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Product listing: BMAL1 (D2L7G) Rabbit mAb, UniProt ID O00327 #14020 to BRSK2 (D29B6) Rabbit mAb, UniProt ID Q8IWQ3 #5460

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: Circadian rhythms govern many key physiological processes that fluctuate with a period of approximately 24 hours. These processes include the sleep-wake cycle, glucose, lipid and drug metabolism, heart rate, hormone secretion, renal blood flow, and body temperature, as well as basic cellular processes such as DNA repair and the timing of the cell division cycle (1,2). The mammalian circadian system consists of many individual tissue-specific clocks (peripheral clocks) that are controlled by a master circadian pacemaker residing in the suprachiasmatic nuclei (SCN) of the brain (1,2). The periodic circadian rhythm is prominently manifested by the light-dark cycle, which is sensed by the visual system and processed by the SCN. The SCN processes the light-dark information and synchronizes peripheral clocks through neural and humoral output signals (1,2).The cellular circadian clockwork consists of interwoven positive and negative regulatory loops, or limbs (1,2). The positive limb includes the CLOCK and BMAL1 proteins, two basic helix-loop-helix-PAS containing transcription factors that bind E box enhancer elements and activate transcription of their target genes. CLOCK is a histone acetyltransferase (HAT) protein, which acetylates both histone H3 and H4 (3). BMAL1 binds to CLOCK and enhances its HAT activity (3). The CLOCK/BMAL1 dimer exhibits a periodic oscillation in both nuclear/cytoplasmic localization and protein levels, both of which are regulated by phosphorylation (4,5). CLOCK/BMAL1 target genes include the Cry and Per genes, whose proteins form the negative limb of the circadian clockwork system (1,2). CRY and PER proteins (CRY1, CRY2, PER1, PER2 and PER3) form oligomers that also periodically shuttle between the nucleus and cytoplasm. When in the nucleus, CRY/PER proteins inhibit CLOCK/BMAL1-mediated transcriptional activation, thus completing the circadian transcriptional loop (1,2). In tissues, roughly six to eight percent of all genes exhibit a circadian expression pattern (1,2). This 24-hour periodicity in gene expression results from coordination of the positive and negative regulatory limbs of the cellular clockwork system, and is fine-tuned by outside signals received from the SCN.

$348
50 assays
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometric analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Bmi1 (D20B7) XP® Rabbit mAb #6964.
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Flow Cytometry

Background: The polycomb group (PcG) of proteins contributes to the maintenance of cell identity, stem cell self-renewal, cell cycle regulation, and oncogenesis by maintaining the silenced state of genes that promote cell lineage specification, cell death, and cell-cycle arrest (1-4). PcG proteins exist in two complexes that cooperate to maintain long-term gene silencing through epigenetic chromatin modifications. The first complex, EED-EZH2, is recruited to genes by DNA-binding transcription factors and methylates histone H3 on Lys27. This histone methyl-transferase activity requires the Ezh2, Eed, and Suz12 subunits of the complex (5). Histone H3 methylation at Lys27 facilitates the recruitment of the second complex, PRC1, which ubiquitinylates histone H2A on Lys119 (6). Bmi1 is a component of the PRC1 complex, which together with Ring1 strongly enhances the E3 ubiquitin ligase activity of the Ring2 catalytic subunit (7). Bmi1 plays an important role in the regulation of cell proliferation and senescence through repression of the p16 INK4A and p19 ARF genes and is required for maintenance of adult hematopoietic and neural stem cells (3,4,8-10).

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

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

Background: The polycomb group (PcG) of proteins contributes to the maintenance of cell identity, stem cell self-renewal, cell cycle regulation, and oncogenesis by maintaining the silenced state of genes that promote cell lineage specification, cell death, and cell-cycle arrest (1-4). PcG proteins exist in two complexes that cooperate to maintain long-term gene silencing through epigenetic chromatin modifications. The first complex, EED-EZH2, is recruited to genes by DNA-binding transcription factors and methylates histone H3 on Lys27. This histone methyl-transferase activity requires the Ezh2, Eed, and Suz12 subunits of the complex (5). Histone H3 methylation at Lys27 facilitates the recruitment of the second complex, PRC1, which ubiquitinylates histone H2A on Lys119 (6). Bmi1 is a component of the PRC1 complex, which together with Ring1 strongly enhances the E3 ubiquitin ligase activity of the Ring2 catalytic subunit (7). Bmi1 plays an important role in the regulation of cell proliferation and senescence through repression of the p16 INK4A and p19 ARF genes and is required for maintenance of adult hematopoietic and neural stem cells (3,4,8-10).

