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Antibody Sampler Kit Interferon-Beta Production

The Toll-like Receptor Antibody Sampler Kit II provides an economical means of detecting expression of various Toll-like receptors (TLRs). The kit contains enough primary and secondary antibodies to perform at least two western blot experiments.

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). TLR1, TLR2, TLR4, TLR5, TLR6, and TLR11 are localized to the plasma membrane, while TLR3, TLR7, TLR8, and TLR9 are localized to intracellular membranes including endosomal membranes. 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. TLR1 and TLR6 associate with TLR2 to cooperatively mediate response to bacterial lipoproteins and fungal zymosan (6,15). TLR3 is an endosomal TLR that recognizes double-stranded RNA derived from viruses (7). TLR7 and TLR8 recognize single-stranded viral RNA and are also activated by synthetic imidazoquinoline compounds including R-848 (16,17). TLR9 recognizes unmethylated CpG motifs present on bacterial DNA (18).

The Innate Immunity Activation Antibody Sampler Kit provides an economical means of detecting the activation of multiple signaling pathways involved in innate immunity using phospho-specific, cleavage-specific, and control antibodies. The kit contains enough primary antibodies to perform at least two western blot experiments.

Background: The innate immune system responds rapidly to pathogens by detecting conserved pathogen-associated molecular patterns (PAMPs) and damage/danger-associated molecular patterns (DAMPs) through pattern recognition receptors (PRRs). There are several families of PRRs. Toll-like receptors (TLRs) are transmembrane PRRs and signal through recruitment of adaptor proteins, including MyD88, which leads to recruitment and phosphorylation of IRAK1 and IRAK4, followed by activation of NF-κB and MAP kinases (1-3). Some TLRs also activate IRFs, which upregulate the type I interferon response. Activation of TLR3 and TLR4 results in phosphorylation and activation of IRF-3, while TLR7, TLR8, and TLR9 lead to activation of IRF-7 (2, 3). STING is a multi-pass ER transmembrane protein that is activated in response to intracellular DNA downstream of DNA-sensing cytoplasmic PRRs, such as DDX41, or by binding the second messenger cyclic-GMP-AMP (cGAMP) produced by cGAS (4-6). Following activation, STING translocates with TBK1 to perinuclear endosomes, leading to phosphorylation and activation of IRF-3 and NF-κB (7, 8). Following activation and translocation, STING gets phosphorylated by ULK1, resulting in STING inactivation and degradation (9). Inflammasomes are cytoplasmic multimeric protein complexes that assemble in response to PAMPs or DAMPs detected by AIM2 or members of the nod-like receptor (NLR) family, such as NLRP3 (10). Inflammasomes activate Caspase-1, which cleaves the IL-1β and IL-18 precursor proteins into the mature forms (10).

The Mouse-Reactive STING Pathway Antibody Sampler Kit provides an economical means of detecting activation and expression of key components of the STING pathway using phospho-specific and control antibodies. The kit includes enough antibody to perform two western blot experiments with each primary antibody.

Background: Stimulator of interferon genes (STING, TMEM173, MITA) is a transmembrane adaptor protein that is a critical component of the cellular innate immune response to pathogenic cytoplasmic DNA (1,2). STING is a ubiquitously expressed protein found predominantly in the ER (1). The enzyme cGAMP synthase (cGAS) produces the second messenger cyclic-GMP-AMP (cGAMP) in response to cytoplasmic DNA (3,4). cGAMP binds and activates STING (3,4). In addition, detection of cytoplasmic DNA by nucleic acid sensors, including DDX41 or IFI16, results in STING activation (5,6). Following activation, STING translocates with TBK1 to perinuclear endosomes and gets phosphorylated by ULK1 at Ser366 (Ser365 in mouse) (7, 8). The TBK1 kinase phosphorylates and activates IRF-3 and NF-κB, which leads to the induction of type I interferon and other immune response genes (1,2,7).

The Toll-Like Receptor Antibody Sampler Kit is an economical way to examine the total protein levels of a number of toll-like receptors. This kit includes enough primary and secondary antibodies to perform two Western blot experiments with each antibody.

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.

