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Product listing: CABIN1 (D2B9F) Rabbit mAb, UniProt ID Q9Y6J0 #12660 to Cyclin T1 (D1B6G) Rabbit mAb, UniProt ID O60563 #81464

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Calcineurin binding protein CABIN1 was originally identified as an inhibitor of the calcium-dependent serine/threonine phosphatase, calcineurin. CABIN1 inhibits calcineurin signaling in T cells, regulating T cell receptor (TCR) signaling, transcription, and apoptosis (1-4). CABIN1 represses myocyte enhancer factor 2 (MEF2)-mediated transcription by recruiting chromatin remodeling enzymes (5), and also negatively regulates the activity of the tumor suppressor p53 (6). In response to genotoxic stress, CABIN1 is degraded and releases its inhibition of p53, allowing p53 to elicit cellular stress responses (7). CABIN1 is also involved in regulation of chromatin structure as part of the highly conserved HIRA/UBN1/CABIN1/ASF1A (HUCA) histone chaperone complex (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
All Species Expected

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

Background: The CRISPR associated protein 9 (Cas9) is an RNA-guided DNA nuclease and part of the CRISPR antiviral immunity system that provides adaptive immunity against extra chromosomal genetic material (1). The CRISPR antiviral mechanism of action involves three steps: (i), acquisition of foreign DNA by host bacterium; (ii), synthesis and maturation of CRISPR RNA (crRNA), followed by the formation of RNA-Cas nuclease protein complexes; and (iii), target interference through recognition of foreign DNA by the complex and its cleavage by Cas nuclease activity (2). The type II CRISPR/Cas antiviral immunity system provides a powerful tool for precise genome editing and has potential for specific gene regulation and therapeutic applications (3). The Cas9 protein and a guide RNA consisting of a fusion between a crRNA and a trans-activating crRNA (tracrRNA) must be introduced or expressed in a cell. A 20-nucleotide sequence at the 5' end of the guide RNA directs Cas9 to a specific DNA target site. As a result, Cas9 can be "programmed" to cut various DNA sites both in vitro and in cells and organisms. CRISPR/Cas9 genome editing tools have been used in many organisms, including mouse and human cells (4,5). Research studies demonstrate that CRISPR can be used to generate mutant alleles or reporter genes in rodents and primate embryonic stem cells (6-8).Cas9 (S. aureus) is a Cas9 ortholog that is smaller, but as efficient, as the more commonly used Cas9 ortholog, Cas9 (S. Pyogenes) (9).

$260
100 µl
APPLICATIONS
REACTIVITY
All Species Expected

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

Background: The CRISPR associated protein 9 (Cas9) is an RNA-guided DNA nuclease and part of the CRISPR antiviral immunity system that provides adaptive immunity against extra chromosomal genetic material (1). The CRISPR antiviral mechanism of action involves three steps: (i), acquisition of foreign DNA by host bacterium; (ii), synthesis and maturation of CRISPR RNA (crRNA), followed by the formation of RNA-Cas nuclease protein complexes; and (iii), target interference through recognition of foreign DNA by the complex and its cleavage by Cas nuclease activity (2). The type II CRISPR/Cas antiviral immunity system provides a powerful tool for precise genome editing and has potential for specific gene regulation and therapeutic applications (3). The Cas9 protein and a guide RNA consisting of a fusion between a crRNA and a trans-activating crRNA (tracrRNA) must be introduced or expressed in a cell. A 20-nucleotide sequence at the 5' end of the guide RNA directs Cas9 to a specific DNA target site. As a result, Cas9 can be "programmed" to cut various DNA sites both in vitro and in cells and organisms. CRISPR/Cas9 genome editing tools have been used in many organisms, including mouse and human cells (4,5). Research studies demonstrate that CRISPR can be used to generate mutant alleles or reporter genes in rodents and primate embryonic stem cells (6-8).Cas9 (S. aureus) is a Cas9 ortholog that is smaller, but as efficient, as the more commonly used Cas9 ortholog, Cas9 (S. Pyogenes) (9).

