Antibody News

IL-33 is a member of the interleukin family of cytokines that regulates a wide variety of cellular functions. Its receptor is ST2, an IL-1 receptor family member that also acts as a negative regulator of TLR-IL-1R signaling and the IL-1R accessory protein (IL-1RAcP). Receptor binding of IL-33 activates NF-kB and MAP kinases, stimulating downstream expression of TH2-associated cytokines such as IL-4, IL-5 and IL-6. Prolonged IL-33 treatment in mice leads to the development of eosinophilia, splenomegaly, and severe pathological changes in mucosal organs. IL-33 has been shown to co-localize with heterochromatin and possesses transcriptional repressor activities, suggesting that it may function as both a proinflammatory cytokine as well as an intracellular nuclear factor with transcriptional regulatory properties.

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NUT has been found to fuse with bromodomain-containing proteins 3 and 4 (BRD3 and BRD4) in NUT midline carcinoma (NMC), a very rare, extremely aggressive, and genetically defined human cancer. NMC has recently been designated as a sub classification of poorly differentiated squamous cell carcinoma. In the majority of NMCs (~75%), most of the coding sequence is fused to form chimeric genes that encode BRD-NUT fusion proteins. This simple chromosomal translocation results in elevated NUT overexpression and is sufficient for malignancy. The actual structure and function of the NUT protein is still unclear.

Immunohistochemistry-Paraffin: NUT Antibody 

A case report of...

PABP is found complexed to the 3-prime poly(A) tail of eukaryotic mRNA and is required for poly(A) shortening, translation initiation, and possibly mRNA export and import. In humans, PABPs are small nuclear isoforms within a conserved gene family of at least 3 functional proteins: PABP1 (PABPC1), inducible PABP (iPABP, or PABPC4), and PABP3 (PABPC3). PABPs are of special interest because due to their high affinity for A-rich mRNA sequences, they are involved in all mRNA-dependent events. Not surprisingly, they interact with a wide variety of proteins and are important to study because RNA-binding proteins are the foundation for proper mRNA function and organization within the cell.

Immunocytochemistry/Immunofluorescence: PABP Antibody

The...

TNF alpha is a multifunctional proinflammatory cytokine that is part of the tumor necrosis factor (TNF) superfamily. It is mainly secreted by macrophages and causes tumor necrosis when injected into tumor -earing mice. It exists as a multimer of two, three, or five noncovalently linked units. TNF alpha is closely related to the 25kD Tumor Necrosis Factor beta (TNF beta, or lymphotoxin), and both proteins share the same receptors and cellular functions. TNF alpha binds and functions through the TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR receptors. It is involved in the regulation of a wide spectrum of biological processes - cell proliferation, differentiation, apoptosis, lipid metabolism, and coagulation. TNF alpha has been implicated in a variety of conditions, including autoimmune diseases, insulin resistance, and cancer.

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CRLF2 has been reported as an important factor that drives dendritic cell maturation and activation. It was originally shown to participate in the positive selection of regulatory T-cells, maintenance of peripheral CD4+ T-cell homeostasis, and induction of CD4+ T cell-mediated allergic reactions. CRLF2 binds to its receptor with low-affinity; high-affinity binding is facilitated by the presence of IL-7R-alpha to form a functional heteromeric complex. This protein is also capable of supporting the growth of fetal liver and adult B-cell progenitors. CRLF2 is now known to have wide-ranging roles not just in these hematopoietic cell lineages, but also in multiple disease states within multiple organ systems.

Western Blot: TSLP R/CRLF2 Antibody 

NALP6 belongs to the NLRP family of which function as innate sensors of endogenous and exogenous stress and damage-associated molecular patterns (DAMPs). NLRPs are vital components of the inflammasome which is the cytoplasmic multiprotein complex that coordinates inflammation and cell homeostasis in various type of cells/tissues. NALP6 is one of the newest NLR protein family members and is highly expressed in intestinal epithelium and granulocytes, and to a relatively lower level in T-cells. NALP6 behaves as an arginine-vasopressin V2 receptor and has been suggested to contribute to AVP-mediated regulation of renal salt-water balance, glucose and lipid metabolism, apoptosis, and the cell cycle.

