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Mouse interleukin-1 Secretion

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: The nucleotide-binding oligomerization domain (NOD)-like receptor (NLR) family of proteins is a diverse family of cytoplasmic innate immune receptors. They are characterized by the presence of an amino-terminal effector domain, which is often either a caspase activation and recruitment domain (CARD) or a pyrin domain (PYD), followed by a NACHT domain and carboxy-terminal leucine-rich-repeats (LRR) involved in recognition of pathogen-associated molecular patterns (PAMPs) (1). NLR proteins play a variety of roles during the innate immune response including pathogen sensing, transcriptional activation of proinflammatory cytokines through NF-κB, transcriptional activation of type I interferons through IRFs, and formation of inflammasomes leading to activation of inflammatory caspases (1-7).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: High mobility group protein B1 (HMGB1) belongs to a family of highly conserved proteins that contain HMG box domains (1,2). All three family members (HMGB1, HMGB2, and HMGB3) contain two HMG box domains and a C-terminal acidic domain. HMGB1 is a widely expressed and highly abundant protein (2). HMGB2 is widely expressed during embryonic development, but is restricted to lymphoid organs and testis in adult animals (3). HMGB3 is only expressed during embryogenesis (4). While expression varies, the biochemical properties of the different family members may be indistinguishable. The HMG box domains facilitate the binding of HMGB proteins to the minor groove of DNA, which results in local bending of the DNA double helix (1,2). HMGB proteins are recruited by and help facilitate the assembly of site-specific DNA binding proteins to their cognate binding sites in chromatin. For example, HMGB1 facilitates the binding of Hox proteins, Oct-1, p53, Rel proteins, and steroid hormone receptor proteins to their target gene promoters (1,2). In addition to their functions in the nucleus, HMGB proteins play a significant role in extracellular signaling associated with inflammation (5,6). HMGB1 is massively released into the extracellular environment during cell necrosis, but not apoptosis. Extracellular HMGB1 "alarms" the innate immune system by acting as a chemoattractant for inflammatory leukocytes, smooth muscle cells, and stem cells, functioning as an immune adjuvant for soluble and particulate antigens, and triggering activation of T cells and dendritic cells. In addition, activated monocytes, macrophages and, dendritic cells also secrete HMGB1, forming a positive feedback loop that results in the release of additional cytokines and neutrophils. Hypoxia has also been shown to cause the release of HMGB1 in the liver, and some studies suggest a role for extracellular HMGB1 in tumor homeostasis (5,6).