The Inflammasome Antibody Sampler Kit provides an economical means of detecting multiple inflammasome components. The kit contains enough primary antibodies to perform at least two western blot experiments.

Background: The innate immune system works as the first line of defense in protection from pathogenic microbes and host-derived signals of cellular distress. One way in which these “danger” signals trigger inflammation is through activation of inflammasomes, which are multiprotein complexes that assemble in the cytosol after exposure to pathogen-associated molecular patterns (PAMPs) or danger-associated molecular patterns (DAMPs) and result in the activation of caspase-1 and subsequent cleavage of proinflammatory cytokines IL-1β and IL-18 (Reviewed in 1-6). Inflammasome complexes typically consist of a cytosolic pattern recognition receptor (PRR; a nucleotide-binding domain and leucine-rich-repeat [NLR] or AIM2-like receptor [ALR] family member), an adaptor protein (ASC/TMS1), and pro-caspase-1. A number of distinct inflammasome complexes have been identified, each with a unique PRR and activation triggers. The best characterized is the NLRP3 complex, which contains NLRP3, ASC/TMS1, and pro-caspase-1. The NLRP3 inflammasome is activated in a two-step process. First, NF-κB signaling is induced through PAMP- or DAMP-mediated activation of TLR4 or TNFR, resulting in increased expression of NLRP3, pro-IL-1β, and pro-IL-18 (priming step, signal 1). Next, indirect activation of NLRP3 occurs by a multitude of signals (whole pathogens, PAMPs/DAMPs, potassium efflux, lysosomal-damaging environmental factors [uric acid, silica, alum] and endogenous factors [amyloid-β, cholesterol crystals], and mitochondrial damage), leading to complex assembly and activation of caspase-1 (signal 2). The complex inflammasome structure is built via domain interactions among the protein components. Other inflammasomes are activated by more direct means: double-stranded DNA activates the AIM2 complex, anthrax toxin activates NLRP1, and bacterial flagellin activates NLRC4. Activated caspase-1 induces secretion of proinflammatory cytokines IL-1β and -18, but also regulates metabolic enzyme expression, phagosome maturation, vasodilation, and pyroptosis, an inflammatory programmed cell death. Inflammasome signaling contributes to the onset of a number of diseases, including atherosclerosis, type II diabetes, Alzheimer’s disease, and autoimmune disorders.

The Microglia Interferon-Related Module Antibody Sampler Kit provides an economical means of detecting proteins identified as markers of interferon-related microglial activity by western blot and/or immunofluorescence.

Background: Distinct microglial activation states have been identified using RNA-seq data from a vast array of neurological disease and aging models. These activation states have been categorized into modules corresponding to proliferation, neurodegeneration, interferon-relation, LPS-relation, and many others (1). Previous work identifying markers of specific brain cell types using RNA-seq has shown HS1 and ASC/TMS1 to be useful and specific tools to study microglia (2). HS1 is a protein kinase substrate that is expressed only in tissues and cells of hematopoietic origin (3) and ASC/TMS1 has been found to be a critical component of inflammatory signaling where it associates with and activates caspase-1 in response to pro-inflammatory signals (4).

The Mouse Reactive Inflammasome Antibody Sampler Kit provides an economical means of detecting multiple inflammasome components. The kit includes enough antibodies to perform at least two western blot experiments with each primary antibody.