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

Application Methods: Chromatin IP, Chromatin IP-seq, Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: The polycomb group (PcG) of proteins contributes to the maintenance of cell identity, stem cell self-renewal, cell cycle regulation, and oncogenesis by maintaining the silenced state of genes that promote cell lineage specification, cell death, and cell-cycle arrest (1-4). PcG proteins exist in two complexes that cooperate to maintain long-term gene silencing through epigenetic chromatin modifications. The first complex, EED-EZH2, is recruited to genes by DNA-binding transcription factors and methylates histone H3 on Lys27. This histone methyl-transferase activity requires the Ezh2, Eed, and Suz12 subunits of the complex (5). Histone H3 methylation at Lys27 facilitates the recruitment of the second complex, PRC1, which ubiquitinylates histone H2A on Lys119 (6). Bmi1 is a component of the PRC1 complex, which together with Ring1 strongly enhances the E3 ubiquitin ligase activity of the Ring2 catalytic subunit (7). Bmi1 plays an important role in the regulation of cell proliferation and senescence through repression of the p16 INK4A and p19 ARF genes and is required for maintenance of adult hematopoietic and neural stem cells (3,4,8-10).

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

Application Methods: Western Blotting

Background: The polycomb group (PcG) of proteins contributes to the maintenance of cell identity, stem cell self-renewal, cell cycle regulation, and oncogenesis by maintaining the silenced state of genes that promote cell lineage specification, cell death, and cell-cycle arrest (1-4). PcG proteins exist in two complexes that cooperate to maintain long-term gene silencing through epigenetic chromatin modifications. The first complex, EED-EZH2, is recruited to genes by DNA-binding transcription factors and methylates histone H3 on Lys27. This histone methyl-transferase activity requires the Ezh2, Eed, and Suz12 subunits of the complex (5). Histone H3 methylation at Lys27 facilitates the recruitment of the second complex, PRC1, which ubiquitinylates histone H2A on Lys119 (6). Bmi1 is a component of the PRC1 complex, which together with Ring1 strongly enhances the E3 ubiquitin ligase activity of the Ring2 catalytic subunit (7). Bmi1 plays an important role in the regulation of cell proliferation and senescence through repression of the p16 INK4A and p19 ARF genes and is required for maintenance of adult hematopoietic and neural stem cells (3,4,8-10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Bone morphogenetic proteins (BMPs) were first identified as molecules that can induce ectopic bone and cartilage formation (1,2). BMPs belong to the TGF-β superfamily, playing many diverse functions during development (3). BMPs are synthesized as precursor proteins and then processed by cleavage to release the C-terminal mature BMP. BMPs initiate signaling by binding to a receptor complex containing type I and type II serine/threonine receptor kinases that then phosphorylate Smad (mainly Smad1, 5, and 8), resulting in the translocation of Smad into the nucleus. BMP was also reported to activate MAPK pathways in some systems (3,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Bone morphogenetic proteins (BMPs) were first identified as molecules that can induce ectopic bone and cartilage formation (1,2). BMPs belong to the TGF-β superfamily, playing many diverse functions during development (3). BMPs are synthesized as precursor proteins and then processed by cleavage to release the C-terminal mature BMP. BMPs initiate signaling by binding to a receptor complex containing type I and type II serine/threonine receptor kinases that then phosphorylate Smad (mainly Smad1, 5, and 8), resulting in the translocation of Smad into the nucleus. BMP was also reported to activate MAPK pathways in some systems (3,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: BNIP3 (Bcl-2/E1B-19kDa interacting protein 3) is a pro-apoptotic mitochondrial protein and Bcl-2 family member that contains a Bcl-2 homology 3 (BH3) domain and a carboxyl-terminal transmembrane (TM) domain (1-3). While BNIP3 has a predicted molecular weight of about 22 kDa, it runs anomalously on SDS-PAGE and includes a band of around 60 kDa that may be a dimeric form that is not reduced (2). BNIP3 associates with anti-apoptotic family members Bcl-2, Bcl-xL, and the adenovirus homologue E1B-19kDa. BNIP3 is distinct from other Bcl-2 family members that contain only the BH3 domain in that the TM domain, and not the BH3 domain, is required for mitochondrial targeting and pro-apoptotic activity (4). In addition to apoptosis, BNIP3 has been implicated in necrosis (5) and autophagy (6-11). In hypoxic conditions, BNIP3 can induce mitochondrial autophagy (mitophagy) by disrupting the Bcl-2-Beclin-1 complex (9). BNIP3 can also promote mitophagy by triggering the translocation of the E3 ubiquitin ligase Parkin to the mitochondria (10) or by directly binding LC3 on the autophagosome (11). BNIP3 may also localize to the endoplasmic reticulum (ER) where it can selectively induce the autophagic clearance of ER (ERphagy) (11). Increased expression of BNIP3 under hypoxic conditions is mainly regulated by the transcription factor HIF-1α (12-14). Silencing of the BNIP3 promoter by methylation has been observed in several types of cancer cells and may play an important role in their survival (14-18).

