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Mouse Defense Response to Fungus

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Myeloperoxidase (MPO) is a peroxidase enzyme that is part of the host defense system of polymorphonuclear leukocytes (reviewed in 1). The gene for MPO was cloned independently from several laboratories (2-5). A decrease in MPO expression was noticed upon differentiation of HL-60 cells (5). MPO catalyzes the reaction of hydrogen peroxide and chloride (or other halides) to produce hypochlorous acid and other potent antimicrobial oxidants. Knockout mice of MPO are impaired in clearing select microbial infections (6). Processing of mature MPO from an initial 80-90 kDa translation product involves insertion of a heme moiety, glycosylation, and proteolytic cleavage. The mature protein is a tetramer of two heavy chains (60 kDa) and two light chains (12 kDa). It is abundantly expressed in neutrophils and monocytes and secreted during their activation. Heightened MPO levels have been associated with tissue damage and a number of pathological conditions (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Transforming growth factor-β (TGF-β) superfamily members are critical regulators of cell proliferation and differentiation, developmental patterning and morphogenesis, and disease pathogenesis (1-4). TGF-β elicits signaling through three cell surface receptors: type I (RI), type II (RII), and type III (RIII). Type I and type II receptors are serine/threonine kinases that form a heteromeric complex. In response to ligand binding, the type II receptors form a stable complex with the type I receptors allowing phosphorylation and activation of type I receptor kinases (5). The type III receptor, also known as betaglycan, is a transmembrane proteoglycan with a large extracellular domain that binds TGF-β with high affinity but lacks a cytoplasmic signaling domain (6,7). Expression of the type III receptor can regulate TGF-β signaling through presentation of the ligand to the signaling complex. The only known direct TGF-β signaling effectors are the Smad family proteins, which transduce signals from the cell surface directly to the nucleus to regulate target gene transcription (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Phosphoinositide 3-kinase (PI3K) catalyzes the production of phosphatidylinositol-3,4,5-triphosphate by phosphorylating phosphatidylinositol (PI), phosphatidylinositol-4-phosphate (PIP), and phosphatidylinositol-4,5-bisphosphate (PIP2). Growth factors and hormones trigger this phosphorylation event, which in turn coordinates cell growth, cell cycle entry, cell migration, and cell survival (1). PTEN reverses this process, and research studies have shown that the PI3K signaling pathway is constitutively activated in human cancers that have loss of function of PTEN (2). PI3Ks are composed of a catalytic subunit (p110) and a regulatory subunit. Various isoforms of the catalytic subunit (p110α, p110β, p110γ, and p110δ) have been isolated, and the regulatory subunits that associate with p110α, p110β, and p110δ are p85α and p85β (3). In contrast, p110γ associates with a p101 regulatory subunit that is unrelated to p85. Furthermore, p110γ is activated by βγ subunits of heterotrimeric G proteins (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: CARD9 is a caspase recruitment domain (CARD)-containing adaptor protein expressed by myeloid cells (1,2). It is required for antifungal immunity downstream of pathogen detection by C-type lectin receptors (CLRs) such as Dectin-1 (3,4). Recognition of carbohydrates on fungal cell walls by CLRs leads to activation of the tyrosine kinase Syk, followed by activation of PKCδ (5,6). PKCδ phosphorylates CARD9, enabling the assembly of a complex containing CARD9 and Bcl10 (6). This complex activates NF-κB, resulting in upregulation of inflammatory cytokines important for initiation of adaptive immunity (3,4,6,7). CARD9 was also shown to be important for the induction of IL-1β, downstream of the viral nucleic acid sensor RIG-I, as well as for the generation of reactive oxygen species important for bacterial killing by macrophages (2,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Bcl10/CIPER/CLAP/mE10 is a widely expressed CARD (caspase recruitment domain) containing protein shown to induce apoptosis and activate NF-κB (1-5). The CARD domain mediates self-oligomerization, interactions with other CARD proteins and is necessary for NF-κB activation, although the precise mechanism which Bcl10 regulates these processes is not fully understood. The discovery of Bcl10 came from observations of the chromosomal translocation t(1;14)(p22;q32) from B cell lymphomas of the mucosa-associated lymphoid tissue (MALT) (1,5). This translocation results in deregulated expression of a truncated form of Bcl10 which lacks apoptotic activity and enhances transformation. Studies from Bcl10 deficient mice demonstrate that Bcl10 is essential for the activation of NF-κB by T- and B-cell receptors (6). One third of Bcl10 deficient mice developed lethal exencephaly. Surviving mice were unaffected by various apoptotic stimuli, but were severely immunodeficient and defective in antigen receptor-induced NF-κB activiation. PKC or T-cell receptor signaling results in a downregulation of Bcl10 protein levels, attenuating both NF-κB activation and cellular proliferation and also provides a negative feedback regulation of the NF-κB signaling to T cell signaling (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Mucosa-associated lymphoid tissue translocation gene 1 (MALT1) is a paracaspase that is a critical mediator of T-cell receptor activation of NF-κB and may contribute to the progression of MALT lymphomas (1-4). It contains two immunoglobulin-like domains, an amino-terminal death domain and a carboxy-terminal caspase-like domain. Association of MALT1 with Bcl-10 and CARD11/Carma1 leads to activation of IKK and subsequent stimulation of NF-κB, resulting in increased proliferation and inhibition of apoptosis (5,6). A common translocation in MALT B-cell non-Hodgkin lymphomas t(11;18)(q21;q21) results in the fusion of the amino terminus of API2 (c-IAP2), a member of the inhibitor of apoptosis protein family, to the carboxy terminus of MALT1 (1,2). The API2-MALT1 fusion protein likely leads to deregulation of NF-κB, contributing to increased oncogenic potential (7).