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Product listing: IFN-α (6B18) Mouse mAb, UniProt ID P01562 #3110 to IKKε (D61F9) XP® Rabbit mAb (PE Conjugate), UniProt ID Q14164 #85033

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Interferons (IFNs) appear both locally and systematically early after viral infection and participate in limiting the spread of infection. They also affect cell differentiation, growth, surface antigen expression and immunoregulation (1). There are three naturally occurring interferons: α, β and γ. IFN-α is derived from lymphoblastic tissue and has a number of therapeutic applications in the treatment of various human cancers and diseases of viral origin. Recombinant IFN-α from both natural and synthetic genes binds to a common cell surface receptor and induces antiviral activity in a variety of cell lines. When binding to discrete cell surface receptors on target cells, IFN-α induces rapid changes in Jak/Stat phosphorylation, which initiates the Jak/Stat signaling pathway (2). IFN-α signaling also involves production of DAG without an increased intracellular free calcium concentration and the subsequent activation of calcium-independent isoforms of PKC (β and ε) (3). All IFN-α signaling pathways lead to final alterations of gene expression, which mediate their pleiotropic biologic activities.

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Interferons (IFNs) appear both locally and systematically early after viral infection and participate in limiting the spread of infection. They also affect cell differentiation, growth, surface antigen expression and immunoregulation (1). There are three naturally occurring interferons: α, β and γ. IFN-α is derived from lymphoblastic tissue and has a number of therapeutic applications in the treatment of various human cancers and diseases of viral origin. Recombinant IFN-α from both natural and synthetic genes binds to a common cell surface receptor and induces antiviral activity in a variety of cell lines. When binding to discrete cell surface receptors on target cells, IFN-α induces rapid changes in Jak/Stat phosphorylation, which initiates the Jak/Stat signaling pathway (2). IFN-α signaling also involves production of DAG without an increased intracellular free calcium concentration and the subsequent activation of calcium-independent isoforms of PKC (β and ε) (3). All IFN-α signaling pathways lead to final alterations of gene expression, which mediate their pleiotropic biologic activities.

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The type I interferon (IFN) family includes IFN-β1 and IFN-α1 through IFN-α13 in humans and IFN-α1 through IFN-α14 in mice. Type I IFN is produced following detection of pathogen-associated molecular patterns (PAMPs) and is important for induction of antiviral genes, activation of dendritic cells, and initiation of adaptive immunity (1, 2). Type I IFNs signal through the IFN alpha receptor (IFNAR), which is a heterodimer composed of IFNAR1 and IFNAR2. Activation of IFNAR leads to formation of the nuclear complex IFN-stimulated gene factor 3 (ISGF3), which consists of STAT1, STAT2, and IRF-9 (3, 4). ISGF3 binds to IFN-stimulated response elements (ISREs) to initiate transcription of interferon-stimulated genes (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Flow Cytometry, Western Blotting

Background: The type I interferon (IFN) family includes IFN-β1 and IFN-α1 through IFN-α13 in humans and IFN-α1 through IFN-α14 in mice. Type I IFN is produced following detection of pathogen-associated molecular patterns (PAMPs) and is important for induction of antiviral genes, activation of dendritic cells, and initiation of adaptive immunity (1, 2). Type I IFNs signal through the IFN alpha receptor (IFNAR), which is a heterodimer composed of IFNAR1 and IFNAR2. Activation of IFNAR leads to formation of the nuclear complex IFN-stimulated gene factor 3 (ISGF3), which consists of STAT1, STAT2, and IRF-9 (3, 4). ISGF3 binds to IFN-stimulated response elements (ISREs) to initiate transcription of interferon-stimulated genes (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Peptide ELISA (DELFIA), Western Blotting