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

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

Background: BCL2/Adenovirus E1B 19 kDa protein-interacting protein 3-like (BNIP3L) (1), also termed BNIP3α (2), B5 (3), and Nix (4), is a member of the Bcl-2 family of apoptotic regulators with highest homology to BNIP3. BNIP3L can bind BNIP3, Bcl-xL, and Bcl-2 (1-5). BNIP3L forms homodimers that withstand denaturing by SDS and reducing conditions (5). BNIP3L is a mitochondrial protein and knockout studies suggest that BNIP3L regulates autophagic clearance of damaged mitochondria during erythroid maturation via mitochondrial autophagy (6,7). It has been shown that the expression of BNIP3L is up-regulated during terminal erythroid differentiation (6-8), as well as in tumor cell lines during hypoxia (9-11). BNIP3L directly regulates the elimination of mitochondria through its ability to bind to and recruit important components of the autophagic machinery, including LC3/Atg8 and GABARAP proteins, via its amino-terminal LC3-interacting region (LIR) (12). BNIP3L may also indirectly activate phagophore formation either via the recruitment of autophagy proteins or by binding Bcl-xL, which in turn releases Beclin-1 (13). BNIP3L/Nix also plays a pivotal role in Parkin-mediated mitochondrial autophagy via its ability to mediate the mitochondrial translocation of Parkin (14). Activated BNIP3L can promote the opening of mitochondrial permeability transition pores resulting in mitochondrial depolarization, generation of reactive oxygen species, and induction of necrosis. Due to its involvement in cell death and autophagy, research scientists have implicated BNIP3L in heart disease and cancer (13).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The Bcl-2 family consists of a number of evolutionarily conserved proteins containing Bcl-2 homology domains (BH) that regulate apoptosis through control of mitochondrial membrane permeability and release of cytochrome c (1-3). Four BH domains have been identified (BH1-4) that mediate protein interactions. The family can be separated into three groups based upon function and sequence homology: pro-survival members include Bcl-2, Bcl-xL, Mcl-1, A1 and Bcl-w; pro-apoptotic proteins include Bax, Bak and Bok; and "BH3 only" proteins Bad, Bik, Bid, Puma, Bim, Bmf, Noxa and Hrk. Interactions between death-promoting and death-suppressing Bcl-2 family members has led to a rheostat model in which the ratio of pro-apoptotic and anti-apoptotic proteins controls cell fate (4). Thus, pro-survival members exert their behavior by binding to and antagonizing death-promoting members. In general, the "BH3-only members" can bind to and antagonize the pro-survival proteins leading to increased apoptosis (5). While some redundancy of this system likely exists, tissue specificity, transcriptional and post-translational regulation of many of these family members can account for distinct physiological roles.

