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Monoclonal Antibody Nuclear Membrane

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

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

Background: Nucleoporin 98 kDa (NUP98) is a component of the nuclear pore complex. It is expressed as three different precursors that undergo auto-cleavage to generate a common amino-terminal 98 kDa peptide (NUP98) and carboxy-terminal 6, 96 (NUP96) and 88 (p88) kDa peptides (1,2). NUP98 contains FG and GLFG repeat domains at its amino terminus and a RNA-binding domain in its carboxy terminus (3). The NUP98 gene is localized on chromosome 11p15.5, a region frequently rearranged in leukemias. To date, 15 fusion partners have been identified for NUP98 (4,5).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Nur77, also known as TR3 and NGFI-B, is an immediate-early response gene and an orphan member of the steroid/thyroid/retinoid receptor superfamily (1-3). Nur77 is composed of an amino-terminal transactivation domain, a central DNA-binding domain and a carboxy-terminal ligand-binding domain. Expression of Nur77 is rapidly induced by a variety of stimuli, including apoptotic, mitogenic and stress signals (1-6). It has been proposed to have many functions related to cell proliferation, differentiation and apoptosis. Nur77 has been extensively studied in T cells where it has been implicated in the process of negative selection and TCR-mediated apoptosis (5,6). Nur77 binds to specific DNA elements leading to the regulation of target genes (7). As a possible mechanism for regulating apoptosis, Nur77 can induce the expression of apoptotic genes such as FasL and TRAIL (8,9). Nur77 is heavily phosphorylated by multiple kinases, which may affect its transactivation activity as well as its subcellular localization (4,10,11). Translocation of Nur77 from the nucleus to the mitochondria can regulate its association with Bcl-2 and control the release of cytochrome c, thereby triggering apoptosis (12,13).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Lamins are nuclear membrane structural components that are important in maintaining normal cell functions such as cell cycle control, DNA replication, and chromatin organization (1-3). Lamin A/C is cleaved by caspase-6 and serves as a marker for caspase-6 activation. During apoptosis, lamin A/C is specifically cleaved into a large (41-50 kDa) and a small (28 kDa) fragment (3,4). The cleavage of lamins results in nuclear dysregulation and cell death (5,6).

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

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

Background: Lamins are nuclear membrane structural components that are important in maintaining normal cell functions such as cell cycle control, DNA replication, and chromatin organization (1-3). Lamin A/C is cleaved by caspase-6 and serves as a marker for caspase-6 activation. During apoptosis, lamin A/C is specifically cleaved into a large (41-50 kDa) and a small (28 kDa) fragment (3,4). The cleavage of lamins results in nuclear dysregulation and cell death (5,6).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 488 fluorescent dye and tested in-house for direct flow cytometry and immunofluorescent analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Lamin A/C (4C11) Mouse mAb #4777.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Frozen), Immunofluorescence (Immunocytochemistry)

Background: Lamins are nuclear membrane structural components that are important in maintaining normal cell functions such as cell cycle control, DNA replication, and chromatin organization (1-3). Lamin A/C is cleaved by caspase-6 and serves as a marker for caspase-6 activation. During apoptosis, lamin A/C is specifically cleaved into a large (41-50 kDa) and a small (28 kDa) fragment (3,4). The cleavage of lamins results in nuclear dysregulation and cell death (5,6).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Lamin A/C (4C11) Mouse mAb #4777.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry

Background: Lamins are nuclear membrane structural components that are important in maintaining normal cell functions such as cell cycle control, DNA replication, and chromatin organization (1-3). Lamin A/C is cleaved by caspase-6 and serves as a marker for caspase-6 activation. During apoptosis, lamin A/C is specifically cleaved into a large (41-50 kDa) and a small (28 kDa) fragment (3,4). The cleavage of lamins results in nuclear dysregulation and cell death (5,6).

