).

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

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).

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

Application Methods: 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).

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

Application Methods: 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).

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

Application Methods: 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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: MGMT (O-6-methylguanine-DNA methyltransferase) is a DNA repair enzyme that participates in a suicide reaction that specifically removes methyl or alkyl groups from the O(6) position of guanine, restoring guanine to its normal form without causing DNA breaks (1). MGMT protects cells from alkylating toxins, and is an important factor in drug resistance to alkylating therapeutic agents (2,3). It is ubiquitously expressed in normal human tissues (4) and is overexpressed in many types of human tumors, but epigenetically silenced in other tumors. MGMT silencing is a marker associated with poor prognosis, but is a good predictive marker for response to alkylating agent chemotherapy (5).

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

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

Background: Mre11, originally described in genetic screens from the yeast Saccharomyces cerevisiae in which mutants were defective in meiotic recombination (1), is a central part of a multisubunit nuclease composed of Mre11, Rad50 and Nbs1 (MRN) (2,3). The MRN complex plays a critical role in sensing, processing and repairing DNA double strand breaks. Defects lead to genomic instability, telomere shortening, aberrant meiosis and hypersensitivity to DNA damage (4). Hypomorphic mutations of Mre11 are found in ataxia-telangiectasia-like disease (ATLD), with phenotypes similar to mutations in ATM that cause ataxia-telangiectasia (A-T), including a predisposition to malignancy in humans (5). Cellular consequences of ATLD include chromosomal instability and defects in the intra-S phase and G2/M checkpoints in response to DNA damage. The MRN complex may directly activate the ATM checkpoint kinase at DNA breaks (6).

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

Application Methods: Western Blotting

Background: The DNA mismatch repair system (MMR) repairs post-replication DNA, inhibits recombination between nonidentical DNA sequences, and induces both checkpoint and apoptotic responses following certain types of DNA damage (1). MSH2 (MutS homologue 2) forms the hMutS-α dimer with MSH6 and is an essential component of the mismatch repair process. hMutS-α is part of the BRCA1-associated surveillance complex (BASC), a complex that also contains BRCA1, MLH1, ATM, BLM, PMS2 proteins, and the Rad50-Mre11-NBS1 complex (2). Mutations in MSH6 and other MMR proteins have been found in a large proportion of hereditary nonpolyposis colorectal cancer (Lynch Syndrome), the most common form of inherited colorectal cancer in the Western world (3). Mutations in MSH6 have been shown to occur in glioblastoma in response to temozolomide therapy and to promote temozolomide resistance (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Base excision repair (BER) proteins catalyze the removal of incorrect or damaged bases, including oxidized bases, from DNA. N-glycosylases specific to a given lesion remove the incorrect base as the first step in BER. MYH is the mammalian ortholog of E. coli MutY, a DNA glycosylase that catalyzes the removal of 8-oxoG:A mismatches (1). Several MYH isoforms have been detected in human cells localizing to either the nucleus or the mitochondria (2). MYH interacts with DNA repair proteins and localizes to DNA damage foci after oxidative damage (3). Research studies have shown that mutations in the corresponding MYH gene are associated with human gastric (4) and colorectal (5-7) cancers.

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

Application Methods: Immunohistochemistry (Paraffin), 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