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Immunoprecipitation, Western Blotting

Background: The eukaryotic cell cycle is carefully controlled by protein phosphorylation involving a number of phosphatases, kinases, and co-factors. Cyclin-dependent kinases (CDKs/cdcs), Polo-like kinases (PLKs), and Aurora kinases have been shown to be major regulators of mitotic control (reviewed in 1,2). Protein aurora borealis (Bora), a co-factor of Aurora-A first identified in Drosophila, also plays a key roll in cell cycle progression (3). Bora levels are low in G0/G1, increasing in S-phase and peaking at G2 (4).Found to be conserved from C. elegans to humans, Bora is translocated from the nucleus to the cytoplasm upon activation of cdc2 at the onset of mitosis. Once present in the cytoplasm, Bora binds to and activates Aurora-A and PLK1 (3-5). It has been proposed that the binding of human Bora to PLK1 may lead to a conformational change in the protein that disrupts the autoinhibition by the Polo-Box Domain (PBD). This would allow for Thr210 on PLK1 to become more accessible for phosphorylation by Aurora-A (reviewed in 6). Active PLK1 then initiates the PLK1-cdc25-cdc2 positive feedback loop, leading to mitotic entry and the phosphorylation of Bora. Once phosphorylated in prophase, Bora is degraded allowing for normal mitotic progression (7).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) 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 Brachyury (D2Z3J) Rabbit mAb #81694.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: Brachyury protein, encoded by the T gene, is a transcription factor that is vital for the formation of posterior mesoderm and axial development during vertebrate embryogenesis (1). In the mouse, brachyury is necessary for mesodermal morphogenetic cell movements during gastrulation. Brachyury mutant mice die in utero and display deficient mesoderm formation including an abnormal notochord, missing posterior somites, and a reduced allantois (2). Human brachyury is expressed in the notochord, as well as in chordoma tumors that occur along the spine, making it a good marker for notochord and notochord-derived tumors (3,4). A common polymorphism in the human T gene has also been shown to be associated with development of the multifactorial neural tube defect, spina bifida (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Brachyury protein, encoded by the T gene, is a transcription factor that is vital for the formation of posterior mesoderm and axial development during vertebrate embryogenesis (1). In the mouse, brachyury is necessary for mesodermal morphogenetic cell movements during gastrulation. Brachyury mutant mice die in utero and display deficient mesoderm formation including an abnormal notochord, missing posterior somites, and a reduced allantois (2). Human brachyury is expressed in the notochord, as well as in chordoma tumors that occur along the spine, making it a good marker for notochord and notochord-derived tumors (3,4). A common polymorphism in the human T gene has also been shown to be associated with development of the multifactorial neural tube defect, spina bifida (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The breast cancer susceptibility proteins BRCA1 and BRCA2 are frequently mutated in cases of hereditary breast and ovarian cancers and have roles in multiple processes related to DNA damage, repair, cell cycle progression, transcription, ubiquitination, and apoptosis (1-4). BRCA2 has been shown to be required for localization of Rad51 to sites of double stranded breaks (DSBs) in DNA, and cells lacking BRCA1 and BRCA2 cannot repair DSBs through the Rad51-dependent process of homologous recombination (HR) (5). Numerous DNA damage-induced phosphorylation sites on BRCA1 have been identified, including Ser988, 1189, 1387, 1423, 1457, 1524, and 1542, and kinases activated in a cell cycle-dependent manner, including Aurora A and CDK2, can also phosphorylate BRCA1 at Ser308 and Ser1497, respectively (6-10). Cell cycle-dependent phosphorylation of BRCA2 at Ser3291 by CDKs has been proposed as a mechanism to switch off HR as cells progress beyond S-phase by blocking the carboxy terminal Rad51 binding site (11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The breast cancer susceptibility proteins BRCA1 and BRCA2 are frequently mutated in cases of hereditary breast and ovarian cancers and have roles in multiple processes related to DNA damage, repair, cell cycle progression, transcription, ubiquitination, and apoptosis (1-4). BRCA2 has been shown to be required for localization of Rad51 to sites of double stranded breaks (DSBs) in DNA, and cells lacking BRCA1 and BRCA2 cannot repair DSBs through the Rad51-dependent process of homologous recombination (HR) (5). Numerous DNA damage-induced phosphorylation sites on BRCA1 have been identified, including Ser988, 1189, 1387, 1423, 1457, 1524, and 1542, and kinases activated in a cell cycle-dependent manner, including Aurora A and CDK2, can also phosphorylate BRCA1 at Ser308 and Ser1497, respectively (6-10). Cell cycle-dependent phosphorylation of BRCA2 at Ser3291 by CDKs has been proposed as a mechanism to switch off HR as cells progress beyond S-phase by blocking the carboxy terminal Rad51 binding site (11).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Protein ubiquitination and deubiquitination are reversible processes catalyzed by ubiquitinating enzymes and deubiquitinating enzymes, respectively (1,2). Deubiquitinating enzymes (DUBs) are categorized into five subfamilies based on catalytic domain structure: USP, OTU, MJD, UCH, and JAMM/MPN. BRCC36 is a zinc-dependent DUB belonging to the JAMM/MPN subfamily and participates in DNA damage responses and interferon signaling by specifically catalyzing hydrolysis of K63-linked polyubiquitin chains (3,4). In the nucleus, BRCC36 is part of the BRCA1-A complex that contains RAP80, BRCA1, ABRAXAS, and MERIT40 (5,6). This complex plays a critical role in mediating the cellular repair of DNA double strand breaks induced by ionizing radiation (7-10). Research studies have shown that BRCC36 is overexpressed in a high percentage of breast tumors, which may contribute to resistance of breast cancer cells to ionizing radiation-induced apoptosis (4). BRCC36 also functions in the cytoplasm as part of a distinct complex known as the BRCC36-containing isopeptide complex (BRISC) (5,6). Indeed, research studies have shown that BRCC36 deubquitinates and stabilizes IFNAR1 to modulate the cellular response to interferons (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Chromatin IP, Chromatin IP-seq, Western Blotting