Background: The innate immune system works as the first line of defense in protection from pathogenic microbes and host-derived signals of cellular distress. One way in which these “danger” signals trigger inflammation is through activation of inflammasomes, which are multiprotein complexes that assemble in the cytosol after exposure to pathogen-associated molecular patterns (PAMPs) or danger-associated molecular patterns (DAMPs) and result in the activation of caspase-1 and subsequent cleavage of proinflammatory cytokines IL-1β and IL-18 (Reviewed in 1-6). Inflammasome complexes typically consist of a cytosolic pattern recognition receptor (PRR; a nucleotide-binding domain and leucine-rich-repeat [NLR] or AIM2-like receptor [ALR] family member), an adaptor protein (ASC/TMS1), and pro-caspase-1. A number of distinct inflammasome complexes have been identified, each with a unique PRR and activation triggers. The best characterized is the NLRP3 complex, which contains NLRP3, ASC/TMS1, and pro-caspase-1. The NLRP3 inflammasome is activated in a two-step process. First, NF-κB signaling is induced through PAMP- or DAMP-mediated activation of TLR4 or TNFR, resulting in increased expression of NLRP3, pro-IL-1β, and pro-IL-18 (priming step, signal 1). Next, indirect activation of NLRP3 occurs by a multitude of signals (whole pathogens, PAMPs/DAMPs, potassium efflux, lysosomal-damaging environmental factors [uric acid, silica, alum] and endogenous factors [amyloid-β, cholesterol crystals], and mitochondrial damage), leading to complex assembly and activation of caspase-1 (signal 2). The complex inflammasome structure is built via domain interactions among the protein components. Other inflammasomes are activated by more direct means: double-stranded DNA activates the AIM2 complex, anthrax toxin activates NLRP1, and bacterial flagellin activates NLRC4. Activated caspase-1 induces secretion of proinflammatory cytokines IL-1β and -18, but also regulates metabolic enzyme expression, phagosome maturation, vasodilation, and pyroptosis, an inflammatory programmed cell death. Inflammasome signaling contributes to the onset of a number of diseases, including atherosclerosis, type II diabetes, Alzheimer’s disease, and autoimmune disorders.

The Human Reactive Inflammasome Antibody Sampler Kit II provides an economical means of detecting multiple inflammasome components. The kit contains enough primary antibodies to perform at least two western blot experiments.

Background: The innate immune system works as the first line of defense in protection from pathogenic microbes and host-derived signals of cellular distress. One way in which these “danger” signals trigger inflammation is through activation of inflammasomes, which are multiprotein complexes that assemble in the cytosol after exposure to pathogen-associated molecular patterns (PAMPs) or danger-associated molecular patterns (DAMPs) and result in the activation of caspase-1 and subsequent cleavage of proinflammatory cytokines IL-1β and IL-18 (Reviewed in 1-6). Inflammasome complexes typically consist of a cytosolic pattern recognition receptor (PRR; a nucleotide-binding domain and leucine-rich-repeat [NLR] or AIM2-like receptor [ALR] family member), an adaptor protein (ASC/TMS1), and pro-caspase-1. A number of distinct inflammasome complexes have been identified, each with a unique PRR and activation triggers. The best characterized is the NLRP3 complex, which contains NLRP3, ASC/TMS1, and pro-caspase-1. The NLRP3 inflammasome is activated in a two-step process. First, NF-κB signaling is induced through PAMP- or DAMP-mediated activation of TLR4 or TNFR, resulting in increased expression of NLRP3, pro-IL-1β, and pro-IL-18 (priming step, signal 1). Next, indirect activation of NLRP3 occurs by a multitude of signals (whole pathogens, PAMPs/DAMPs, potassium efflux, lysosomal-damaging environmental factors [uric acid, silica, alum] and endogenous factors [amyloid-β, cholesterol crystals], and mitochondrial damage), leading to complex assembly and activation of caspase-1 (signal 2). The complex inflammasome structure is built via domain interactions among the protein components. Other inflammasomes are activated by more direct means: double-stranded DNA activates the AIM2 complex, anthrax toxin activates NLRP1, and bacterial flagellin activates NLRC4. Activated caspase-1 induces secretion of proinflammatory cytokines IL-1β and -18, but also regulates metabolic enzyme expression, phagosome maturation, vasodilation, and pyroptosis, an inflammatory programmed cell death. Inflammasome signaling contributes to the onset of a number of diseases, including atherosclerosis, type II diabetes, Alzheimer’s disease, and autoimmune disorders.

The Microglia Cross Module Antibody Sampler Kit provides an economical means of detecting proteins identified as markers of microglial activity corresponding to proliferation, neurodegeneration, interferon and LPS-relation by western blot and/or immunofluorescence.