Application Methods: Western Blotting

Background: NIPA (nuclear interaction partner of ALK) is an F-box-containing protein that is an essential component of the SCF-type E3 ligase (SCFNIPA) complex, a complex that controls the completion of S-phase and mitotic entry (1). This control is mediated by the ubiquitination and subsequent degradation of cell cycle regulatory proteins, whose oscillation of protein levels is required for proper cell cycle progression (2).Expression levels of NIPA are low in G0/G1 phases and upregulated in S and G2/M phases. The SCFNIPA complex targets nuclear cyclin B1 for ubiquitination in interphase, whereas phosphorylation of NIPA in late G2 phase and mitosis inactivates the complex to allow for accumulation of cyclin B1 (3). NIPA may have an anti-apoptotic role in NPM-ALK-mediated signaling events (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Nucleophosmin (NPM; also known as B23, numatrin or NO38) is an abundant phosphoprotein primarily found in nucleoli. It has been implicated in several distinct cellular functions, including assembly and transport of ribosomes, cytoplasmic/nuclear trafficking, regulation of DNA polymerase α activity, centrosome duplication and molecular chaperoning activities (1,2). The NPM gene is also known for its fusion with the anaplastic lymphoma kinase (ALK) receptor tyrosine kinase. The NPM portion contributes to transformation by providing a dimerization domain, which results in activation of the fused kinase (3,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: The nuclear mitotic apparatus protein (NuMA) is a coiled coil protein involved in the formation and maintenance of the mitotic spindle. NuMA plays a role in chromatin organization during interphase, which influences mammary epithelial differentiation (1,2). During apoptosis, carboxy-terminal cleavage of NuMA may amplify signaling in the cell death pathway (2). NuMA is phosphorylated at numerous sites, with phosphorylation at Ser395 occurring in an ATM/ATR-dependent manner in response to DNA damage (3,4).Phosphorylation at Thr2055 by CDK1 is required for spindle pole association of NuMA at the onset of mitosis. Dephosphorylation by PPP2CA leads to enhancement of NuMA at the cell cortex in anaphase and proper cell-cycle progression (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: The tumor suppressor protein p21 Waf1/Cip1 acts as an inhibitor of cell cycle progression. It functions in stoichiometric relationships forming heterotrimeric complexes with cyclins and cyclin-dependent kinases. In association with CDK2 complexes, it serves to inhibit kinase activity and block progression through G1/S (1). However, p21 may also enhance assembly and activity in complexes of CDK4 or CDK6 and cyclin D (2). The carboxy-terminal region of p21 is sufficient to bind and inhibit PCNA, a subunit of DNA polymerase, and may coordinate DNA replication with cell cycle progression (3). Upon UV damage or during cell cycle stages when cdc2/cyclin B or CDK2/cyclin A are active, p53 is phosphorylated and upregulates p21 transcription via a p53-responsive element (4). Protein levels of p21 are downregulated through ubiquitination and proteasomal degradation (5).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: p27 Kip1 is a member of the Cip/Kip family of cyclin-dependent kinase inhibitors. Like its relatives, p57 Kip2 and p21 Waf1/Cip1, the ability to enforce the G1 restriction point is derived from its inhibitory binding to CDK2/cyclin E and other CDK/cyclin complexes. Expression levels of p27 are upregulated in quiescent cells and in cells treated with cAMP or other negative cell cycle regulators. Downregulation of p27 can be induced by treatment with interleukin-2 or other mitogens; this involves phosphorylation of p27 and its degradation by the ubiquitin-proteasome pathway (1-4).