Background: Brd2 is a highly conserved member of the BET subfamily of bromodomain proteins that contain two tandem N-terminal bromodomains and a single C-terminal extra-terminal (ET) domain (1). In addition to its involvement in guiding the expression of cell cycle genes through its binding to multiple E2Fs (2), Brd2 has been shown to be associated with several regulators of transcription, including TFIID and Swi/Snf complexes (3,4). First identified as a nuclear serine/threonine kinase (5), Brd2, like other bromodomain proteins, is thought to function in mammalian development by regulating chromatin structure and transcription (6). Brd2 has been shown to bind to histone H4 via acetylated Lys12, a substrate of several histone acetyltransferase transcriptional coactivators (7). In mouse, Brd2 has the highest levels of expression during embryogenesis and in the adult testis, ovaries, and brain (8,9,10). Brd2-deficient mouse embryos exhibit delayed development and eventual death due to neural tube closure defects (11). Mutations in the promoter of the Brd2 gene have been associated with increased susceptibility to juvenile myoclonic epilepsy (JME) (12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: Bromodomain-containing protein 4 (BRD4) is a member of the bromodomains and extra terminal (BET) family of proteins, which also includes BRD2, BRD3, and BRDT (1-3). BET family proteins contain two tandem bromodomains and an extra terminal (ET) domain, and bind acetyl lysine residues (3). BRD4 is a chromatin-binding protein with a preference for Lys14 on histone H3 as well as Lys5 and Lys12 on histone H4 (4). BRD4 chromatin binding occurs throughout the cell cycle, including condensed mitotic chromosomes, when the majority of genes are silenced (5). BRD4 association with chromatin during mitosis is thought to be an important part of the bookmarking mechanism to accelerate re-activation of the silenced genes upon exit from mitosis (2,6). BRD4 has been shown to facilitate transcription by recruiting the positive transcription elongation factor b (pTEFb) complex that phosphorylates Ser2 of the heptapeptide repeat of the carboxy-terminal domain of RNA polymerase II, promoting transcription elongation (3,7,8). In addition, BRD4 has been found to be part of the super elongation complex and the polymerase associated factor complex (PAFc) in MLL-fusion derived leukemia cell lines, demonstrating a role for BRD4 in the regulation of transcription elongation (9). Research studies have shown that BRD4 (and BET family proteins) may be promising therapeutic targets for various Myc-driven cancers, such as Burkitt’s lymphoma and certain acute myeloid leukemias (1,10,11). Investigators have found molecular inhibition of BET proteins to be effective in inducing apoptosis in various MLL-fusion driven leukemic cell lines by competing BRD3 and BRD4 from chromatin, leading to reduced expression of Bcl-2, Myc, and CDK6 (9). BET inhibition has also been shown to have antitumor activities against nuclear protein in testis (NUT) midline carcinoma cell lines and xenografts in mice where BRD4 is found to be a frequent translocation partner of the NUT protein (12). In addition, BRD4 regulates the expression of some inflammatory genes, and inhibition of BRD4 (and BET family proteins) chromatin binding causes reduced expression of a subset of inflammatory genes in macrophages, leading to protection against endotoxic shock and sepsis (13).