$305
100 µl
This Cell Signaling Technology antibody is conjugated to biotin under optimal conditions. The biotinylated antibody is expected to exhibit the same species cross-reactivity as the unconjugated Lamin A/C (4C11) Mouse mAb #4777.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Lamins are nuclear membrane structural components that are important in maintaining normal cell functions such as cell cycle control, DNA replication, and chromatin organization (1-3). Lamin A/C is cleaved by caspase-6 and serves as a marker for caspase-6 activation. During apoptosis, lamin A/C is specifically cleaved into a large (41-50 kDa) and a small (28 kDa) fragment (3,4). The cleavage of lamins results in nuclear dysregulation and cell death (5,6).

$260
100 µg
APPLICATIONS
REACTIVITY
Human

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

Background: Lamins are nuclear membrane structural components that are important in maintaining normal cell functions such as cell cycle control, DNA replication, and chromatin organization (1-3). Lamin A/C is cleaved by caspase-6 and serves as a marker for caspase-6 activation. During apoptosis, lamin A/C is specifically cleaved into a large (41-50 kDa) and a small (28 kDa) fragment (3,4). The cleavage of lamins results in nuclear dysregulation and cell death (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: The nuclear pore complex (NPC) is a multi-subunit protein channel that spans the nuclear envelope and is responsible for the nucleocytoplasmic trafficking of RNA, proteins, and ribonucleoproteins (1,2). Nucleoporin 153 kDa (NUP153) protein functions as a scaffolding element that recruits other proteins to form the “nuclear basket” on the nuclear side of the pore complex. NUP153 is essential for normal nucleocytoplasmic transport of proteins and mRNAs and is critical for the quality control and retention of unspliced mRNAs in the nucleus (1,2). NUP153 is a potential DNA-binding subunit of the NPC and is important for proper regulation of embryonic stem cell pluripotency and differentiation (1,3). Depletion of NUP153 leads to derepression of developmental genes and induction of early differentiation. NUP153 binds to Nucleoporin-Associated Regions (NARs) that are found near the transcriptional start sites of developmental genes and mediates recruitment of Polycomb Repressor Complex 1 (PRC1) to repress transcription in embryonic stem cells (3).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Nucleoporin 98 kDa (NUP98) is a component of the nuclear pore complex. It is expressed as three different precursors that undergo auto-cleavage to generate a common amino-terminal 98 kDa peptide (NUP98) and carboxy-terminal 6, 96 (NUP96) and 88 (p88) kDa peptides (1,2). NUP98 contains FG and GLFG repeat domains at its amino terminus and a RNA-binding domain in its carboxy terminus (3). The NUP98 gene is localized on chromosome 11p15.5, a region frequently rearranged in leukemias. To date, 15 fusion partners have been identified for NUP98 (4,5).