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

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: High mobility group protein B1 (HMGB1) belongs to a family of highly conserved proteins that contain HMG box domains (1,2). All three family members (HMGB1, HMGB2, and HMGB3) contain two HMG box domains and a C-terminal acidic domain. HMGB1 is a widely expressed and highly abundant protein (2). HMGB2 is widely expressed during embryonic development, but is restricted to lymphoid organs and testis in adult animals (3). HMGB3 is only expressed during embryogenesis (4). While expression varies, the biochemical properties of the different family members may be indistinguishable. The HMG box domains facilitate the binding of HMGB proteins to the minor groove of DNA, which results in local bending of the DNA double helix (1,2). HMGB proteins are recruited by and help facilitate the assembly of site-specific DNA binding proteins to their cognate binding sites in chromatin. For example, HMGB1 facilitates the binding of Hox proteins, Oct-1, p53, Rel proteins, and steroid hormone receptor proteins to their target gene promoters (1,2). In addition to their functions in the nucleus, HMGB proteins play a significant role in extracellular signaling associated with inflammation (5,6). HMGB1 is massively released into the extracellular environment during cell necrosis, but not apoptosis. Extracellular HMGB1 "alarms" the innate immune system by acting as a chemoattractant for inflammatory leukocytes, smooth muscle cells, and stem cells, functioning as an immune adjuvant for soluble and particulate antigens, and triggering activation of T cells and dendritic cells. In addition, activated monocytes, macrophages and, dendritic cells also secrete HMGB1, forming a positive feedback loop that results in the release of additional cytokines and neutrophils. Hypoxia has also been shown to cause the release of HMGB1 in the liver, and some studies suggest a role for extracellular HMGB1 in tumor homeostasis (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 HMGB1 (D3E5) Rabbit mAb #6893.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: High mobility group protein B1 (HMGB1) belongs to a family of highly conserved proteins that contain HMG box domains (1,2). All three family members (HMGB1, HMGB2, and HMGB3) contain two HMG box domains and a C-terminal acidic domain. HMGB1 is a widely expressed and highly abundant protein (2). HMGB2 is widely expressed during embryonic development, but is restricted to lymphoid organs and testis in adult animals (3). HMGB3 is only expressed during embryogenesis (4). While expression varies, the biochemical properties of the different family members may be indistinguishable. The HMG box domains facilitate the binding of HMGB proteins to the minor groove of DNA, which results in local bending of the DNA double helix (1,2). HMGB proteins are recruited by and help facilitate the assembly of site-specific DNA binding proteins to their cognate binding sites in chromatin. For example, HMGB1 facilitates the binding of Hox proteins, Oct-1, p53, Rel proteins, and steroid hormone receptor proteins to their target gene promoters (1,2). In addition to their functions in the nucleus, HMGB proteins play a significant role in extracellular signaling associated with inflammation (5,6). HMGB1 is massively released into the extracellular environment during cell necrosis, but not apoptosis. Extracellular HMGB1 "alarms" the innate immune system by acting as a chemoattractant for inflammatory leukocytes, smooth muscle cells, and stem cells, functioning as an immune adjuvant for soluble and particulate antigens, and triggering activation of T cells and dendritic cells. In addition, activated monocytes, macrophages and, dendritic cells also secrete HMGB1, forming a positive feedback loop that results in the release of additional cytokines and neutrophils. Hypoxia has also been shown to cause the release of HMGB1 in the liver, and some studies suggest a role for extracellular HMGB1 in tumor homeostasis (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Interleukin-1β (IL-1β), one of the major caspase-1 targets, is a multifunctional cytokine that is involved in a host of immune and proinflammatory responses (1). It is produced primarily by activated monocytes and macrophages. It signals through various adaptor proteins and kinases that lead to activation of numerous downstream targets (2-6). Human IL-1β is synthesized as a 31 kDa precursor. To gain activity, the precursor must be cleaved by caspase-1 between Asp116 and Ala117 to yield a 17 kDa mature form (7,8). Detection of the 17 kDa mature form of IL-1β is a good indicator of caspase-1 activity.

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: Interleukin-1β (IL-1β) is a proinflammatory cytokine produced predominantly by activated monocytes and epithelial cells (1). Precursor IL-1β is cleaved by caspase-1 and mature IL-1β is then secreted (1-3). Target cells include macrophages and many other cell types. Signaling by IL-1β involves IL-1β binding to IL-1 accessory protein (IL-1-AcP); the complex then binds to IL-1RI (1,2). Signaling occurs through activation of MAP kinase and NF-κB pathways (1,2). IL-1β also binds to IL-1RII, which lacks an intracellular signaling domain and thereby serves as a high affinity decoy receptor. IL-1β binding to IL-1RI is inhibited by the negative regulator, IL-1R antagonist (IL-1Ra). IL-1Ra binding to IL-1RI does not signal and serves to block IL-1β signaling. IL-1β plays critical roles in the acute phase response and sepsis (1-3).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Caspase-1, or interleukin-1ß converting enzyme (ICE/ICEα), is a class I cysteine protease, which also includes caspases -4, -5, -11, and -12. Caspase-1 cleaves inflammatory cytokines such as pro-IL-1ß and interferon-γ inducing factor (IL-18) into their mature forms (1,2). Like other caspases, caspase-1 is proteolytically activated from a proenzyme to produce a tetramer of its two active subunits, p20 and p10. Caspase-1 has a large amino-terminal pro-domain that contains a caspase recruitment domain (CARD). Overexpression of caspase-1 can induce apoptosis (3). Mice deficient in caspase-1, however, have no overt defects in apoptosis but do have defects in the maturation of pro-IL-1β and are resistant to endotoxic shock (4,5). At least six caspase-1 isoforms have been identified, including caspase-1 α, β, γ, δ, ε and ζ (6). Most caspase-1 isoforms (α, β, γ and δ) produce products between 30-48 kDa and induce apoptosis upon over-expression. Caspase-1 ε typically contains only the p10 subunit, does not induce apoptosis and may act as a dominant negative. The widely expressed ζ isoform of caspase-1 induces apoptosis and lacks 39 amino-terminal residues found in the α isoform (6). Activation of caspase-1 occurs through an oligomerization molecular platform designated the "inflammasome" that includes caspase-5, Pycard/Asc, and NALP1 (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: Interleukin-1β (IL-1β) is a proinflammatory cytokine produced predominantly by activated monocytes and epithelial cells (1). Precursor IL-1β is cleaved by caspase-1 and mature IL-1β is then secreted (1-3). Target cells include macrophages and many other cell types. Signaling by IL-1β involves IL-1β binding to IL-1 accessory protein (IL-1-AcP); the complex then binds to IL-1RI (1,2). Signaling occurs through activation of MAP kinase and NF-κB pathways (1,2). IL-1β also binds to IL-1RII, which lacks an intracellular signaling domain and thereby serves as a high affinity decoy receptor. IL-1β binding to IL-1RI is inhibited by the negative regulator, IL-1R antagonist (IL-1Ra). IL-1Ra binding to IL-1RI does not signal and serves to block IL-1β signaling. IL-1β plays critical roles in the acute phase response and sepsis (1-3).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Flow Cytometry, Western Blotting