Background: Distinct microglial activation states have been identified using RNA-seq data from a vast array of neurological disease and aging models. These activation states have been categorized into modules corresponding to proliferation, neurodegeneration, interferon-relation, LPS-relation, and many others (1). Previous work identifying markers of specific brain cell types using RNA-seq has shown HS1 and ASC/TMS1 to be useful and specific tools to study microglia (2). HS1 is a protein kinase substrate that is expressed only in tissues and cells of hematopoietic origin (3) and ASC/TMS1 has been found to be a critical component of inflammatory signaling where it associates with and activates caspase-1 in response to pro-inflammatory signals (4).

The Microglia Neurodegeneration Module Antibody Sampler Kit provides an economical means of detecting proteins identified as markers of microglial activity during neurodegeneration by western blot and/or immunofluorescence.

Background: Distinct microglial activation states have been identified using RNA-seq data from a vast array of neurological disease and aging models. These activation states have been categorized into modules corresponding to proliferation, neurodegeneration, interferon-relation, LPS-relation, and many others (1). Previous work identifying markers of specific brain cell types using RNA-seq has shown HS1 and ASC/TMS1 to be useful and specific tools to study microglia (2). HS1 is a protein kinase substrate that is expressed only in tissues and cells of hematopoietic origin (3) and ASC/TMS1 has been found to be a critical component of inflammatory signaling where it associates with and activates caspase-1 in response to pro-inflammatory signals (4).

This kit contains reagents to examine total protein levels of the five NF-κB/Rel family members: p65/RelA, RelB, c-Rel, NF-κB1 (p105/p50) and NF-κB2 (p100/p52).

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).

The NF-κB Family Antibody Sampler Kit II provides an economical means of detecting members of the NF-κB family. The kit includes enough antibody to perform two western blots with each primary antibody.

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).

The Microglia LPS-Related Module Antibody Sampler Kit provides an economical means of detecting proteins identified as markers of LPS-related microglial activity by western blot and/or immunofluorescence.

Background: Distinct microglial activation states have been identified using RNA-seq data from a vast array of neurological disease and aging models. These activation states have been categorized into modules corresponding to proliferation, neurodegeneration, interferon-relation, LPS-relation, and many others (1). Previous work identifying markers of specific brain cell types using RNA-seq has shown HS1 and ASC/TMS1 to be useful and specific tools to study microglia (2). HS1 is a protein kinase substrate that is expressed only in tissues and cells of hematopoietic origin (3) and ASC/TMS1 has been found to be a critical component of inflammatory signaling where it associates with and activates caspase-1 in response to pro-inflammatory signals (4).

The Microglia Proliferation Module Antibody Sampler Kit provides an economical means of detecting proteins identified as markers of microglial proliferation by western blot and/or immunofluorescence.

Background: Distinct microglial activation states have been identified using RNA-seq data from a vast array of neurological disease and aging models. These activation states have been categorized into modules corresponding to proliferation, neurodegeneration, interferon-relation, LPS-relation, and many others (1). Previous work identifying markers of specific brain cell types using RNA-seq has shown HS1 and ASC/TMS1 to be useful and specific tools to study microglia (2). HS1 is a protein kinase substrate that is expressed only in tissues and cells of hematopoietic origin (3) and ASC/TMS1 has been found to be a critical component of inflammatory signaling where it associates with and activates caspase-1 in response to pro-inflammatory signals (4).

The TRAF Antibody Sampler Kit provides an economical means to evaluate endogenous levels of TRAF1, 2, 3, and 6. The kit contains enough primary and secondary antibodies to perform two western mini-blot experiments.

Background: TRAFs (TNF receptor-associated factors) are a family of multifunctional adaptor proteins that bind to surface receptors and recruit additional proteins to form multiprotein signaling complexes capable of promoting cellular responses (1-3). Members of the TRAF family share a common carboxy-terminal "TRAF domain", which mediates interactions with associated proteins; many also contain amino-terminal Zinc/RING finger motifs. The first TRAFs identified, TRAF1 and TRAF2, were found by virtue of their interactions with the cytoplasmic domain of TNF-receptor 2 (TNFRII) (4). The six known TRAFs (TRAF1-6) act as adaptor proteins for a wide range of cell surface receptors and participate in the regulation of cell survival, proliferation, differentiation, and stress responses.