$348
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 Nur77 (D63C5) XP® Rabbit mAb #3960.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: Nur77, also known as TR3 and NGFI-B, is an immediate-early response gene and an orphan member of the steroid/thyroid/retinoid receptor superfamily (1-3). Nur77 is composed of an amino-terminal transactivation domain, a central DNA-binding domain and a carboxy-terminal ligand-binding domain. Expression of Nur77 is rapidly induced by a variety of stimuli, including apoptotic, mitogenic and stress signals (1-6). It has been proposed to have many functions related to cell proliferation, differentiation and apoptosis. Nur77 has been extensively studied in T cells where it has been implicated in the process of negative selection and TCR-mediated apoptosis (5,6). Nur77 binds to specific DNA elements leading to the regulation of target genes (7). As a possible mechanism for regulating apoptosis, Nur77 can induce the expression of apoptotic genes such as FasL and TRAIL (8,9). Nur77 is heavily phosphorylated by multiple kinases, which may affect its transactivation activity as well as its subcellular localization (4,10,11). Translocation of Nur77 from the nucleus to the mitochondria can regulate its association with Bcl-2 and control the release of cytochrome c, thereby triggering apoptosis (12,13).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Methyltransferase-like protein 3 (METTL3) and methytransferase-like protein 14 (METTL14) are the two catalytic subunits of an N6-methyltransferase complex that methylates adenosine residues in RNA (1). Methylation of adenosine residues regulates mRNA splicing, processing, translation efficiency, editing and stability, in addition to regulating primary miRNA processing, and is critical for proper regulation of the circadian clock, embryonic stem cell self-renewal, immune tolerance, response to various stimuli, meiosis and mouse fertility (2,3). In this complex, METTL3 functions as the catalytic methyltransferase subunit and METTL14 functions as the target recognition subunit by binding to RNA (4). In addition, the Wilms tumor 1-associated protein (WTAP) functions as a regulatory subunit and is required for accumulation of the complex to nuclear speckles, which are sites of RNA processing (5). Several studies suggest a role for this complex in cancer. METTL3 expression is elevated in lung adenocarcinoma where it promotes growth, survival and invasion of human lung cancer cells (6). In addition, WTAP is over-expressed in a number of different cancers and positively regulates cell migration and invasion in glioblastoma and cholangiocarcinoma (7,8).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Nur77, also known as TR3 and NGFI-B, is an immediate-early response gene and an orphan member of the steroid/thyroid/retinoid receptor superfamily (1-3). Nur77 is composed of an amino-terminal transactivation domain, a central DNA-binding domain and a carboxy-terminal ligand-binding domain. Expression of Nur77 is rapidly induced by a variety of stimuli, including apoptotic, mitogenic and stress signals (1-6). It has been proposed to have many functions related to cell proliferation, differentiation and apoptosis. Nur77 has been extensively studied in T cells where it has been implicated in the process of negative selection and TCR-mediated apoptosis (5,6). Nur77 binds to specific DNA elements leading to the regulation of target genes (7). As a possible mechanism for regulating apoptosis, Nur77 can induce the expression of apoptotic genes such as FasL and TRAIL (8,9). Nur77 is heavily phosphorylated by multiple kinases, which may affect its transactivation activity as well as its subcellular localization (4,10,11). Translocation of Nur77 from the nucleus to the mitochondria can regulate its association with Bcl-2 and control the release of cytochrome c, thereby triggering apoptosis (12,13).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Emerin is a broadly expressed integral protein of the nuclear inner membrane (1). It contains a LEM domain and binds to several nuclear proteins, such as BAF (barrier-to-autointegration factor) and A- and B-type lamins, which are important in nuclear functions (2-5). Emerin may regulate gene expression through binding to other transcriptional regulators (6,7). Emerin binds to β-catenin and inhibits its nuclear accumulation (8). Recent studies demonstrate that emerin is required for HIV-1 infectivity (9). Mutations in the gene encoding emerin (EMD) are a major cause of Emery-Dreifuss muscular dystrophy (EDMD), a disorder characterized by progressive skeletal muscle weakening (10).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 647 fluorescent dye and tested in-house for direct immunofluorescent analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated NUP98 (C39A3) Rabbit mAb #2598.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry)

Background: Nucleoporin 98 kDa (NUP98) is a component of the nuclear pore complex. It is expressed as three different precursors that undergo auto-cleavage to generate a common amino-terminal 98 kDa peptide (NUP98) and carboxy-terminal 6, 96 (NUP96) and 88 (p88) kDa peptides (1,2). NUP98 contains FG and GLFG repeat domains at its amino terminus and a RNA-binding domain in its carboxy terminus (3). The NUP98 gene is localized on chromosome 11p15.5, a region frequently rearranged in leukemias. To date, 15 fusion partners have been identified for NUP98 (4,5).

$134
20 µl
$336
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Lamins are nuclear membrane structural components that are important in maintaining normal cell functions such as cell cycle control, DNA replication, and chromatin organization (1-3). Lamin A/C is cleaved by caspase-6 and serves as a marker for caspase-6 activation. During apoptosis, lamin A/C is specifically cleaved into a large (41-50 kDa) and a small (28 kDa) fragment (3,4). The cleavage of lamins results in nuclear dysregulation and cell death (5,6).