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Peroxisome proliferators are non-genotoxic carcinogens which are purported to exert their effect on cells by interacting with members of the nuclear hormone receptor superfamily known as peroxisome proliferator activated receptors (PPARs). There are four of these nuclear hormone receptors known to date, and they are ligand-dependent intracellular proteins that stimulate downstream gene transcription of genes such as acyl coenzyme A oxidase and cytochrome P450 (CYP450). Activation occurs through direct binding to specific DNA response elements following activation by an appropriate ligand. PPARs have pleiotropic effects upon a wide range of cellular functions including vascular tone, inflammation and energy homeostasis. Because of this, PPARs are important targets to consider in therapies for hypertension, obesity, and metabolic syndromes.

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SHARP1 encodes a transcription repressor factor that belongs to the Hairy/Enhancer of the Split subfamily of basic helix-loop-helix factors (bHLH). Sequence alignment shows that SHARP1 is only distantly related to these proteins with a 37-42% sequence identity within its bHLH domain. Unlike most other bHLH proteins, SHARP-1 is not expressed in neuronal progenitor cells or early differentiating neurons but is instead restricted to neuronal subset within the postnatal central nervous system (CNS). SHARP1 appears to play a regulatory role in the clockwork system integrating with Clock and Bmal1. Mutations in this gene (designated hDEC2-P385R) are associated with short sleep phenotypes in both humans and mice, resulting in elevated levels of vigilance time and concomitant decreases in sleep time.

CD73 is a 70kD glycosyl-phosphatidylinositol (GPI)-anchored cell surface molecule that belongs to the 5'-nucleosidase family. It hydrolyzes extracellular nucleotides into membrane permeable nucleosides and is found as both a membrane-bound and soluble molecule. Because it is abundantly expressed on vascular endothelium and some lymphocyte subpopulations, CD73 is a useful lymphocyte differentiation marker. Like many other GPI-anchored molecules, it transmits T-cell activation signals upon ligand engagement. CD73 functions as a co-stimulatory molecule in human T-cells for both proliferation and activation, and also appears to modulate lymphocyte adhesion. Furthermore, the ecto-5'-nucleotidase activity itself is an important mediator of anti-inflammation because it converts extracellular AMP into adenosine which is a potent anti-inflammatory trigger. 

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CD90 is a 25-35kD glycosylphosphatidylinositol (GPI)-linked glycoprotein receptor of the immunoglobulin (Ig) superfamily. It is found on murine T-cells, thymocytes, neuronal cells, granulocytic lineage-derived cells, hematopoietic stem cells, fibroblasts, neurons, and Kupffer's cells. CD90 is often used as a marker for a variety of stem cells and mature neuronal axon processes.  CD90 appears to play a role in cell-cell and cell-matrix interactions and adhesion during synaptogenesis, nerve regeneration, apoptosis and necrosis, inflammation, fibrosis, and metastasis.

Flow cytometry studies with the CD90 antibody were used by Mayani et al to phenotype cord blood cells (1). Those researchers correlated CD90 expression to the highest levels of proliferative potential...

CD16 is a lymphocyte Fc gamma type III low-affinity receptor for IgG and is represented by two similar genes, CD16A (Fc gamma RIII A) and CD16B (Fc gamma RIIIB). CD16A exists as a heterooligomeric polypeptide-anchored form in macrophages and NK cells. CD16B exists as a monomeric glycosylphosphatidylinositol (GPI)-anchored form in neutrophils. CD16 binds IgG in the form of immune complexes or free antibody. It exhibits preferential binding to IgG1 and IgG3 isotypes, with minimal binding of IgG2 and IgG4. Upon IgG binding, both CD16 isoforms initiate signaling cascades that produce a diverse variety of responses including antibody-dependent cell-mediated cytotoxicity (ADCC), phagocytosis, degranulation, and proliferation. CD16 is expressed on macrophages, natural killer (NK) cells and neutrophils. Their expression is constitutive, although cytokines and lymphokines can modulate their expression levels.

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