Background: IFN-γ plays key roles in both the innate and adaptive immune response. IFN-γ activates the cytotoxic activity of innate immune cells, such as macrophages and NK cells (1,2). IFN-γ production by NK cells and antigen presenting cells (APCs) promotes cell-mediated adaptive immunity by inducing IFN-γ production by T lymphocytes, increasing class I and class II MHC expression, and enhancing peptide antigen presentation (1). The anti-viral activity of IFN-γ is due to its induction of PKR and other regulatory proteins. Binding of IFN-γ to the IFNGR1/IFNGR2 complex promotes dimerization of the receptor complexes to form the (IFNGR1/IFNGR2)2 -IFN-γ dimer. Binding induces a conformational change in receptor intracellular domains and signaling involves Jak1, Jak2, and Stat1 (3). The critical role of IFN-γ in amplification of immune surveillance and function is supported by increased susceptibility to pathogen infection by IFN-γ or IFNGR knockout mice and in humans with inactivating mutations in IFNGR1 or IFNGR2. IFN-γ also appears to have a role in atherosclerosis (4).

$293
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: IFN-γ plays key roles in both the innate and adaptive immune response. IFN-γ activates the cytotoxic activity of innate immune cells, such as macrophages and NK cells (1,2). IFN-γ production by NK cells and antigen presenting cells (APCs) promotes cell-mediated adaptive immunity by inducing IFN-γ production by T lymphocytes, increasing class I and class II MHC expression, and enhancing peptide antigen presentation (1). The anti-viral activity of IFN-γ is due to its induction of PKR and other regulatory proteins. Binding of IFN-γ to the IFNGR1/IFNGR2 complex promotes dimerization of the receptor complexes to form the (IFNGR1/IFNGR2)2 -IFN-γ dimer. Binding induces a conformational change in receptor intracellular domains and signaling involves Jak1, Jak2, and Stat1 (3). The critical role of IFN-γ in amplification of immune surveillance and function is supported by increased susceptibility to pathogen infection by IFN-γ or IFNGR knockout mice and in humans with inactivating mutations in IFNGR1 or IFNGR2. IFN-γ also appears to have a role in atherosclerosis (4).

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

Application Methods: Immunoprecipitation, Western Blotting

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The type 1 insulin-like growth factor receptor (IGF1R) is a transmembrane receptor tyrosine kinase that is widely expressed in many cell types in fetal and postnatal tissues, and which is highly similar in sequence and structure to the insulin receptor (1-4). IGF1R is synthesized as a preproprotein which is proteolytically cleaved into alpha and beta subunits. Receptor assembly involves heterodimerization of two alpha and two beta subunits to generate the heterotetrameric transmembrane receptor. The alpha subunits form the extracellular ligand binding domain; ligand binding by IGF-I or IGF-II initiates autophosphorylation of conserved intracellular residues in the beta subunit kinase domain, leading to kinase activation and subsequent activation of downstream signal transduction pathways (e.g., Akt and MAPK) (4-8). Enhanced mitogenic signaling through the IGF1R is frequently observed in cancer, making the IGF1R an important research target in translational oncology (9).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Type I insulin-like growth factor receptor (IGF-IR) is a transmembrane receptor tyrosine kinase that is widely expressed in many cell lines and cell types within fetal and postnatal tissues (1-3). Receptor autophosphorylation follows binding of the IGF-I and IGF-II ligands. Three tyrosine residues within the kinase domain (Tyr1131, Tyr1135, and Tyr1136) are the earliest major autophosphorylation sites (4). Phosphorylation of these three tyrosine residues is necessary for kinase activation (5,6). Insulin receptors (IRs) share significant structural and functional similarity with IGF-I receptors, including the presence of an equivalent tyrosine cluster (Tyr1146/1150/1151) within the kinase domain activation loop. Tyrosine autophosphorylation of IRs is one of the earliest cellular responses to insulin stimulation (7). Autophosphorylation begins with phosphorylation at Tyr1146 and either Tyr1150 or Tyr1151, while full kinase activation requires triple tyrosine phosphorylation (8).

