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Monoclonal Antibody Germinal Center Formation

Also showing Monoclonal Antibody Positive Regulation of Germinal Center Formation, Monoclonal Antibody Regulation of Germinal Center Formation

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

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

Background: MEF2C is a member of the MEF2 (myocyte enhancer factor 2) family of transcription factors. In mammals, there are four MEF2C-related genes (MEF2A, MEF2B, MEF2C and MEF2D) that encode proteins that exhibit significant amino acid sequence similarity within their DNA binding domains and, to a lesser extent, throughout the rest of the proteins (1). The MEF2 family members were originally described as muscle-specific DNA binding proteins that recognize MEF2 motifs found within the promoters of many muscle-specific genes (2,3). Recently, several groups have reported MEF2 binding activity and MEF2 proteins in a wide variety of cell types where these proteins appear to play an important role in growth factor- and stress-induced early gene responses (4-6).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 488 fluorescent dye 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 BCL6 (D4I2V) XP® Rabbit mAb #14895.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: Chromosomal translocations result in misregulation of the proto-oncogene BCL6 in patients with B cell-derived non-Hodgkin's lymphoma (1). The BCL6 gene is selectively expressed in mature B cells and encodes a nuclear phosphoprotein that belongs to the BTB/POZ zinc finger family of transcription factors (2,3). BCL6 protein can bind to target DNA sequences of Stat6 and, analogous to Stat6, modulate the expression of interleukin-4-induced genes (4). Furthermore, BCL6 restrains p53-dependent senescence, making BCL6-active tumors functionally p53-negative (5). The mitogen-activated protein kinases, Erk1 and Erk2, but not JNK, phosphorylate BCL6 at multiple sites. Phosphorylation of BCL6 at Ser333 and Ser343 results in degradation of BCL6 by the ubiquitin/proteasome pathway in B cells (6,7). In addition, BCL6 is acetylated and its transcriptional repressor function is inhibited by the transcriptional co-activator p300 (8).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: IHC-Leica® Bond™, Immunohistochemistry (Paraffin)

Background: Chromosomal translocations result in misregulation of the proto-oncogene BCL6 in patients with B cell-derived non-Hodgkin's lymphoma (1). The BCL6 gene is selectively expressed in mature B cells and encodes a nuclear phosphoprotein that belongs to the BTB/POZ zinc finger family of transcription factors (2,3). BCL6 protein can bind to target DNA sequences of Stat6 and, analogous to Stat6, modulate the expression of interleukin-4-induced genes (4). Furthermore, BCL6 restrains p53-dependent senescence, making BCL6-active tumors functionally p53-negative (5). The mitogen-activated protein kinases, Erk1 and Erk2, but not JNK, phosphorylate BCL6 at multiple sites. Phosphorylation of BCL6 at Ser333 and Ser343 results in degradation of BCL6 by the ubiquitin/proteasome pathway in B cells (6,7). In addition, BCL6 is acetylated and its transcriptional repressor function is inhibited by the transcriptional co-activator p300 (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: Chromosomal translocations result in misregulation of the proto-oncogene BCL6 in patients with B cell-derived non-Hodgkin's lymphoma (1). The BCL6 gene is selectively expressed in mature B cells and encodes a nuclear phosphoprotein that belongs to the BTB/POZ zinc finger family of transcription factors (2,3). BCL6 protein can bind to target DNA sequences of Stat6 and, analogous to Stat6, modulate the expression of interleukin-4-induced genes (4). Furthermore, BCL6 restrains p53-dependent senescence, making BCL6-active tumors functionally p53-negative (5). The mitogen-activated protein kinases, Erk1 and Erk2, but not JNK, phosphorylate BCL6 at multiple sites. Phosphorylation of BCL6 at Ser333 and Ser343 results in degradation of BCL6 by the ubiquitin/proteasome pathway in B cells (6,7). In addition, BCL6 is acetylated and its transcriptional repressor function is inhibited by the transcriptional co-activator p300 (8).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Chromosomal translocations result in misregulation of the proto-oncogene BCL6 in patients with B cell-derived non-Hodgkin's lymphoma (1). The BCL6 gene is selectively expressed in mature B cells and encodes a nuclear phosphoprotein that belongs to the BTB/POZ zinc finger family of transcription factors (2,3). BCL6 protein can bind to target DNA sequences of Stat6 and, analogous to Stat6, modulate the expression of interleukin-4-induced genes (4). Furthermore, BCL6 restrains p53-dependent senescence, making BCL6-active tumors functionally p53-negative (5). The mitogen-activated protein kinases, Erk1 and Erk2, but not JNK, phosphorylate BCL6 at multiple sites. Phosphorylation of BCL6 at Ser333 and Ser343 results in degradation of BCL6 by the ubiquitin/proteasome pathway in B cells (6,7). In addition, BCL6 is acetylated and its transcriptional repressor function is inhibited by the transcriptional co-activator p300 (8).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 647 fluorescent dye 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 BCL6 (D4I2V) XP® Rabbit mAb #14895.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: Chromosomal translocations result in misregulation of the proto-oncogene BCL6 in patients with B cell-derived non-Hodgkin's lymphoma (1). The BCL6 gene is selectively expressed in mature B cells and encodes a nuclear phosphoprotein that belongs to the BTB/POZ zinc finger family of transcription factors (2,3). BCL6 protein can bind to target DNA sequences of Stat6 and, analogous to Stat6, modulate the expression of interleukin-4-induced genes (4). Furthermore, BCL6 restrains p53-dependent senescence, making BCL6-active tumors functionally p53-negative (5). The mitogen-activated protein kinases, Erk1 and Erk2, but not JNK, phosphorylate BCL6 at multiple sites. Phosphorylation of BCL6 at Ser333 and Ser343 results in degradation of BCL6 by the ubiquitin/proteasome pathway in B cells (6,7). In addition, BCL6 is acetylated and its transcriptional repressor function is inhibited by the transcriptional co-activator p300 (8).