$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 Cas9 (S. aureus) (E4G3U) Rabbit mAb #51610.
APPLICATIONS
REACTIVITY
All Species Expected

Application Methods: Flow Cytometry

Background: The CRISPR associated protein 9 (Cas9) is an RNA-guided DNA nuclease and part of the CRISPR antiviral immunity system that provides adaptive immunity against extra chromosomal genetic material (1). The CRISPR antiviral mechanism of action involves three steps: (i), acquisition of foreign DNA by host bacterium; (ii), synthesis and maturation of CRISPR RNA (crRNA), followed by the formation of RNA-Cas nuclease protein complexes; and (iii), target interference through recognition of foreign DNA by the complex and its cleavage by Cas nuclease activity (2). The type II CRISPR/Cas antiviral immunity system provides a powerful tool for precise genome editing and has potential for specific gene regulation and therapeutic applications (3). The Cas9 protein and a guide RNA consisting of a fusion between a crRNA and a trans-activating crRNA (tracrRNA) must be introduced or expressed in a cell. A 20-nucleotide sequence at the 5' end of the guide RNA directs Cas9 to a specific DNA target site. As a result, Cas9 can be "programmed" to cut various DNA sites both in vitro and in cells and organisms. CRISPR/Cas9 genome editing tools have been used in many organisms, including mouse and human cells (4,5). Research studies demonstrate that CRISPR can be used to generate mutant alleles or reporter genes in rodents and primate embryonic stem cells (6-8).Cas9 (S. aureus) is a Cas9 ortholog that is smaller, but as efficient, as the more commonly used Cas9 ortholog, Cas9 (S. Pyogenes) (9).

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

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

Background: CBP (CREB-binding protein) and p300 are highly conserved and functionally related transcriptional co-activators that associate with transcriptional regulators and signaling molecules, integrating multiple signal transduction pathways with the transcriptional machinery (1,2). CBP/p300 also contain histone acetyltransferase (HAT) activity, allowing them to acetylate histones and other proteins (2). Phosphorylation of p300 at Ser89 by PKC represses its transciptional acitivity, and phosphorylation at the same site by AMPK disrupts the association of p300 with nuclear receptors (3,4). Ser1834 phosphorylation of p300 by Akt disrupts its association with C/EBPβ (5). Growth factors induce phosphorylation of CBP at Ser437, which is required for CBP recruitment to the transcription complex (6). CaM kinase IV phosphorylates CBP at Ser302, which is required for CBP-dependent transcriptional activation in the CNS (7). The role of acetylation of CBP/p300 is of particular interest (2,8). Acetylation of p300 at Lys1499 has been demonstrated to enhance its HAT activity and affect a wide variety of signaling events (9).

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

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

Background: CBP (CREB-binding protein) and p300 are highly conserved and functionally related transcriptional co-activators that associate with transcriptional regulators and signaling molecules, integrating multiple signal transduction pathways with the transcriptional machinery (1,2). CBP/p300 also contain histone acetyltransferase (HAT) activity, allowing them to acetylate histones and other proteins (2). Phosphorylation of p300 at Ser89 by PKC represses its transciptional acitivity, and phosphorylation at the same site by AMPK disrupts the association of p300 with nuclear receptors (3,4). Ser1834 phosphorylation of p300 by Akt disrupts its association with C/EBPβ (5). Growth factors induce phosphorylation of CBP at Ser437, which is required for CBP recruitment to the transcription complex (6). CaM kinase IV phosphorylates CBP at Ser302, which is required for CBP-dependent transcriptional activation in the CNS (7). The role of acetylation of CBP/p300 is of particular interest (2,8). Acetylation of p300 at Lys1499 has been demonstrated to enhance its HAT activity and affect a wide variety of signaling events (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

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

Background: The polycomb group (PcG) proteins contribute 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). CBX4 is a component of the PRC1 complex, which together with Ring1 strongly enhances the E3 ubiquitin ligase activity of the Ring2 catalytic subunit (7,8). CBX4 itself is a SUMO E3 ligase, and its function influences EMT, DNA damage response, tumor angiogenesis, and self-renewal (9-13).