$260
100 µl
REACTIVITY
Human

Background: Bromodomain-containing protein 7 (BRD7, BP75, CELTIX-1) is a conserved bromodomain-containing protein that was first identified in a screen for proteins that interact with the PDZ domain of PSD95 (1). Subsequent studies identified BRD7 as a major component of SWI/SNF chromatin remodeling complexes, where it was shown to interact directly with acetylated histones to regulate gene transcription (2,3). BRD7 also interacts with p53, and was shown to participate directly in p53-dependent transcriptional regulation (4). Loss-of-function BRD7 mutations were identified in a subset of wild-type p53 breast cancer tumor samples, implicating BRD7 as a putative tumor-suppressor of potential clinical significance (5). BRD7 also associates with the BRCA1 protein, an interaction that facilitates recruitment of BRCA1 to the ERα gene promoter (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Bromodomain-containing protein 7 (BRD7, BP75, CELTIX-1) is a conserved bromodomain-containing protein that was first identified in a screen for proteins that interact with the PDZ domain of PSD95 (1). Subsequent studies identified BRD7 as a major component of SWI/SNF chromatin remodeling complexes, where it was shown to interact directly with acetylated histones to regulate gene transcription (2,3). BRD7 also interacts with p53, and was shown to participate directly in p53-dependent transcriptional regulation (4). Loss-of-function BRD7 mutations were identified in a subset of wild-type p53 breast cancer tumor samples, implicating BRD7 as a putative tumor-suppressor of potential clinical significance (5). BRD7 also associates with the BRCA1 protein, an interaction that facilitates recruitment of BRCA1 to the ERα gene promoter (6).

$260
100 µl
APPLICATIONS
REACTIVITY
All Species Expected

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

Background: Halogenated nucleotides such as the pyrimidine analog bromodeoxyuridine (BrdU) are useful for labeling nascent DNA in living cells and tissues. BrdU becomes incorporated into replicating DNA in place of thymidine and subsequent immunodetection of BrdU using specific monoclonal antibodies allows labeling of cells in S phase of the cell cycle. After pulse-labeling cells or tissues with bromodeoxyuridine, BrdU (Bu20a) Mouse mAb can be used to detect BrdU incorporated into single stranded DNA. Please see our detailed protocol for information regarding the labeling procedure and denaturation of double stranded DNA for various immunodetection applications (1-4).