$348
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 IGF-I Receptor β (D23H3) XP® Rabbit mAb #9750.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Type I insulin-like growth factor receptor (IGF-IR) is a transmembrane receptor tyrosine kinase that is widely expressed in many cell lines and cell types within fetal and postnatal tissues (1-3). Receptor autophosphorylation follows binding of the IGF-I and IGF-II ligands. Three tyrosine residues within the kinase domain (Tyr1131, Tyr1135, and Tyr1136) are the earliest major autophosphorylation sites (4). Phosphorylation of these three tyrosine residues is necessary for kinase activation (5,6). Insulin receptors (IRs) share significant structural and functional similarity with IGF-I receptors, including the presence of an equivalent tyrosine cluster (Tyr1146/1150/1151) within the kinase domain activation loop. Tyrosine autophosphorylation of IRs is one of the earliest cellular responses to insulin stimulation (7). Autophosphorylation begins with phosphorylation at Tyr1146 and either Tyr1150 or Tyr1151, while full kinase activation requires triple tyrosine phosphorylation (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. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated IGF-I Receptor β (D23H3) XP® Rabbit mAb #9750.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry

Background: Type I insulin-like growth factor receptor (IGF-IR) is a transmembrane receptor tyrosine kinase that is widely expressed in many cell lines and cell types within fetal and postnatal tissues (1-3). Receptor autophosphorylation follows binding of the IGF-I and IGF-II ligands. Three tyrosine residues within the kinase domain (Tyr1131, Tyr1135, and Tyr1136) are the earliest major autophosphorylation sites (4). Phosphorylation of these three tyrosine residues is necessary for kinase activation (5,6). Insulin receptors (IRs) share significant structural and functional similarity with IGF-I receptors, including the presence of an equivalent tyrosine cluster (Tyr1146/1150/1151) within the kinase domain activation loop. Tyrosine autophosphorylation of IRs is one of the earliest cellular responses to insulin stimulation (7). Autophosphorylation begins with phosphorylation at Tyr1146 and either Tyr1150 or Tyr1151, while full kinase activation requires triple tyrosine phosphorylation (8).

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

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

Background: Type I insulin-like growth factor receptor (IGF-IR) is a transmembrane receptor tyrosine kinase that is widely expressed in many cell lines and cell types within fetal and postnatal tissues (1-3). Receptor autophosphorylation follows binding of the IGF-I and IGF-II ligands. Three tyrosine residues within the kinase domain (Tyr1131, Tyr1135, and Tyr1136) are the earliest major autophosphorylation sites (4). Phosphorylation of these three tyrosine residues is necessary for kinase activation (5,6). Insulin receptors (IRs) share significant structural and functional similarity with IGF-I receptors, including the presence of an equivalent tyrosine cluster (Tyr1146/1150/1151) within the kinase domain activation loop. Tyrosine autophosphorylation of IRs is one of the earliest cellular responses to insulin stimulation (7). Autophosphorylation begins with phosphorylation at Tyr1146 and either Tyr1150 or Tyr1151, while full kinase activation requires triple tyrosine phosphorylation (8).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Type I insulin-like growth factor receptor (IGF-IR) is a transmembrane receptor tyrosine kinase that is widely expressed in many cell lines and cell types within fetal and postnatal tissues (1-3). Receptor autophosphorylation follows binding of the IGF-I and IGF-II ligands. Three tyrosine residues within the kinase domain (Tyr1131, Tyr1135, and Tyr1136) are the earliest major autophosphorylation sites (4). Phosphorylation of these three tyrosine residues is necessary for kinase activation (5,6). Insulin receptors (IRs) share significant structural and functional similarity with IGF-I receptors, including the presence of an equivalent tyrosine cluster (Tyr1146/1150/1151) within the kinase domain activation loop. Tyrosine autophosphorylation of IRs is one of the earliest cellular responses to insulin stimulation (7). Autophosphorylation begins with phosphorylation at Tyr1146 and either Tyr1150 or Tyr1151, while full kinase activation requires triple tyrosine phosphorylation (8).