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

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

Background: The polycomb group (PcG) proteins contribute 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: PRC1 and PRC2. PRC1 is a multi-subunit protein complex consisting of a combination of five core protein families: CBX, RING1, PHC, PCGF, and RYPB (5-7). Different combinations of protein family members lead to a diverse array of PRC1 complexes with distinct functions (8). At least two distinct classes of PRC1 complexes have been defined. The first class, known as canonical PRC1, contains RING1, PHC, PCGF and CBX protein subunits, but not RYPB (5-8). This class of PRC1 complexes requires PRC2 and H3K27Me3 for proper recruitment to target genes. CBX proteins mediate recruitment by binding to H3K27Me3. CBX8 in particular is required for repression of many lineage-specific genes during differentiation of hematopoietic stem cells and may play a role in activation of lineage-specific genes during differentiation of embryonic stem cells (9,10). The second class, known as variant PRC1, contains RYPB instead of CBX proteins (5-8). RYBP-containing PRC1 is recruited to chromatin independently of PRC2 and H3K27Me3. These variant PRC1 complexes can function independently of PRC2, or in some cases function upstream to recruit PRC2 complex to target genes.

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: Modulation of chromatin structure plays a critical role in the regulation of transcription and replication of the eukaryotic genome. The nucleosome, made up of four core histone proteins (H2A, H2B, H3, and H4), is the primary building block of chromatin. In addition to the growing number of post-translational histone modifications regulating chromatin structure, cells can also exchange canonical histones with variant histones that can directly or indirectly modulate chromatin structure (1). CENP-A, also known as the chromatin-associated protein CSE4 (capping-enzyme suppressor 4-p), is an essential histone H3 variant that replaces canonical histone H3 in centromeric heterochromatin (2). The greatest divergence between CENP-A and canonical histone H3 occurs in the amino-terminal tail of the protein, which binds linker DNA between nucleosomes and facilitates proper folding of centromeric heterochromatin (3). The amino-terminal tail of CENP-A is also required for recruitment of other centromeric proteins (CENP-C, hSMC1, hZW10), proper kinetochore assembly and chromosome segregation during mitosis (4). Additional sequence divergence in the histone fold domain is responsible for correct targeting of CENP-A to the centromere (5). Many of the functions of CENP-A are regulated by phosphorylation (6,7). Aurora A-dependent phosphorylation of CENP-A on Ser7 during prophase is required for proper targeting of Aurora B to the inner centromere in prometaphase, proper kinetochore/microtubule attachment and proper alignment of chromosomes during mitosis (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Modulation of chromatin structure plays a critical role in the regulation of transcription and replication of the eukaryotic genome. The nucleosome, made up of four core histone proteins (H2A, H2B, H3, and H4), is the primary building block of chromatin. In addition to the growing number of post-translational histone modifications regulating chromatin structure, cells can also exchange canonical histones with variant histones that can directly or indirectly modulate chromatin structure (1). CENP-A, also known as the chromatin-associated protein CSE4 (capping-enzyme suppressor 4-p), is an essential histone H3 variant that replaces canonical histone H3 in centromeric heterochromatin (2). The greatest divergence between CENP-A and canonical histone H3 occurs in the amino-terminal tail of the protein, which binds linker DNA between nucleosomes and facilitates proper folding of centromeric heterochromatin (3). The amino-terminal tail of CENP-A is also required for recruitment of other centromeric proteins (CENP-C, hSMC1, hZW10), proper kinetochore assembly and chromosome segregation during mitosis (4). Additional sequence divergence in the histone fold domain is responsible for correct targeting of CENP-A to the centromere (5). Many of the functions of CENP-A are regulated by phosphorylation (6,7). Aurora A-dependent phosphorylation of CENP-A on Ser7 during prophase is required for proper targeting of Aurora B to the inner centromere in prometaphase, proper kinetochore/microtubule attachment and proper alignment of chromosomes during mitosis (6).

$293
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: Chromatin assembly factor 1 (CAF-1) is a histone H3/H4 chaperone complex that functions in de novo assembly of nucleosomes during DNA replication and nucleotide excision repair (1). Nucleosome assembly is a two-step process, involving initial deposition of a histone H3/H4 tetramer onto DNA, followed by the deposition of a pair of histone H2A/H2B dimers (1). CAF-1 interacts with PCNA and localizes to DNA replication and DNA repair foci, where it functions to assemble newly synthesized histone H3/H4 tetramers onto replicating DNA (2-6). Assembly of histone H2A/H2B dimers requires additional assembly factors. The CAF-1 complex consists of three proteins: CHAF1A (p150), CHAF1B (p60) and RBAP48 (p48 or RBBP4). CHAF1A and CHAF1B proteins are specific for the CAF-1 complex, while RBAP48 is a component of multiple chromatin modifying complexes (1). CHAF1A and CHAF1B expression levels correlate with cellular proliferation and both proteins are significantly down-regulated in quiescent cells (7).