Background: Interleukin-1β (IL-1β), one of the major caspase-1 targets, is a multifunctional cytokine that is involved in a host of immune and proinflammatory responses (1). It is produced primarily by activated monocytes and macrophages. It signals through various adaptor proteins and kinases that lead to activation of numerous downstream targets (2-6). Human IL-1β is synthesized as a 31 kDa precursor. To gain activity, the precursor must be cleaved by caspase-1 between Asp116 and Ala117 to yield a 17 kDa mature form (7,8). Detection of the 17 kDa mature form of IL-1β is a good indicator of caspase-1 activity.

$303
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Interleukin-1β (IL-1β), one of the major caspase-1 targets, is a multifunctional cytokine that is involved in a host of immune and proinflammatory responses (1). It is produced primarily by activated monocytes and macrophages. It signals through various adaptor proteins and kinases that lead to activation of numerous downstream targets (2-6). Human IL-1β is synthesized as a 31 kDa precursor. To gain activity, the precursor must be cleaved by caspase-1 between Asp116 and Ala117 to yield a 17 kDa mature form (7,8). Detection of the 17 kDa mature form of IL-1β is a good indicator of caspase-1 activity.

$303
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Interleukin-1β (IL-1β), one of the major caspase-1 targets, is a multifunctional cytokine that is involved in a host of immune and proinflammatory responses (1). It is produced primarily by activated monocytes and macrophages. It signals through various adaptor proteins and kinases that lead to activation of numerous downstream targets (2-6). Human IL-1β is synthesized as a 31 kDa precursor. To gain activity, the precursor must be cleaved by caspase-1 between Asp116 and Ala117 to yield a 17 kDa mature form (7,8). Detection of the 17 kDa mature form of IL-1β is a good indicator of caspase-1 activity.

$303
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Caspase-1, or interleukin-1ß converting enzyme (ICE/ICEα), is a class I cysteine protease, which also includes caspases -4, -5, -11, and -12. Caspase-1 cleaves inflammatory cytokines such as pro-IL-1ß and interferon-γ inducing factor (IL-18) into their mature forms (1,2). Like other caspases, caspase-1 is proteolytically activated from a proenzyme to produce a tetramer of its two active subunits, p20 and p10. Caspase-1 has a large amino-terminal pro-domain that contains a caspase recruitment domain (CARD). Overexpression of caspase-1 can induce apoptosis (3). Mice deficient in caspase-1, however, have no overt defects in apoptosis but do have defects in the maturation of pro-IL-1β and are resistant to endotoxic shock (4,5). At least six caspase-1 isoforms have been identified, including caspase-1 α, β, γ, δ, ε and ζ (6). Most caspase-1 isoforms (α, β, γ and δ) produce products between 30-48 kDa and induce apoptosis upon over-expression. Caspase-1 ε typically contains only the p10 subunit, does not induce apoptosis and may act as a dominant negative. The widely expressed ζ isoform of caspase-1 induces apoptosis and lacks 39 amino-terminal residues found in the α isoform (6). Activation of caspase-1 occurs through an oligomerization molecular platform designated the "inflammasome" that includes caspase-5, Pycard/Asc, and NALP1 (7).

$109
100 µg
This Cell Signaling Technology antibody is conjugated to FITC and tested in-house for direct flow cytometric analysis in mouse cells.
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Flow Cytometry

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
Mouse, Rat

Application Methods: Immunofluorescence (Frozen)

Background: Ghrelin, also known as appetite-regulating hormone, is a neuropeptide hormone belonging to the motilin family. It is the ligand for the growth hormone secretagogue receptor type 1 (GHS-R), expressed by cells in the hypothalamic ventromedial nucleus and arcuate nucleus (1). Ghrelin is synthesized as a preprohormone by ghrelinergic cells in the gastrointestinal tract; proteolytic cleavage yields a 28-amino acid peptide hormone, which undergoes obligate n-octanoylation at serine 3 by the enzyme ghrelin O-acetyltransferase (GOAT) (2). Binding of n-octanoyl ghrelin to GHS-R stimulates growth hormone release, while simultaneously exerting multiple neuroendocrine affects that influence appetite, gastric motility and energy balance (3).