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

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

Background: Insulin-like growth factor II (IGF-II) receptor, also widely known as cation-independent mannose 6-phosphate receptor (CI-M6PR), is a multifunctional type I transmembrane glycoprotein that participates in the internalization of mannose-6-phosphate modified hydrolases and IGF-II from the plasma membrane (1,2). In the absence of ligands, IGF-II receptor is constitutively endocytosed from the cell surface to accumulate in the Golgi apparatus (3). In the presence of ligands, the receptor transports the mannose-6-phosphate modified hydrolases to acidified endosomes and lysosomes (4). The ligand-free receptor is then transported back to the Golgi compartment or the cell surface (4). In several research studies, IGF-II receptor has been recognized as a tumor suppressor in a number of cancers (5-7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Insulin-like growth factor II (IGF-II) receptor, also widely known as cation-independent mannose 6-phosphate receptor (CI-M6PR), is a multifunctional type I transmembrane glycoprotein that participates in the internalization of mannose-6-phosphate modified hydrolases and IGF-II from the plasma membrane (1,2). In the absence of ligands, IGF-II receptor is constitutively endocytosed from the cell surface to accumulate in the Golgi apparatus (3). In the presence of ligands, the receptor transports the mannose-6-phosphate modified hydrolases to acidified endosomes and lysosomes (4). The ligand-free receptor is then transported back to the Golgi compartment or the cell surface (4). In several research studies, IGF-II receptor has been recognized as a tumor suppressor in a number of cancers (5-7).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Insulin-like growth factor-binding proteins (IGFBPs) play an integral role in modifying insulin-like growth factor (IGF) actions in a wide variety of cell types. There are six known IGFBP family members (IGFBP1-6), which are structurally related, but encoded by distinct genes. IGFBPs have high affinity for IGFs; in some contexts, IGFBPs inhibit IGF actions by preventing access to IGF receptors, while in others they potentiate IGF actions by facilitating ligand-receptor interaction (1-3). IGFBP1 is produced primarily by the liver and secreted into circulation, and studies show its expression can be negatively regulated by insulin (4, 5). Notably, low levels of IGFBP1 were shown to predict the future onset of Type 2 diabetes (5). Reduced expression of IGFBP1 expression was also associated with tumor progression in breast cancer, prostate cancer, pancreatic cancer and colorectal cancer, possibly stemming from reduced inhibition of mitogenic IGF signaling (6-9). Notably however, other research studies have reported increased levels of IGFBP1 in selected tumor types; in human schwannoma, increased IGFBP1 was associated with stimulation of the integrin β1/FAK pathway, supporting the concept of IGF-independent signaling functions for selected IGFBPs (10,11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Insulin-like growth factor (IGF) signaling plays a major role in regulating the proliferation and metabolism of normal and malignant cells. Insulin-like growth factor-binding proteins (IGFBPs) play an integral role in modifying IGF actions in a wide variety of cell types. The six IGFBP family members share a high affinity for IGF binding and are structurally related, but are encoded by distinct genes (1). IGF binding proteins can exert stimulatory or inhibitory effects by controlling IGF availability through high affinity binding of IGF at the carboxy-terminal domain (2,3). IGFBP3 is the most abundant serum IGF binding protein and the main mediator for IGF-I bioactivities. IGFBP3 also binds IGF-II, insulin, and other cellular and extracellular components to regulate cell growth, development, and apoptosis through both IGF-dependent and IGF-independent mechanisms (4-8). Research studies describe correlations between increased IGF-I levels and reduced levels of IGFBP3 with increased risks of developing cancer, including breast, colon, lung, and prostate cancer (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: The Ikaros family of zinc-finger DNA-binding proteins belongs to the Kruppel transcription factor superfamily. Ikaros proteins are characterized by the presence of an amino-terminal zinc finger DNA-binding domain and a carboxy-terminal dimerization domain. Members of the Ikaros family include Ikaros, Aiolos, Helios, EOS, and Pegasus (1). All family members can form homodimers and heterodimers with other members of the Ikaros family. Most also contain multiple isoforms that are generated as a result of differential splicing, with some isoforms behaving in a dominant negative manner upon dimerization (2).Ikaros (IKZF1, LYF1) is the prototypical Ikaros family zinc-finger transcription factor and is expressed abundantly in lymphoid cells. Genetic studies in mice demonstrate that Ikaros is a tumor suppressor that is important for the normal development of B, T, natural killer, and dendritic cells (3,4). Additional studies show that imbalanced expression of different Ikaros isoforms, as well as mutations in the corresponding IKAROS gene, can be associated with a number of hematologic malignancies in humans (2,5,6).