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

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: Chromodomain-helicase-DNA-binding domain (CHD) proteins have been identified in a variety of organisms (1,2). This family of proteins, which consists of nine members, has been divided into three separate subfamilies: subfamily I (CHD1 and CHD2), subfamily II (CHD3 and CHD4), and subfamily III (CHD5, CHD6, CHD7, CHD8, and CHD9). All of the CHD proteins contain two tandem N-terminal chromodomains, a SWI/SNF-related ATPase domain, and a C-terminal DNA binding domain (1,2). The chromodomains facilitate binding to methylated lysine residues of histone proteins and confer interactions with specific regions of chromatin. The SWI/SNF-related ATPase domain utilizes the energy from ATP hydrolysis to modify chromatin structure. CHD1 is a euchromatic protein that associates with the promoters of active genes, and is required for the maintenance of open chromatin and pluripotency in embryonic stem cells (3-6). The two chromodomains of CHD1 facilitate its recruitment to active genes by binding to methyl-lysine 4 of histone H3, a mark associated with transcriptional activation (4-6). Yeast CHD1 is a component of the SAGA and SLIK histone acetyltransferase complexes, and is believed to link histone methylation with histone acetylation during transcriptional activation (6). The CHD2 protein is not well characterized; however, mouse knockout studies suggest important functions in development and tumor suppression. Homozygous CHD2 knockout mice exhibit delayed growth and perinatal lethality (7). Heterozygous knockout mice show increased mortality and gross organ abnormalities, in addition to increased extramedullary hematopoiesis and susceptibility to lymphomas (7,8). CHD2 mutant cells are defective in hematopoietic stem cell differentiation and exhibit aberrant DNA damage responses (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Chromodomain-helicase-DNA-binding domain 1 like (CHD1L) is a DNA helicase and member of the SNF2 subfamily of ATP dependent chromatin remodeling enzymes (1). Unlike other CHD chromatin remodeling proteins, CHD1L lacks a methylated histone binding chromodomain but does contain a macro domain that binds poly-ADP ribosylated (PARylated) targets (1,2). Following genotoxic stress, CHD1L interacts with PARylated PARP1 and is recruited to sites of DNA damage to facilitate DNA repair (3,4). The CHD1L protein is often over expressed in metastatic hepatocellular carcinoma (HCC) and the corresponding CHD1L gene is located in a region that is frequently amplified in cases of HCC (5-7). Research studies indicate that CHD1L over expression may lead to over relaxation of chromatin and exposing the underlying DNA to genotoxic stress (1). CHD1L can regulate expression of genes that promote tumor cell proliferation, migration and metastasis, providing another mechanism where CHD1L may promote hepatocellular carcinoma progression and metastasis (6,8). Additional research studies suggest that over expression of CHD1L may be involved in the progression of bladder, colon and ovary cancer (9-11).

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

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

Background: Chromodomain-helicase-DNA-binding domain (CHD) proteins have been identified in a variety of organisms (1,2). This family of nine proteins is divided into three separate subfamilies: subfamily I (CHD1 and CHD2), subfamily II (CHD3 and CHD4), and subfamily III (CHD5, CHD6, CHD7, CHD8, and CHD9). All CHD proteins contain two tandem amino-terminal chromodomains, a SWI/SNF-related ATPase domain, and a carboxy-terminal DNA-binding domain (1,2). The chromodomains facilitate binding to methylated lysine residues of histone proteins and confer interactions with specific regions of chromatin. The SWI/SNF-related ATPase domain utilizes energy from ATP hydrolysis to modify chromatin structure. CHD proteins are often found in large, multiprotein complexes with their transcriptional activation or repression activity governed by other proteins within the complex. CHD3 (also known as Mi2-α) and CHD4 (also known as Mi2-β) are central components of the nucleosome remodeling and histone deacetylase (NuRD) transcriptional repressor complex, which also contains HDAC1, HDAC2, RBAP48, RBAP46, MTA1, MTA2, MTA3, and MBD3 (3-8). Both CHD3 and CHD4 contain two plant homeodomain (PHD) zinc finger domains that bind directly to HDAC1 and HDAC2.