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

Application Methods: Western Blotting

Background: MYST1, also known as mammalian male absent on the first (MOF) and lysine acetyltransferase 8 (KAT8), is a member of the MYST (MOZ, YBF2, SAS2 and Tip60) family of histone acetyltransferases (1,2). As the catalytic subunit of two different histone acetyltransferase complexes, MSL and NSL, MYST1 is responsible for the majority of histone H4 lysine 16 acetylation in the cell. MYST1 also acetylates p53 on lysine 120 and is important for activation of pro-apoptotic genes (1,2). As a component of the MSL complex, MYST1 associates with MSL1, MSL2L1, and MSL3L1, and specifically acetylates histone H4 on lysine 16 (3-5). As part of the NSL complex, MYST1 associates with the MLL1 histone methyltransferase complex containing MLL1/KMT2A, ASH2L, HCFC1, WDR5 and RBBP5, and shows broader acetyltransferase activity for histone H4 on lysines 5, 8, and 16 (3-5). MYST1 plays a critical role in the regulation of transcription, DNA repair, autophagy, apoptosis, and emybryonic stem cell pluripotency and differentiation (1,2,6). Loss of MYST1 leads to a global reduction in histone H4 lysine 16 acetylation, a common hallmark found in many human cancers. A reduction of MYST1 protein levels and histone H4 lysine 16 acetylation is associated with poor prognosis in breast, renal, colorectal, gastric, and ovarian cancers (1).

$260
100 µg
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry)

Background: Lamins are nuclear membrane structural components that are important in maintaining normal cell functions, such as cell cycle control, DNA replication, and chromatin organization (1-3). Lamins have been subdivided into types A and B. Type-A lamins consist of lamin A and C, which arise from alternative splicing of the lamin A gene LMNA. Lamin A and C are cleaved by caspases into large (41-50 kDa) and small (28 kDa) fragments, which can be used as markers for apoptosis (4,5). Type-B lamins consist of lamin B1 and B2, encoded by separate genes (6-8). Lamin B1 is also cleaved by caspases during apoptosis (9). Research studies have shown that duplication of the lamin B1 gene LMNB1 is correlated with pathogenesis of the neurological disorder adult-onset leukodystrophy (10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Chromatin IP, Flow Cytometry, Immunoprecipitation, Western Blotting

Background: PHD finger protein 8 (PHF8) is a histone lysine demethylase that functions as a transcriptional activator by specifically demethylating a number of repressive histone methylation marks: mono- and di-methyl-histone H3 Lys9 (H3K9me1 and H3K9me2), di-methyl-histone H3 Lys27 (H3K27me2) and mono-methyl-histone H4 Lys20 (H4K20me1). PHF8 contains an N-terminal zinc finger-like PHD domain that binds tri-methylated histone H3 Lys4 (H3K4Me3) and a C-terminal jumonji domain that is responsible for the demethylase activity (1). Deletion and point mutations (F279S) in the jumonji domain of PHF8 are associated with the onset of X-linked mental retardation (XLMR). In addition, PHF8 is highly expressed in prostate cancer, laryngeal squamous cell carcinoma, and human non-small-cell lung cancer (NSCLC). Its expression is predictive of poor survival (2-4). Overexpression of PHF8 increases cell proliferation and cell motility, while silencing of PHF8 reduces cell proliferation, migration, and invasion (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: 5-Lipoxygenase (5-LO, ALOX5) is an important catalytic enzyme responsible for the biosynthesis of leukotriene LTA4 from arachidonic acid (1,2). Leukotriene synthesis also requires 5-lipoxygenase-activating protein (FLAP, ALOX5AP), a nuclear membrane-bound protein that binds arachidonic acid and is thought to activate 5-LO. A number of related leukotrienes (i.e. B4, C4, D4) are derived from LTA4 and together these lipid mediators function in immune reaction regulation. 5-LO is primarily expressed in polymorphonuclear leukocytes, peripheral blood monocytes, macrophages, and mast cells (1,3). Overexpression of 5-LO protein is seen in certain cancer cells and is associated with poor diagnosis (1,4). Depending upon the cell type, 5-LO is localized to either the cytosol or the nucleus of quiescent cells (5). Following stimulation, 5-LO translocates to the nucleus and associates with FLAP to catalyze LTA4 synthesis (2,3). Phosphorylation of specific residues can regulate 5-LO enzymatic activity. Phosphorylation of 5-LO at Ser523 by PKA family kinases inhibits oxygenase activity (6,7) while MAPKAP2 and ERK family kinase phosphorylation at Ser271 and Ser663 stimulates 5-LO enzymatic activity in vivo (8,9).