$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 cytometric analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Ikaros (D6N9Y) Rabbit mAb #14859.
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Flow Cytometry

Background: The Ikaros family of zinc-finger DNA-binding proteins belongs to the Kruppel transcription factor superfamily. Ikaros proteins are characterized by the presence of an amino-terminal zinc finger DNA-binding domain and a carboxy-terminal dimerization domain. Members of the Ikaros family include Ikaros, Aiolos, Helios, EOS, and Pegasus (1). All family members can form homodimers and heterodimers with other members of the Ikaros family. Most also contain multiple isoforms that are generated as a result of differential splicing, with some isoforms behaving in a dominant negative manner upon dimerization (2).Ikaros (IKZF1, LYF1) is the prototypical Ikaros family zinc-finger transcription factor and is expressed abundantly in lymphoid cells. Genetic studies in mice demonstrate that Ikaros is a tumor suppressor that is important for the normal development of B, T, natural killer, and dendritic cells (3,4). Additional studies show that imbalanced expression of different Ikaros isoforms, as well as mutations in the corresponding IKAROS gene, can be associated with a number of hematologic malignancies in humans (2,5,6).

$305
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 Ikaros (D6N9Y) Rabbit mAb #14859.
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Flow Cytometry

Background: The Ikaros family of zinc-finger DNA-binding proteins belongs to the Kruppel transcription factor superfamily. Ikaros proteins are characterized by the presence of an amino-terminal zinc finger DNA-binding domain and a carboxy-terminal dimerization domain. Members of the Ikaros family include Ikaros, Aiolos, Helios, EOS, and Pegasus (1). All family members can form homodimers and heterodimers with other members of the Ikaros family. Most also contain multiple isoforms that are generated as a result of differential splicing, with some isoforms behaving in a dominant negative manner upon dimerization (2).Ikaros (IKZF1, LYF1) is the prototypical Ikaros family zinc-finger transcription factor and is expressed abundantly in lymphoid cells. Genetic studies in mice demonstrate that Ikaros is a tumor suppressor that is important for the normal development of B, T, natural killer, and dendritic cells (3,4). Additional studies show that imbalanced expression of different Ikaros isoforms, as well as mutations in the corresponding IKAROS gene, can be associated with a number of hematologic malignancies in humans (2,5,6).

$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 Ikaros (D6N9Y) Rabbit mAb #14859.
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Flow Cytometry