$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 BCL6 (D4I2V) XP® Rabbit mAb #14895.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: Chromosomal translocations result in misregulation of the proto-oncogene BCL6 in patients with B cell-derived non-Hodgkin's lymphoma (1). The BCL6 gene is selectively expressed in mature B cells and encodes a nuclear phosphoprotein that belongs to the BTB/POZ zinc finger family of transcription factors (2,3). BCL6 protein can bind to target DNA sequences of Stat6 and, analogous to Stat6, modulate the expression of interleukin-4-induced genes (4). Furthermore, BCL6 restrains p53-dependent senescence, making BCL6-active tumors functionally p53-negative (5). The mitogen-activated protein kinases, Erk1 and Erk2, but not JNK, phosphorylate BCL6 at multiple sites. Phosphorylation of BCL6 at Ser333 and Ser343 results in degradation of BCL6 by the ubiquitin/proteasome pathway in B cells (6,7). In addition, BCL6 is acetylated and its transcriptional repressor function is inhibited by the transcriptional co-activator p300 (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Adenosine deaminase (ADA) catalyzes adenosine degradation (1). Lack of this enzyme leads to the accumulation of toxic metabolites causing severe combined immunodeficiency (ADA-SCID), an autosomal recessive disorder. Differentiation and function of T cells, B cells, and natural killer cells are impaired in ADA-SCID patients leading to recurrent infections (1,2). Gene therapies for ADA-SCID were reported to correct the metabolic defect and restore the deficient immune function (1-3).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: A20, also referred to as TNF-α-induced protein 3 (TNFAIP3), is cytokine-inducible protein that functions to inhibit apoptosis and activate NF-κB (1,2). It was first identified as a TNF-α inducible primary response gene in human umbilical vein endothelial cells, and encodes a 790-amino acid protein containing seven Cys2/Cys2-zinc finger motifs (3). Constitutive expression of A20 is observed in lymphoid tissues (4), but it is transiently expressed in a variety of cell types in response to inflammatory signals such as TNF-α (3,5), IL-1 (3,5), phorbol esters (6), and LPS (7). Expression of A20 can confer resistance to apoptosis and NF-κB activation triggered by these signals, probably through interference with TRAF (TNF receptor associated factor) family members (8,9), and interaction with the NF-κB inhibiting protein ABIN (10). Studies also show that A20 contains site-specific ubiquitin modifying activity that can contribute to its biological functions (11,12). The amino-terminus of A20 contains de-ubiquitinating (DUB) activity for Lys63 branches, such as those found in TRAF6 and RIP, while the carboxyl-terminus contains ubiquitin ligase (E3) activity for Lys48 branches of the same substrates and leads to their degradation (12).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: TACE (TNF-α converting enzyme), also known as ADAM17, is a transmembrane metalloprotease that plays a key role in the cleavage of a number cell surface molecules in a process known as “shedding". TACE is abundantly expressed in many adult tissues, but in fetal development expression is differentially regulated (1). An important substrate of TACE is pro-TNF-α (1). Increased expression of TACE is associated with several pathological conditions including osteoarthritis and rheumatoid arthritis, where the pro-inflammatory effects of increased TNF-α contribute to disease pathogenesis (2,3). Regulation of other important molecules by TACE such as EGFR and Notch has recently been documented. TACE is responsible for the shedding of EGFR ligands such as amphiregulin and TNF-α. Some tumors have hyperactivated EGFR due to upregulated TNF-α production and upregulated TACE, making TACE a potential target for drug development (4). TACE activates Notch in a ligand-independent manner and has been shown to play a role in the development of the Drosophila nervous system (5). TACE has also been proposed to act as α-secretase for amyloid precursor protein (APP) (6), and to be involved in the renewal and proliferation of neural stem cells (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: Transcription factors of the nuclear factor κB (NF-κB)/Rel family play a pivotal role in inflammatory and immune responses (1,2). There are five family members in mammals: RelA, c-Rel, RelB, NF-κB1 (p105/p50), and NF-κB2 (p100/p52). Both p105 and p100 are proteolytically processed by the proteasome to produce p50 and p52, respectively. Rel proteins bind p50 and p52 to form dimeric complexes that bind DNA and regulate transcription. In unstimulated cells, NF-κB is sequestered in the cytoplasm by IκB inhibitory proteins (3-5). NF-κB-activating agents can induce the phosphorylation of IκB proteins, targeting them for rapid degradation through the ubiquitin-proteasome pathway and releasing NF-κB to enter the nucleus where it regulates gene expression (6-8). NIK and IKKα (IKK1) regulate the phosphorylation and processing of NF-κB2 (p100) to produce p52, which translocates to the nucleus (9-11).