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Chromodomain-helicase-DNA-binding domain (CHD) proteins have been identified in a variety of organisms (1,2). This family of nine proteins is divided into three separate subfamilies: subfamily I (CHD1 and CHD2), subfamily II (CHD3 and CHD4), and subfamily III (CHD5, CHD6, CHD7, CHD8, and CHD9). All CHD proteins contain two tandem amino-terminal chromodomains, a SWI/SNF-related ATPase domain, and a carboxy-terminal DNA-binding domain (1,2). The chromodomains facilitate binding to methylated lysine residues of histone proteins and confer interactions with specific regions of chromatin. The SWI/SNF-related ATPase domain utilizes energy from ATP hydrolysis to modify chromatin structure. CHD proteins are often found in large, multiprotein complexes with their transcriptional activation or repression activity governed by other proteins within the complex. CHD3 (also known as Mi2-α) and CHD4 (also known as Mi2-β) are central components of the nucleosome remodeling and histone deacetylase (NuRD) transcriptional repressor complex, which also contains HDAC1, HDAC2, RBAP48, RBAP46, MTA1, MTA2, MTA3, and MBD3 (3-8). Both CHD3 and CHD4 contain two plant homeodomain (PHD) zinc finger domains that bind directly to HDAC1 and HDAC2.

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: CHD5 (chromodomain-helicase-DNA-binding-5) is one of the 9 known CHD proteins and is homologous to its family members, CHD3 and CHD4 (1-3). CHD5 interacts with the nucleosome remodeling and deacetylation (NuRD) complex (1,4). CHD5 is characterized by two PHD domains, two chromo domains, a SNF2-like helicase/ATPase domain, as well as a conserved coiled-coil motif in the C-terminal region (1). CHD5 binds to the N-terminus of Histone H3 via its PHD domains (1). CHD5 was first characterized as a tumor suppressor gene found to be frequently lost in neuroblastomas (1). Since its initial discovery, CHD5 has been studied extensively and has been implicated in numerous other cancers including gliomas, breast, lung, ovarian, and prostate cancers as well as in laryngeal squamous cell carcinomas and gallbladder carcinoma (1). CHD5 is thought to be a prognostic marker in neuroblastoma patients. High CHD5 levels are strongly correlated with favorable clinical outcomes, whereas low or absent expression is associated with MYCN amplification and poor outcomes (1). In addition, CHD5 has a dual function in neurogenesis, playing a transcription activating role in neurogenesis, while interacting with the Polycomb group proteins to repress genes encoding regulators of other lineages. Deletion of CHD5 also inhibits neuronal differentiation leading to the accumulation of undifferentiated progenitors (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: CHD7 belongs to the chromodomain helicase DNA-binding (CHD) family of ATP-dependent chromatin remodeling proteins (1). The CHD family of proteins has been shown to play an important role in regulating gene expression by altering the chromatin structure at target genes (1,2). The nine members of the CHD family are characterized by the presence of two tandem chromodomains in the N-terminal region and an SNF2-like ATPase domain near the central region of the protein (2-4). The CHD proteins can be further divided into three subgroups based on the presence of additional conserved functional domains. CHD7 belongs to the third subgroup of CHD proteins together with CHD6, 8, and 9, which are distinguished by the presence of three conserved region (CR) domains, a switching-defective protein 3, adaptor 2, nuclear receptor co-repressor, transcription factor IIB (SANT) like domain, two brahma and kismet (BRK) domains, and a DNA binding domain (2). CHD7 regulates embryonic stem cell (ESC) specific gene expression together with ESC master regulators Oct-4, Sox2 and nanog, and is necessary for neural stem cell development and formation of the neural crest (5-7). Research studies have shown that CHD7 mutations are frequently found in patients with CHARGE syndrome (coloboma of the eye, heart defects, atresia of the choanae, retardation of growth/development, genital/urinary abnormalities, and ear abnormalities and deafness) (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: CHD8 belongs to the chromodomain helicase DNA-binding (CHD) family of ATP-dependent chromatin remodeling proteins (1). The CHD family of proteins has been shown to play an important role in regulating gene expression by utilizing the energy derived from ATP hydrolysis to alter chromatin architecture (1,2). The nine CHD family members are characterized by the presence of two tandem chromodomains in the N-terminal region and an SNF2-like ATPase domain near the central region of the protein (2-4). In addition, CHD8 contains three CR (conserved region) domains, a SANT (switching-defective protein 3, adaptor 2, nuclear receptor co-repressor, transcription factor IIB)-like domain, two BRK (brahma and kismet) domains, and a DNA-binding domain (2). The chromatin remodeling activity of CHD8 has been shown to be important for the regulation of a wide variety of genes, such as the HOX genes (5) and genes that are driven by β-catenin (6), p53 (7), estrogen receptor (8), or androgen receptor (9). CHD8 can also interact with the insulator binding protein CTCF and is required for CTCF insulator activity at multiple gene loci (10).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: CHD8 belongs to the chromodomain helicase DNA-binding (CHD) family of ATP-dependent chromatin remodeling proteins (1). The CHD family of proteins has been shown to play an important role in regulating gene expression by utilizing the energy derived from ATP hydrolysis to alter chromatin architecture (1,2). The nine CHD family members are characterized by the presence of two tandem chromodomains in the N-terminal region and an SNF2-like ATPase domain near the central region of the protein (2-4). In addition, CHD8 contains three CR (conserved region) domains, a SANT (switching-defective protein 3, adaptor 2, nuclear receptor co-repressor, transcription factor IIB)-like domain, two BRK (brahma and kismet) domains, and a DNA-binding domain (2). The chromatin remodeling activity of CHD8 has been shown to be important for the regulation of a wide variety of genes, such as the HOX genes (5) and genes that are driven by β-catenin (6), p53 (7), estrogen receptor (8), or androgen receptor (9). CHD8 can also interact with the insulator binding protein CTCF and is required for CTCF insulator activity at multiple gene loci (10).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Modulation of chromatin structure has a critical role in the control of various DNA directed activities such as transcription, DNA replication, and repair (1). The basic unit of chromatin, the nucleosome, consists of two turns of DNA wrapped around two copies each of four core histone proteins (H2A, H2B, H3, and H4) (2,3). Amino-terminal tails of histones undergo various post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination in response to physiological and environmental stimuli. These modifications modulate the accessibility of chromatin to effector proteins as well as act as binding sites for specific histone modification recognizing effector proteins that regulate gene expression (1,4,5). Such alterations in chromatin modifications and architecture that accompany gene expression changes have been observed during embryonic stem cell differentiation (6). One of the ways in which chromatin modifications may be altered in stem cells involves regulated proteolysis of histone H3 by Cathepsin L. Cathepsin L cleaves the histone H3 amino-terminal tail predominantly at Thr22 in differentiating stem cells, leading to removal of histone modification marks which could then influence the expression patterns of developmentally regulated genes (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: 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.