Background: The Ikaros family of zinc-finger DNA-binding proteins belongs to the Kruppel transcription factor superfamily. Ikaros proteins are characterized by the presence of an amino-terminal zinc finger DNA-binding domain and a carboxy-terminal dimerization domain. Members of the Ikaros family include Ikaros, Aiolos, Helios, EOS, and Pegasus (1). All family members can form homodimers and heterodimers with other members of the Ikaros family. Most also contain multiple isoforms that are generated as a result of differential splicing, with some isoforms behaving in a dominant negative manner upon dimerization (2).Ikaros (IKZF1, LYF1) is the prototypical Ikaros family zinc-finger transcription factor and is expressed abundantly in lymphoid cells. Genetic studies in mice demonstrate that Ikaros is a tumor suppressor that is important for the normal development of B, T, natural killer, and dendritic cells (3,4). Additional studies show that imbalanced expression of different Ikaros isoforms, as well as mutations in the corresponding IKAROS gene, can be associated with a number of hematologic malignancies in humans (2,5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: The Ikaros family of zinc-finger DNA-binding proteins belongs to the Kruppel transcription factor superfamily. Ikaros proteins are characterized by the presence of an amino-terminal zinc finger DNA-binding domain and a carboxy-terminal dimerization domain. Members of the Ikaros family include Ikaros, Aiolos, Helios, EOS, and Pegasus (1). All family members can form homodimers and heterodimers with other members of the Ikaros family. Most also contain multiple isoforms that are generated as a result of differential splicing, with some isoforms behaving in a dominant negative manner upon dimerization (2).Ikaros (IKZF1, LYF1) is the prototypical Ikaros family zinc-finger transcription factor and is expressed abundantly in lymphoid cells. Genetic studies in mice demonstrate that Ikaros is a tumor suppressor that is important for the normal development of B, T, natural killer, and dendritic cells (3,4). Additional studies show that imbalanced expression of different Ikaros isoforms, as well as mutations in the corresponding IKAROS gene, can be associated with a number of hematologic malignancies in humans (2,5,6).

$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 IKKα (3G12) Mouse mAb #11930.
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Flow Cytometry

Background: The NF-κB/Rel transcription factors are present in the cytosol in an inactive state, complexed with the inhibitory IκB proteins (1-3). Most agents that activate NF-κB do so through a common pathway based on phosphorylation-induced, proteasome-mediated degradation of IκB (3-7). The key regulatory step in this pathway involves activation of a high molecular weight IκB kinase (IKK) complex whose catalysis is generally carried out by three tightly associated IKK subunits. IKKα and IKKβ serve as the catalytic subunits of the kinase and IKKγ serves as the regulatory subunit (8,9). Activation of IKK depends upon phosphorylation at Ser177 and Ser181 in the activation loop of IKKβ (Ser176 and Ser180 in IKKα), which causes conformational changes, resulting in kinase activation (10-13).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: The NF-κB/Rel transcription factors are present in the cytosol in an inactive state, complexed with the inhibitory IκB proteins (1-3). Most agents that activate NF-κB do so through a common pathway based on phosphorylation-induced, proteasome-mediated degradation of IκB (3-7). The key regulatory step in this pathway involves activation of a high molecular weight IκB kinase (IKK) complex whose catalysis is generally carried out by three tightly associated IKK subunits. IKKα and IKKβ serve as the catalytic subunits of the kinase and IKKγ serves as the regulatory subunit (8,9). Activation of IKK depends upon phosphorylation at Ser177 and Ser181 in the activation loop of IKKβ (Ser176 and Ser180 in IKKα), which causes conformational changes, resulting in kinase activation (10-13).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The NF-κB/Rel transcription factors are present in the cytosol in an inactive state, complexed with the inhibitory IκB proteins (1-3). Most agents that activate NF-κB do so through a common pathway based on phosphorylation-induced, proteasome-mediated degradation of IκB (3-7). The key regulatory step in this pathway involves activation of a high molecular weight IκB kinase (IKK) complex whose catalysis is generally carried out by three tightly associated IKK subunits. IKKα and IKKβ serve as the catalytic subunits of the kinase and IKKγ serves as the regulatory subunit (8,9). Activation of IKK depends upon phosphorylation at Ser177 and Ser181 in the activation loop of IKKβ (Ser176 and Ser180 in IKKα), which causes conformational changes, resulting in kinase activation (10-13).