$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 BrdU (Bu20a) Mouse mAb #5292.
APPLICATIONS
REACTIVITY
All Species Expected

Application Methods: Flow Cytometry

Background: Halogenated nucleotides such as the pyrimidine analog bromodeoxyuridine (BrdU) are useful for labeling nascent DNA in living cells and tissues. BrdU becomes incorporated into replicating DNA in place of thymidine and subsequent immunodetection of BrdU using specific monoclonal antibodies allows labeling of cells in S phase of the cell cycle. After pulse-labeling cells or tissues with bromodeoxyuridine, BrdU (Bu20a) Mouse mAb can be used to detect BrdU incorporated into single stranded DNA. Please see our detailed protocol for information regarding the labeling procedure and denaturation of double stranded DNA for various immunodetection applications (1-4).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The breast cancer susceptibility gene, BRCA1, codes for an E3 ubiquitin ligase that functions in the maintenance of genome stability through regulation of the DNA damage response and DNA repair. BRCA1 protein forms at least three distinct complexes (BRCA1 A, B, and C) with other DNA repair proteins, and these interactions are vital for regulation of BRCA1 function. The BRCA1 A complex includes Rap80, BRCC36, Abraxas, MERIT40/NBA1, and BRE/BRCC45 and functions in G2/M phase checkpoint control (reviewed in 1,2). MERIT40 and BRE maintain the stability of both the BRCA1 A complex and the cytoplasmic BRISC complex, which contains BRCC36 and ABRO1 but not BRCA1 (3).Researchers have shown that the expression level of BRE is related to patient survival in breast cancer (4), and it may predict a favorable outcome in acute myeloid leukemia (AML) (5,6). Studies have also shown that BRE is overexpressed in human hepatocellular carcinoma (7) and that overexpression of BRE can cause resistance to apoptotic signaling and promote tumor growth (7,8).

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

Application Methods: Chromatin IP, Chromatin IP-seq, Immunoprecipitation, Western Blotting

Background: ATP-dependent chromatin remodeling complexes play an essential role in the regulation of various nuclear processes, such as gene expression, DNA replication, and repair (1,2). The SWI/SNF chromatin remodeling complex consists of more than 10 subunits with a single molecule of the ATPase catalytic subunit BRM or BRG1, but not both. The activities of these two subunits drive the disruption of histone-DNA contacts that lead to changes in accessibility of crucial regulatory elements within chromatin (2-5). The BRM/BRG1 containing SWI/SNF complexes are recruited to target promoters by transcription factors, such as nuclear receptors, p53, RB, and BRCA1 to regulate gene activation, cell growth, the cell cycle, and differentiation processes (1,6-9). BRM and BRG1 are also considered to be tumor suppressors and their expression levels are severely reduced in several cancer cell lines (10-13).

$269
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: The modulation of chromatin structure is an essential component in the regulation of transcriptional activation and repression. Modifications can be made by at least two evolutionarily conserved strategies, through the disruption of histone-DNA contacts by ATP-dependent chromatin remodelers, or by histone tail modifications including methylation and acetylation. One of the four classes of ATP-dependent histone remodelers is the SWI/SNF complex, the central catalytic subunit of which is Brg1 or the highly related protein hBRM (1). This SWI/SNF complex contains varying subunits but its association with either Brg1 or hBRM remains constant (1). SWI/SNF complexes have been shown to regulate gene activation, cell growth, the cell cycle and differentiation (1). Brg1/hBRM have been shown to regulate transcription through enhancing transcriptional activation of glucocorticoid receptors (2). Although usually associated with transcriptional activation, Brg1/hBRM have also been found in complexes associated with transcriptional repression including with HDACs, Rb and Tif1β (3-5). Brg1/hBRM plays a vital role in the regulation of gene transcription during early mammalian embryogenesis. In addition, Brg1/hBRM also play a role as a tumor suppressors and Brg1 is mutated in several tumor cell lines (6-8).

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

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: The modulation of chromatin structure is an essential component in the regulation of transcriptional activation and repression. Modifications can be made by at least two evolutionarily conserved strategies, through the disruption of histone-DNA contacts by ATP-dependent chromatin remodelers, or by histone tail modifications including methylation and acetylation. One of the four classes of ATP-dependent histone remodelers is the SWI/SNF complex, the central catalytic subunit of which is Brg1 or the highly related protein hBRM (1). This SWI/SNF complex contains varying subunits but its association with either Brg1 or hBRM remains constant (1). SWI/SNF complexes have been shown to regulate gene activation, cell growth, the cell cycle and differentiation (1). Brg1/hBRM have been shown to regulate transcription through enhancing transcriptional activation of glucocorticoid receptors (2). Although usually associated with transcriptional activation, Brg1/hBRM have also been found in complexes associated with transcriptional repression including with HDACs, Rb and Tif1β (3-5). Brg1/hBRM plays a vital role in the regulation of gene transcription during early mammalian embryogenesis. In addition, Brg1/hBRM also play a role as a tumor suppressors and Brg1 is mutated in several tumor cell lines (6-8).