$159
100 µg
This Cell Signaling Technology antibody is conjugated to APC and tested in-house for direct flow cytometric analysis in mouse cells.
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Flow Cytometry

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).

$129
100 µg
This Cell Signaling Technology antibody is conjugated to PE and tested in-house for direct flow cytometric analysis in mouse cells.
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Flow Cytometry

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
Mouse

Application Methods: Western Blotting

Background: Members of the Toll-like receptor (TLR) family, named for the closely related Toll receptor in Drosophila, play a pivotal role in innate immune responses (1-4). TLRs recognize conserved motifs found in various pathogens and mediate defense responses (5-7). Triggering of the TLR pathway leads to the activation of NF-κB and subsequent regulation of immune and inflammatory genes (4). The TLRs and members of the IL-1 receptor family share a conserved stretch of approximately 200 amino acids known as the Toll/Interleukin-1 receptor (TIR) domain (1). Upon activation, TLRs associate with a number of cytoplasmic adaptor proteins containing TIR domains, including myeloid differentiation factor 88 (MyD88), MyD88-adaptor-like/TIR-associated protein (MAL/TIRAP), Toll-receptor-associated activator of interferon (TRIF), and Toll-receptor-associated molecule (TRAM) (8-10). This association leads to the recruitment and activation of IRAK1 and IRAK4, which form a complex with TRAF6 to activate TAK1 and IKK (8,11-14). Activation of IKK leads to the degradation of IκB, which normally maintains NF-κB in an inactive state by sequestering it in the cytoplasm.

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: The Wnt family includes several secreted glycoproteins that play important roles in animal development (1). There are 19 Wnt genes in the human genome that encode functionally distinct Wnt proteins (2). Wnt members bind to the Frizzled family of seven-pass transmembrane proteins and activate several signaling pathways (3). The canonical Wnt/β-catenin pathway also requires a coreceptor from the low-density lipoprotein receptor family (4). Aberrant activation of Wnt signaling pathways is involved in several types of cancers (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Absent in melanoma 2 (AIM2) is an interferon-inducible protein containing an amino-terminal pyrin domain and carboxy-terminal HIN-200 domain that functions in innate immunity and tumor progression (1). Expression of AIM2 can inhibit cell growth and tumor formation (2,3). Furthermore, the AIM2 gene has a high frequency of mutations associated with microsatellite-unstable colorectal cancers (4). AIM2 has a critical role in the activation of caspase-1, the protease responsible for the processing of pro-inflammatory cytokines IL-1β and IL-18. Caspase-1 activation is regulated by multi-protein complexes referred to as “inflammasomes” (5,6). Distinct inflammasome complexes have been described containing NLRP1/NALP1, NLRP3/NALP3, IPAF, and AIM2. The HIN-200 domain of AIM2 is responsible for binding to cytoplasmic double stranded DNA, resulting in caspase-1 activation. (7-9). This inflammasome complex also involves binding of the pyrin domain of AIM2 to the CARD-domain protein ASC/TMS1, which then interacts directly with caspase-1. As a result, AIM2 has been demonstrated to be an important sensor for a number of different pathogens (10-12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The pannexin family (pannexin-1, -2, and -3; PANX1-3) of gap junction proteins has homology to the invertebrate innexins and display distinct expression patterns (1). Pannexin-1 is widely expressed, with highest expression in the heart, brain, skeletal muscle, testis, and ovary (1,2). Pannexin-2 is predominately expressed in the brain (1,2) and pannexin-3 is found within the skin and connective tissues (1,3). Connexin family gap junction proteins form hemichannels that align adjacent cells, creating functional intercellular channels that are permeable to ions and small molecules. In contrast, pannexin proteins may not function as gap junction proteins since pannexins on adjacent cells may not align to form complete channels (3). These pannexin “hemichannels” may play a role in inflammation, apoptosis, and neuronal signaling by allowing permeability of ions, ATP, and potentially other small molecules into the extracellular space (4-6). Pannexin-1 can be activated by effector caspases (caspase-3 and -7), which leads to release of signal molecules that promote phagocytosis of apoptotic cells (7).