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

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

Background: Transcription factors of the nuclear factor κB (NF-κB)/Rel family play a pivotal role in inflammatory and immune responses (1,2). There are five family members in mammals: RelA, c-Rel, RelB, NF-κB1 (p105/p50), and NF-κB2 (p100/p52). Both p105 and p100 are proteolytically processed by the proteasome to produce p50 and p52, respectively. Rel proteins bind p50 and p52 to form dimeric complexes that bind DNA and regulate transcription. In unstimulated cells, NF-κB is sequestered in the cytoplasm by IκB inhibitory proteins (3-5). NF-κB-activating agents can induce the phosphorylation of IκB proteins, targeting them for rapid degradation through the ubiquitin-proteasome pathway and releasing NF-κB to enter the nucleus where it regulates gene expression (6-8). NIK and IKKα (IKK1) regulate the phosphorylation and processing of NF-κB2 (p100) to produce p52, which translocates to the nucleus (9-11).

$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. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated NF-κB2 p100/p52 (18D10) Rabbit mAb #3017.
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Flow Cytometry

Background: Transcription factors of the nuclear factor κB (NF-κB)/Rel family play a pivotal role in inflammatory and immune responses (1,2). There are five family members in mammals: RelA, c-Rel, RelB, NF-κB1 (p105/p50), and NF-κB2 (p100/p52). Both p105 and p100 are proteolytically processed by the proteasome to produce p50 and p52, respectively. Rel proteins bind p50 and p52 to form dimeric complexes that bind DNA and regulate transcription. In unstimulated cells, NF-κB is sequestered in the cytoplasm by IκB inhibitory proteins (3-5). NF-κB-activating agents can induce the phosphorylation of IκB proteins, targeting them for rapid degradation through the ubiquitin-proteasome pathway and releasing NF-κB to enter the nucleus where it regulates gene expression (6-8). NIK and IKKα (IKK1) regulate the phosphorylation and processing of NF-κB2 (p100) to produce p52, which translocates to the nucleus (9-11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: BAFF, a member of the TNF superfamily of proteins, is a homotrimeric transmembrane protein, which is cleaved to produce a soluble cytokine (1). BAFF may also further oligomerize into 60-mer structures (1). BAFF is expressed by monocytes, neutrophils, macrophages, dendritic cells, activated T cells, and epithelial cells (1,2). BAFF plays a key role in B cell development, survival, and activation (1,3,4). BAFF binds to three distinct receptors, BAFF-R, TACI, and BCMA (1). These receptors are differentially expressed during B cell development and among B cell subsets (1,2,4). While BAFF-R and BCMA bind to the homotrimeric form of BAFF, TACI only binds to membrane bound or higher order BAFF structures (1). The BAFF/ BAFF-R interaction activates both canonical and non-canonical NF-κB pathways, PI3K/Akt, and mTOR (2,4). Activation of the noncanonical NF-κB pathway via BAFF-R is negatively regulated by TRAF3 (5). Research studies have shown that elevated levels of BAFF may exacerbate many autoimmune disorders, making it a potential therapeutic target (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Transcription factors of the nuclear factor κB (NF-κB)/Rel family play a pivotal role in inflammatory and immune responses (1,2). There are five family members in mammals: RelA, c-Rel, RelB, NF-κB1 (p105/p50), and NF-κB2 (p100/p52). Both p105 and p100 are proteolytically processed by the proteasome to produce p50 and p52, respectively. Rel proteins bind p50 and p52 to form dimeric complexes that bind DNA and regulate transcription. In unstimulated cells, NF-κB is sequestered in the cytoplasm by IκB inhibitory proteins (3-5). NF-κB-activating agents can induce the phosphorylation of IκB proteins, targeting them for rapid degradation through the ubiquitin-proteasome pathway and releasing NF-κB to enter the nucleus where it regulates gene expression (6-8). NIK and IKKα (IKK1) regulate the phosphorylation and processing of NF-κB2 (p100) to produce p52, which translocates to the nucleus (9-11).