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

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

Background: ATP-dependent chromatin remodeling complexes play an essential role in the regulation of various nuclear processes, such as gene expression, DNA replication, and repair (1,2). The SWI/SNF chromatin remodeling complex consists of more than 10 subunits with a single molecule of the ATPase catalytic subunit BRM or BRG1, but not both. The activities of these two subunits drive the disruption of histone-DNA contacts that lead to changes in accessibility of crucial regulatory elements within chromatin (2-5). The BRM/BRG1 containing SWI/SNF complexes are recruited to target promoters by transcription factors, such as nuclear receptors, p53, RB, and BRCA1 to regulate gene activation, cell growth, the cell cycle, and differentiation processes (1,6-9). BRM and BRG1 are also considered to be tumor suppressors and their expression levels are severely reduced in several cancer cell lines (10-13).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Chromatin IP, Chromatin IP-seq, Immunofluorescence (Frozen), Immunoprecipitation, Western Blotting

Background: Brn2/POU3F2 is a POU domain-containing transcription factor involved in neuronal differentiation and activation of the corticotrophin-releasing hormone gene (1,2). In mice, disruption of the Brn2 gene results in loss of specific neuronal lineages in the hypothalamus (3). In addition to its role in mammalian neurogenesis, Brn2 has also been implicated in melanoma tumorigenesis and has been shown in the literature to be overexpressed in human melanoma cells compared to normal melanocytes (4,5). Recent studies also identify Brn2 as a transcription factor playing an important role in keratinocyte differentiation (6). Recent reports demonstrate that overexpression of three transcription factors (Brn2, Ascl1, and Myt1L) can directly convert human fibroblasts into functional neurons under precisely defined conditions (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Brain-specific kinase 1 (BRSK1; SAD-B) and Brain-specific kinase 2 (BRSK2; SAD-A) are serine/threonine kinases closely related to AMPK. LKB1 phosphorylates Thr189 in the T-loop of BRSK1 and Thr174 in the T-loop of BRSK2, resulting in activation of the kinases (1). BRSK1 localizes to synaptic vesicles in the hippocampus and cerebellum, together with the active zone proteins Bassoon and CAST, and BRSK1 phoshorylates the active zone protein RIM1 (2). An alternatively spliced from of BRSK1 displays unique activity during the cell cycle, phosphorylating Ser131 of γ-tubulin and controling centrosome duplication (3). Neuronal polarization, including axon formation, is fundamental for normal brain development. BRSK1 -/- and BRSK2 -/- mice have defects in neuronal polarity and impaired corticogenesis (4). Knockdown of BRSK1 and BRSK2 in vitro diminishes axonal growth (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Brain-specific kinase 1 (BRSK1; SAD-B) and Brain-specific kinase 2 (BRSK2; SAD-A) are serine/threonine kinases closely related to AMPK. LKB1 phosphorylates Thr189 in the T-loop of BRSK1 and Thr174 in the T-loop of BRSK2, resulting in activation of the kinases (1). BRSK1 localizes to synaptic vesicles in the hippocampus and cerebellum, together with the active zone proteins Bassoon and CAST, and BRSK1 phoshorylates the active zone protein RIM1 (2). An alternatively spliced from of BRSK1 displays unique activity during the cell cycle, phosphorylating Ser131 of γ-tubulin and controling centrosome duplication (3). Neuronal polarization, including axon formation, is fundamental for normal brain development. BRSK1 -/- and BRSK2 -/- mice have defects in neuronal polarity and impaired corticogenesis (4). Knockdown of BRSK1 and BRSK2 in vitro diminishes axonal growth (5).