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

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: The p53 tumor suppressor protein plays a major role in cellular response to DNA damage and other genomic aberrations. Activation of p53 can lead to either cell cycle arrest and DNA repair or apoptosis (1). p53 is phosphorylated at multiple sites in vivo and by several different protein kinases in vitro (2,3). DNA damage induces phosphorylation of p53 at Ser15 and Ser20 and leads to a reduced interaction between p53 and its negative regulator, the oncoprotein MDM2 (4). MDM2 inhibits p53 accumulation by targeting it for ubiquitination and proteasomal degradation (5,6). p53 can be phosphorylated by ATM, ATR, and DNA-PK at Ser15 and Ser37. Phosphorylation impairs the ability of MDM2 to bind p53, promoting both the accumulation and activation of p53 in response to DNA damage (4,7). Chk2 and Chk1 can phosphorylate p53 at Ser20, enhancing its tetramerization, stability, and activity (8,9). p53 is phosphorylated at Ser392 in vivo (10,11) and by CAK in vitro (11). Phosphorylation of p53 at Ser392 is increased in human tumors (12) and has been reported to influence the growth suppressor function, DNA binding, and transcriptional activation of p53 (10,13,14). p53 is phosphorylated at Ser6 and Ser9 by CK1δ and CK1ε both in vitro and in vivo (13,15). Phosphorylation of p53 at Ser46 regulates the ability of p53 to induce apoptosis (16). Acetylation of p53 is mediated by p300 and CBP acetyltransferases. Inhibition of deacetylation suppressing MDM2 from recruiting HDAC1 complex by p19 (ARF) stabilizes p53. Acetylation appears to play a positive role in the accumulation of p53 protein in stress response (17). Following DNA damage, human p53 becomes acetylated at Lys382 (Lys379 in mouse) in vivo to enhance p53-DNA binding (18). Deacetylation of p53 occurs through interaction with the SIRT1 protein, a deacetylase that may be involved in cellular aging and the DNA damage response (19).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: p27 Kip1 is a member of the Cip/Kip family of cyclin-dependent kinase inhibitors. Like its relatives, p57 Kip2 and p21 Waf1/Cip1, the ability to enforce the G1 restriction point is derived from its inhibitory binding to CDK2/cyclin E and other CDK/cyclin complexes. Expression levels of p27 are upregulated in quiescent cells and in cells treated with cAMP or other negative cell cycle regulators. Downregulation of p27 can be induced by treatment with interleukin-2 or other mitogens; this involves phosphorylation of p27 and its degradation by the ubiquitin-proteasome pathway (1-4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: The p53 tumor suppressor protein plays a major role in cellular response to DNA damage and other genomic aberrations. Activation of p53 can lead to either cell cycle arrest and DNA repair or apoptosis (1). In addition to p53, mammalian cells contain two p53 family members, p63 and p73, which are similar to p53 in both structure and function (2). While p63 can induce p53-responsive genes and apoptosis, mutation of p63 rarely results in tumors (2). Research investigators frequently observe amplification of the p63 gene in squamous cell carcinomas of the lung, head and neck (2,3). The p63 gene contains an alternative transcription initiation site that yields a truncated ΔNp63 lacking the transactivation domain, and alternative splicing at the carboxy-terminus yields the α, β, and γ isoforms (3,4).

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

Application Methods: Western Blotting

Background: Nijmegen breakage syndrome (NBS) is characterized by growth retardation, mental disability, immunodeficiency, defects in cell cycle checkpoints, an increased propensity for cancer, and sensitivity to ionizing radiation (1). Repair of radiation-induced DNA double-strand breaks is dependent on the multifunctional MRN complex containing Mre11, Rad50, and the NBS1 gene product p95/NBS1 (also called p95 or nibrin) (2). p95/NBS1 is a protein with a forkhead-associated domain and a BRCT repeat that regulate interaction with MDC1 and are essential for proper G2/M DNA-damage checkpoint function (3). NBS1 is critical for homologous recombination following DNA double strand breaks. This activity requires CDK-dependent association with CtIP and subsequent phosphorylation by ATM (4). ATM interacts with and phosphorylates p95/NBS1 at Ser278 and Ser343 after exposure to ionizing radiation (5,6).

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

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: PBK/TOPK is a serine/threonine kinase that is phosphorylated and active during mitosis (1). PBK/TOPK is composed of kinase subdomains and a carboxy-terminal PDZ-Binding domain, which is thought to interact with the tumor suppressor protein hDlg (1). Increased PBK/TOPK expression has been observed in highly proliferative malignant cell lines, and PBK/TOPK expression is strongly downregulated during terminal differentiation of HL-60 leukemic cells (2,3). PMA-induced kinase activity toward PBK/TOPK has been observed (4), and cdc2/cyclinB has been shown to phosphorylate PBK/TOPK in vitro, presumably at Thr9 (1). Potential substrates of PBK/TOPK include p38 MAPK and c-Myc (3,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry, Immunoprecipitation, Western Blotting