The Exosomal Marker Antibody Sampler Kit provides an economical means to evaluate the presence of exosomal markers. The kit includes enough primary antibody to perform two western blot experiments for each target.
The Autophagy Vesicle Nucleation Antibody Sampler Kit provides an economical means of detecting target proteins involved in autophagosome formation and maturation. The kit contains enough antibody to perform two western blot experiments per primary antibody.
Senescence Associated Secretory Phenotype (SASP) Antibody Sampler Kit provides an economical means of detecting multiple components of the SASP. The kit includes enough antibody to perform two western blot experiments with each primary antibody.

Background: Senescence is characterized by stable stress-induced proliferative arrest and resistance to mitogenic stimuli, as well as the secretion of proteins such as cytokines, growth factors and proteases. These secreted proteins comprise the senescence-associated secretory phenotype (SASP). Senescent cells are thought to accumulate as an organism ages, and contribute to age-related diseases, including cancer, through promotion of inflammation and disruption of normal cellular function (1,2). The composition of the SASP varies, and SASP components can be either beneficial or deleterious in human disease, depending on the context (3).Senescence Associated Secretory Phenotype (SASP) Antibody Sampler Kit provides a collection of antibodies to various SASP components, including TNF-alpha, interleukin-6 (IL-6), the multifunctional cytokine IL-1beta, the chemokines CXCL10, RANTES/CCL5 and MCP-1, the matrix metalloprotease MMP3, and the serine-protease inhibitor PAI-1.

The Mouse Immune Cell Phenotyping IHC Antibody Sampler Kit provides an economical means of detecting the accumulation of immune cell types in formalin-fixed, paraffin-embedded tissue samples.

Background: Cluster of Differentiation 3 (CD3) is a multiunit protein complex expressed on the surface of T-cells that directly associates with the T-cell receptor (TCR). CD3 is composed of four polypeptides: ζ, γ, ε and δ. Engagement of TCR complex with antigens presented in Major Histocompatibility Complexes (MHC) induces tyrosine phosphorylation in the immunoreceptor tyrosine-based activation motif (ITAM) of CD3 proteins. CD3 phosphorylation is required for downstream signaling through ZAP-70 and p85 subunit of PI-3 kinase, leading to T cell activation, proliferation, and effector functions (1). Cluster of Differentiation 8 (CD8) is a transmembrane glycoprotein expressed primarily on cytotoxic T cells, but has also been described on a subset of dendritic cells in mice (2,3). On T cells, CD8 is a co-receptor for the TCR, and these two distinct structures are required to recognize antigen bound to MHC Class I (2). Cluster of Differentiation 4 (CD4) is expressed on the surface of T helper cells, regulatory T cells, monocytes, macrophages, and dendritic cells, and plays an important role in the development and activation of T cells. On T cells, CD4 is the co-receptor for the TCR, and these two distinct structures recognize antigen bound to MHC Class II. CD8 and CD4 co-receptors ensure specificity of the TCR–antigen interaction, prolong the contact between the T cell and the antigen presenting cell, and recruit the tyrosine kinase Lck, which is essential for T cell activation (2). Granzyme B is a serine protease expressed by CD8+ cytotoxic T lymphocytes and natural killer (NK) cells and is a key component of the immune response to pathogens and transformed cancer cells (4). Forkhead box P3 (FoxP3) is crucial for the development of T cells with immunosuppressive regulatory properties and is a well-established marker for T regulatory cells (Tregs) (5). CD19 is a co-receptor expressed on B cells that amplifies the signaling cascade initiated by the B cell receptor (BCR) to induce activation. It is a biomarker of B lymphocyte development, lymphoma diagnosis, and can be utilized as a target for leukemia immunotherapies (6,7). F4/80 (EMR1) is a heavily glycosylated G-protein-coupled receptor and is a well-established marker for mouse macrophages (8). CD11c (integrin αX, ITGAX) is a transmembrane glycoprotein highly expressed by dendritic cells, and has also been observed on activated NK cells, subsets of B and T cells, monocytes, granulocytes, and some B cell malignancies including hairy cell leukemia (9,10).

The HSP/Chaperone Sampler Kit provides an economical means to investigate protein folding within the cell. The kit contains enough primary and secondary antibodies to perform two Western blot experiments with each antibody.