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

Application Methods: Western Blotting

Background: The NF-κB/Rel transcription factors are present in the cytosol in an inactive state, complexed with the inhibitory IκB proteins (1-3). Most agents that activate NF-κB do so through a common pathway based on phosphorylation-induced, proteasome-mediated degradation of IκB (3-7). The key regulatory step in this pathway involves activation of a high molecular weight IκB kinase (IKK) complex whose catalysis is generally carried out by three tightly associated IKK subunits. IKKα and IKKβ serve as the catalytic subunits of the kinase and IKKγ serves as the regulatory subunit (8,9). Activation of IKK depends upon phosphorylation at Ser177 and Ser181 in the activation loop of IKKβ (Ser176 and Ser180 in IKKα), which causes conformational changes, resulting in kinase activation (10-13).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The NF-κB/Rel transcription factors are present in the cytosol in an inactive state, complexed with the inhibitory IκB proteins (1-3). Most agents that activate NF-κB do so through a common pathway based on phosphorylation-induced, proteasome-mediated degradation of IκB (3-7). The key regulatory step in this pathway involves activation of a high molecular weight IκB kinase (IKK) complex whose catalysis is generally carried out by three tightly associated IKK subunits. IKKα and IKKβ serve as the catalytic subunits of the kinase and IKKγ serves as the regulatory subunit (8,9). Activation of IKK depends upon phosphorylation at Ser177 and Ser181 in the activation loop of IKKβ (Ser176 and Ser180 in IKKα), which causes conformational changes, resulting in kinase activation (10-13).

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

Application Methods: Western Blotting

Background: The NF-κB/Rel transcription factors are present in the cytosol in an inactive state, complexed with the inhibitory IκB proteins (1-3). Most agents that activate NF-κB do so through a common pathway based on phosphorylation-induced, proteasome-mediated degradation of IκB (3-7). The key regulatory step in this pathway involves activation of a high molecular weight IκB kinase (IKK) complex whose catalysis is generally carried out by three tightly associated IKK subunits. IKKα and IKKβ serve as the catalytic subunits of the kinase and IKKγ serves as the regulatory subunit (8,9). Activation of IKK depends upon phosphorylation at Ser177 and Ser181 in the activation loop of IKKβ (Ser176 and Ser180 in IKKα), which causes conformational changes, resulting in kinase activation (10-13).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The NF-κB/Rel transcription factors are present in the cytosol in an inactive state, complexed with the inhibitory IκB proteins (1-3). Most agents that activate NF-κB do so through a common pathway based on phosphorylation-induced, proteasome-mediated degradation of IκB (3-7). The key regulatory step in this pathway involves activation of a high molecular weight IκB kinase (IKK) complex whose catalysis is generally carried out by three tightly associated IKK subunits. IKKα and IKKβ serve as the catalytic subunits of the kinase and IKKγ serves as the regulatory subunit (8,9). Activation of IKK depends upon phosphorylation at Ser177 and Ser181 in the activation loop of IKKβ (Ser176 and Ser180 in IKKα), which causes conformational changes, resulting in kinase activation (10-13).

$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 mouse cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated IKKε (D61F9) XP® Rabbit mAb #3416.
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Flow Cytometry

Background: The NF-κB/Rel transcription factors are present in the cytosol in an inactive state, complexed with the inhibitory IκB proteins (1-3). Most agents that activate NF-κB do so through a common pathway based on phosphorylation-induced, proteasome-mediated degradation of IκB (3-7). The key regulatory step in this pathway involves activation of a high molecular weight IκB kinase (IKK) complex whose catalysis is generally carried out by three tightly associated IKK subunits. IKKα and IKKβ serve as the catalytic subunits of the kinase and IKKγ serves as the regulatory subunit (8,9). Activation of IKK depends upon phosphorylation at Ser177 and Ser181 in the activation loop of IKKβ (Ser176 and Ser180 in IKKα), which causes conformational changes, resulting in kinase activation (10-13).