Background: Three distinct PCTAIRE isoforms (PCTAIRE 1, PCTAIRE 2 and PCTAIRE 3) have been identified in humans and belong to the CDK family of serine/threonine protein kinases. These proteins have a core kinase domain flanked by unique amino- and carboxy-terminal domains. CDK proteins are known to regulate the cell cycle. All three PCTAIRE isoforms are abundantly expressed and catalytically active in post-mitotic brain, suggesting that they may function in processes other than cell division (1). PCTAIRE 1 is a cytoplasmic phosphoprotein whose kinase activity peaks in G2 and S phase (2). While one study indicates that noncovalent interactions with a regulatory component (such as a cyclin) are necessary for catalytic activity of PCTAIRE 1, others show that the monomeric protein is fully active (3). The Cdk5/p25 complex phosphorylates PCTAIRE 1 at Ser95, enhancing its kinase activity (4).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The prohibitins, called PHB1 and PHB2, are highly conserved proteins that are present in multiple compartments in eukaryotic cells. PHB1 is 30kDa tumor suppressor protein involved in cell cycle control (1). PHB1 has been found in mitochondria, the nucleus and the plasma membrane, as well as extracellularly in circulation (2). In mitochondria prohibitins mainly exist as membrane-bound ring complexes and function as chaperones maintaining mitochondrial protein stability during protein synthesis and transportation (3,4). In the nucleus prohibitins interact with transcription factors such as Rb and p53 to regulate target gene transcription (2,5). Extracellular prohibitin can bind and activate C3 to enhance complement activation (6).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: p53-binding protein 1 (53BP1) was originally identified as a p53 binding partner that could enhance the transcriptional activity of p53 (1,2). 53BP1 consists of two BRCA1 carboxy terminal (BRCT) domains that allow for binding to p53 and a separate domain responsible for binding to phosphorylated histone H2A.X (3). 53BP1 rapidly translocates to nuclear foci following treatment of cells with ionizing radiation (IR) or radiomimetic agents that cause DNA double strand breaks (DSBs) (4,5). Because of this localization to DSBs and homology to the yeast protein Rad9, a role for 53BP1 in DSB repair has been proposed. Recruitment of 53BP1 to sites of DNA damage has been demonstrated to be independent of ATM, NBS1, and DNA-PK (4) and retention of 53BP1 at DNA breaks requires phosphorylated H2A.X (6). In cells lacking 53BP1, phosphorylation of ATM substrates is reduced, suggesting that 53BP1 is upstream of ATM (7). In response to IR, phosphorylation of 53BP1 at serines 6, 25, 29, and 784 by ATM has been demonstrated, but phosphorylation at these sites is not required for localization of 53BP1 to sites of DSBs (6). Phosphorylation of 53BP1 at Ser1618 has been reported to be enriched in human cells arrested in mitosis (8).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: p53-binding protein 1 (53BP1) was originally identified as a p53 binding partner that could enhance the transcriptional activity of p53 (1,2). 53BP1 consists of two BRCA1 carboxy terminal (BRCT) domains that allow for binding to p53 and a separate domain responsible for binding to phosphorylated histone H2A.X (3). 53BP1 rapidly translocates to nuclear foci following treatment of cells with ionizing radiation (IR) or radiomimetic agents that cause DNA double strand breaks (DSBs) (4,5). Because of this localization to DSBs and homology to the yeast protein Rad9, a role for 53BP1 in DSB repair has been proposed. Recruitment of 53BP1 to sites of DNA damage has been demonstrated to be independent of ATM, NBS1, and DNA-PK (4) and retention of 53BP1 at DNA breaks requires phosphorylated H2A.X (6). In cells lacking 53BP1, phosphorylation of ATM substrates is reduced, suggesting that 53BP1 is upstream of ATM (7). In response to IR, phosphorylation of 53BP1 at serines 6, 25, 29, and 784 by ATM has been demonstrated, but phosphorylation at these sites is not required for localization of 53BP1 to sites of DSBs (6). Phosphorylation of 53BP1 at Ser1618 has been reported to be enriched in human cells arrested in mitosis (8).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: p53-binding protein 1 (53BP1) was originally identified as a p53 binding partner that could enhance the transcriptional activity of p53 (1,2). 53BP1 consists of two BRCA1 carboxy terminal (BRCT) domains that allow for binding to p53 and a separate domain responsible for binding to phosphorylated histone H2A.X (3). 53BP1 rapidly translocates to nuclear foci following treatment of cells with ionizing radiation (IR) or radiomimetic agents that cause DNA double strand breaks (DSBs) (4,5). Because of this localization to DSBs and homology to the yeast protein Rad9, a role for 53BP1 in DSB repair has been proposed. Recruitment of 53BP1 to sites of DNA damage has been demonstrated to be independent of ATM, NBS1, and DNA-PK (4) and retention of 53BP1 at DNA breaks requires phosphorylated H2A.X (6). In cells lacking 53BP1, phosphorylation of ATM substrates is reduced, suggesting that 53BP1 is upstream of ATM (7). In response to IR, phosphorylation of 53BP1 at serines 6, 25, 29, and 784 by ATM has been demonstrated, but phosphorylation at these sites is not required for localization of 53BP1 to sites of DSBs (6). Phosphorylation of 53BP1 at Ser1618 has been reported to be enriched in human cells arrested in mitosis (8).