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

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

Background: Negative Elongation Factor (NELF) consists of four subunits: WHSC2 (NELF-A), COBRA-1 (NELF-B), TH1L (NELF-C/D), and NELF-E (1). NELF, together with DRB-sensitivity inducing factor (DSIF), inhibits RNA Polymerase II (RNAPII) elongation resulting in RNAPII promoter proximal pausing, where it waits additional signaling to resume transcription (2,3). The release of RNAPII from promoter proximal pausing is a critical regulatory point during transcription and is signaled by positive transcription elongation factor (p-TEF-b) phosphorylation of both NELF and the carboxy-terminal domain (CTD) within the largest subunit of RNAPII (3,4). WHSC2 is thought to connect the NELF complex to RNAPII machinery, while NELF-E contains an RNA binding motif that is necessary for NELF function (1,5,6). TH1L, together with COBRA-1, are integral subunits that bring WHSC2 and NELF-E together in the NELF complex (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The REST corepressor 1 (CoREST, RCOR1) was first identified as a repressor element 1-silencing transcription factor (REST) corepressor (1,2). The CoREST protein is encoded by the RCOR1 gene and is part of a large, multi-subunit repressor complex that includes the histone demethylase LSD1 and histone deacetylases (HDAC) 1 and 2 (1,3-5). CoREST binds the carboxy-terminal domain of REST and is recruited to repress neuronal gene transcription in non-neuronal and neural stem cells (1,6,7). The REST corepressor is essential for repressor complex-nucleosome interaction, the subsequent deacetylation of histone amino-terminal tails by HDAC1/2, and the LSD1 methylation of histone H3 at Lys4 (8-10). The targeting of CoREST to genes that are not repressed by REST suggests a role apart from neural cell fate regulation. These include growth factor independent (Gfi) target genes during erythroid differentiation, targets of carboxy-terminal binding protein (CtBP), and heat shock and pro-inflammatory response genes (11-15).