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Ataxia telangiectasia mutated kinase (ATM) and ataxia telangiectasia and Rad3-related kinase (ATR) are PI3 kinase-related kinase (PIKK) family members that phosphorylate multiple substrates on serine or threonine residues that are followed by a glutamine in response to DNA damage or replication blocks (1-3). Despite the essential role of ATR in cell cycle signaling and DNA repair processes, little is known about its activation. ATR was long thought to exist in a constitutively active state in cells, with DNA damage-induced signaling occurring via recruitment of ATR to single stranded DNA and sites of replication stress. Phosphorylation of ATR at serine 428 in response to UV-induced DNA damage has been suggested as a means of activating ATR (4,5). Recent work has shown autophosphorylation of ATR at threonine 1989. Like ATM Ser1981, phosphorylation of ATR Thr1989 occurs in response to DNA damage, indicating that phosphorylation at this site is important in ATR-mediated signaling (6,7).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Ataxia telangiectasia mutated kinase (ATM) and ataxia telangiectasia and Rad3-related kinase (ATR) are PI3 kinase-related kinase (PIKK) family members that phosphorylate multiple substrates on serine or threonine residues that are followed by a glutamine in response to DNA damage or replication blocks (1-3). Despite the essential role of ATR in cell cycle signaling and DNA repair processes, little is known about its activation. ATR was long thought to exist in a constitutively active state in cells, with DNA damage-induced signaling occurring via recruitment of ATR to single stranded DNA and sites of replication stress. Phosphorylation of ATR at serine 428 in response to UV-induced DNA damage has been suggested as a means of activating ATR (4,5). Recent work has shown autophosphorylation of ATR at threonine 1989. Like ATM Ser1981, phosphorylation of ATR Thr1989 occurs in response to DNA damage, indicating that phosphorylation at this site is important in ATR-mediated signaling (6,7).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: In response to genomic stress, the ATR interacting protein (ATRIP) binds and is phosphorylated by the DNA damage-and checkpoint-activated kinase ATR (ataxia-telangiectasia mutated and rad3-related). Both ATR and ATRIP are integral for checkpoint signaling and are critical in the DNA repair response (1-3). Direct interaction between ATRIP and replication protein A (RPA) at RPA-coated, single-stranded DNA results in the recruitment of phosphorylated ATR/ATRIP to stalled replication forks and sites of DNA damage (3). ATR/ATRIP coordinate DNA repair and cell cycle progression in conjunction with key regulatory proteins, such as Rad17 and the 9-1-1 complex (4). ATR associated with ATRIP can also be stimulated by topoisomerase II binding protein (TOPBP1), suggesting that ATRIP may regulate both ATR localization and activity (5).