$293
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Rat

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

Background: CCCTC-binding factor (CTCF) and its paralog, the Brother of the Regulator of Imprinted Sites (BORIS), are highly conserved transcription factors that regulate transcriptional activation and repression, insulator function, and imprinting control regions (ICRs) (1-4). Although they have divergent amino and carboxy termini, both proteins contain 11 conserved zinc finger domains that work in combination to bind the same DNA elements (1). CTCF is ubiquitously expressed and contributes to transcriptional regulation of cell-growth regulated genes, including c-myc, p19/ARF, p16/INK4A, BRCA1, p53, p27, E2F1, and TERT (1). CTCF also binds to and is required for the enhancer-blocking activity of all known insulator elements and ICRs, including the H19/IgF2, Prader-Willi/Angelman syndrome, and Inactive X-Specific Transcript (XIST) anti-sense loci (5-7). CTCF DNA-binding is sensitive to DNA methylation, a mark that determines selection of the imprinted allele (maternal vs. paternal) (1). The various functions of CTCF are regulated by at least two different post-translational modifications. Poly(ADP-ribosyl)ation of CTCF is required for insulator function (8). Phosphorylation of Ser612 by protein kinase CK2 facilitates a switch of CTCF from a transcriptional repressor to an activator at the c-myc promoter (9). CTCF mutations or deletions have been found in many breast, prostate, and Wilms tumors (10,11). Expression of BORIS is restricted to spermatocytes and is mutually exclusive of CTCF (3). In cells expressing BORIS, promoters of X-linked cancer-testis antigens like MAGE-1A are demethylated and activated, but methylated and inactive in CTCF-expressing somatic cells (12). Like other testis specific proteins, BORIS is abnormally expressed in different cancers, such as breast cancer, and has a greater affinity than CTCF for DNA binding sites, detracting from CTCF’s potential tumor suppressing activity (1,3,13,14).

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

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

Background: CCCTC-binding factor (CTCF) and its paralog, the Brother of the Regulator of Imprinted Sites (BORIS), are highly conserved transcription factors that regulate transcriptional activation and repression, insulator function, and imprinting control regions (ICRs) (1-4). Although they have divergent amino and carboxy termini, both proteins contain 11 conserved zinc finger domains that work in combination to bind the same DNA elements (1). CTCF is ubiquitously expressed and contributes to transcriptional regulation of cell-growth regulated genes, including c-myc, p19/ARF, p16/INK4A, BRCA1, p53, p27, E2F1, and TERT (1). CTCF also binds to and is required for the enhancer-blocking activity of all known insulator elements and ICRs, including the H19/IgF2, Prader-Willi/Angelman syndrome, and Inactive X-Specific Transcript (XIST) anti-sense loci (5-7). CTCF DNA-binding is sensitive to DNA methylation, a mark that determines selection of the imprinted allele (maternal vs. paternal) (1). The various functions of CTCF are regulated by at least two different post-translational modifications. Poly(ADP-ribosyl)ation of CTCF is required for insulator function (8). Phosphorylation of Ser612 by protein kinase CK2 facilitates a switch of CTCF from a transcriptional repressor to an activator at the c-myc promoter (9). CTCF mutations or deletions have been found in many breast, prostate, and Wilms tumors (10,11). Expression of BORIS is restricted to spermatocytes and is mutually exclusive of CTCF (3). In cells expressing BORIS, promoters of X-linked cancer-testis antigens like MAGE-1A are demethylated and activated, but methylated and inactive in CTCF-expressing somatic cells (12). Like other testis specific proteins, BORIS is abnormally expressed in different cancers, such as breast cancer, and has a greater affinity than CTCF for DNA binding sites, detracting from CTCF’s potential tumor suppressing activity (1,3,13,14).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Rat

Application Methods: Western Blotting

Background: CTD small phosphatase-like protein 2 (CTDSPL2, HSPC129) is a putative RNA-polymerase II carboxy-terminal domain (CTD) phosphatase (1) that belongs to a small subfamily of CTD phosphatases (2). The CTD of RNA polymerase II contains multiple Y-S-P-T-S-P-S repeats that are phosphorylated during the transcription cycle (3,4). In general, CTD phosphatases regulate the reversible CTD phosphorylation state of RNA-polymerase II at several stages of RNA synthesis and during post-transcriptional modification (4-6). CTDSPL2 has several structural and functional similarities to other CTD phosphatases, including FCP1, SCP1, DULLARD, and UBLCP1 (1,2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The PAF (RNA polymerase II (RNAPII) associated factor) complex was initially identified in yeast and is comprised of subunits PAF1, Leo1, Ctr9, Cdc73, RTF1 and Ski8 (1,2). The PAF complex plays an important role in transcription initiation and elongation by RNAPII by regulating the establishment of proper histone modifications such as histone H2B ubiquitination and the recruitment of the histone chaperone FACT (facilitates chromatin transcription) (3-5). The PAF complex also plays a role in mRNA processing and maturation by interacting with and recruiting the cleavage and polyadenylation specificity factor and cleavage stimulation factor complexes via the Cdc73 subunit (6,7). In addition, the Ski8 subunit of the PAF complex is part of the hSKi complex that regulates RNA surveillance, suggesting an important function of the complex in coordinating events associated with proper RNA maturation during transcription (1,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: The CXXC finger protein 1 (CXXC1, CGBP, CFP1) is a key subunit of the human SET1 histone methyltransferase complex (1,2) that methylates histone H3 at Lys4 to create a mark of transcriptionally active promoters (3,4). CXXC1 is enriched at CpG islands where it selectively binds non-methylated CpG motifs to provide a link between global H3K4 methylation and CpG islands (5). Research studies have revealed a role for CXXC1 in the maintenance of cytosine methylation through direct interaction with DNMT1 (6-9). The epigenetic functions of CXXC1 are critical for normal embryonic development. Targeted deletion of the murine Cxxc1 gene results in early embryonic lethality while Cxxc1-null embryonic stem (ES) cells exhibit increased apoptosis and fail to undergo differentiation in vitro following withdrawal of leukemia inhibitory factor LIF (6).

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

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

Background: The CXXC-type zinc finger protein 5 (CXXC5) is a nuclear protein that regulates gene expression and is involved in the regulation of cell growth and differentiation, apoptosis, cell adhesion, and cytoskeletal organization. The CXXC5 protein is also known as retinoid-inducible nuclear factor (RINF) as it was originally identified from a set of genes upregulated by retinoic acid stimulation (1). CXXC5 is a transcriptional activator of the vascular endothelial growth factor receptor VEGFR2. The CXXC5 protein regulates differentiation and migration of endothelial cells and subsequent blood vessel formation downstream of bone morphogenic protein (BMP) signaling (2). CXXC5 also regulates TNFα-induced apoptosis by facilitating phosphorylation of Smad3 and the nuclear translocation of Smad4 (3). Expression of CXXC5 in skeletal muscle regulates expression of genes involved in skeletal myogenesis (4). This nuclear factor also plays an important role in the regulation of normal myelopoiesis. The CXXC5 gene is localized to the 5q31.2 chromosomal region that is often involved in abnormalities associated with various myeloid malignancies, and CXXC5 over-expression is associated with decreased overall survival in human AML (5). Interestingly, CXXC5 is also over-expressed in many solid tumors, and high expression is also correlated with poor prognosis in breast cancer (6).

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

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: Positive transcription elongation factor (P-TEFb) is a heterodimer composed of cyclin T proteins and CDK9. P-TEFb plays a critical role in the transition of the RNA polymerase II (RNAPII) machinery from transcription initiation to elongation (1). At some genes during transcription initiation, RNAPII moves approximately 50 nucleotides away from the transcription start site into the gene where it then pauses and awaits signaling for the formation of a productive transcription elongation complex (1,2). The release of this promoter proximal pausing of RNAPII is signaled by phosphorylation of the C-terminal domain (CTD) within the largest subunit of RNAPII at Ser2 of the heptapeptide repeat sequence by P-TEFb (3). This phosphorylation event is important for the recruitment of mRNA processing factors and chromatin modifiers that are necessary for proper gene expression (4,5). P-TEFb also promotes transcription elongation by phosphorylating DSIF (DRB-induced stimulating factor) and NELF (negative elongation factor), two negative elongation factors that retain RNAPII at the promoter proximal region of genes to initiate transcription elongation (6,7).