TrkB (pS478) Positive Control Cell Lysate (Mouse NSC-34)-50 µg Reference: CL-2107-50 This cell lysate is suitable as positive control for Western Blotting, to confirm TrkB phosphorylation at amino acid S478 (rat/mouse) or S479 (human), respectively, using TrkB (pS478/479) rabbit antibody R-1718-50. It is particular useful for complex Western Blotting samples to identify TrkB (pS478/479) immunoreactive bands. This lysate has been prepared by triggering TrkB phosphorylation in retinoic acid-treated mouse NSC34 cells with mature BDNF, and subsequent processing with RIPA buffer. The cell lysate is provided lyophilised for extended stability.
EnhancedFasL, Soluble (human) (rec.) Pack Reference: AG-44B-0001 FasL, Soluble (human) (rec.) induces apoptosis in a concentration range of <1ng/ml in the presence of 0.1 to 1µg/ml of TNF Ligands Enhancer (Prod. No. AG-35B-0001). (Optimal conditions must be determined individually for each cell line tested)
EnhancedTRAIL, Soluble (human) (rec.) Pack Reference: AG-44B-0002 Induces apoptosis in a concentration range of 5-50ng/ml in the presence of 1µg/ml of TNF Ligands Enhancer (Prod. No. AG-35B-0001).
TRAIL-R1 to -R4 Flow Cytometry Pack Reference: AG-44B-0004 TRAIL-R1, -R2, -R3 and -R4 are receptors for the cytotoxic ligand TRAIL. When signaling through TRAIL-R1 and -R2, the adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. They promote the activation of NF-kappaB. TRAIL-R3 lacks a cytoplasmic death domain, and TRAIL-R4 contains a truncated death domain, and hence are not capable of inducing apoptosis. They protect cells against TRAIL mediated apoptosis by competing with TRAIL-R1 and R2 for binding to the ligand.
IDO1 (human) Enzyme+Inhibitor Set Reference: AG-44B-0006 IDO1 is a heme-containing enzyme that catalyzes the first and rate-limiting step in the main pathway of human tryptophan catabolism, the kynurenine pathway, causing depletion of tryptophan which can lead to halted growth of microbes as well as T cells. IDO1 is an immune checkpoint protein, that plays a role in a variety of pathophysiological processes such as antimicrobial and antitumor defense, neuropathology, immunoregulation and antioxidant activity. The IDO1 (human) Enzyme+Inhibitor Set contains the active enzyme IDO1 (human) (rec.) (His) (AG-40B-0161), compound MMG-0358 (AG-CR1-3630), a very potent and specific inhibitor of IDO1, and protocols that can be used for IDO1 enzyme activity and IDO1 inhibition experiments. Both components can be used in vitro: • For cell culture to study the effect of hIDO1 in a cellular system.• For screening assay to search for new inhibitors of hIDO1.
RELM-beta (human) Matched Pair Detection Set Reference: AG-46A-0001 RELM-beta is a 19kDa disulfide-linked homodimeric protein expressed in the epithelium of the colon and small bowel. RELM-beta has been suggested to play a regulatory role during inflammation and may also act to establish links among adipose tissue, the intestine and the liver. Interestingly, the molecular structure of RELM-beta is highly homologous to that of the adipose-derived cytokine resistin. The specific and sensitive RELM-beta Matched Pair Detection Set might detect RELM-beta in serum of gut-inflamed patients (e.g. inflammatory bowel diseases, Crohn disease and ulcerative colitis). Natural levels of RELM-beta were seen in stool, but were not detectable in the serum or other cell culture models of healthy human patients. Further testing are ongoing.
BAFF, Soluble (human) Matched Pair Detection Set Reference: AG-46B-0001 BAFF (B cell-activating factor; BLyS; B lymphocyte stimulator; TNFSF13B; TALL-1; CD257), belonging to the TNF family, is a master regulator of peripheral B cell survival, and together with IL-6, promotes Ig class-switching and plasma cell differentiation. BAFF co-stimulates activated T cells. Increased levels of soluble BAFF have been detected in the serum of patients with various autoimmune diseases, such as Sjögren’s syndrome, rheumatoid arthritis, multiple sclerosis and systemic lupus erythematosus (SLE). Furthermore, BAFF is found in inflammatory sites in which there is lymphoid neogenesis. BAFF levels are elevated in patients with multiple myeloma and B cell chronic lymphoid leukemia (B-CCL).
Periostin (mouse) Matched Pair Detection Set Reference: AG-46B-0002 Periostin is a 90-kDa matricellular protein that consists of a typical signal sequence, followed by a cysteine-rich region, an EMI domain (protein-protein interactions), four tandem fasciclin-like domains that are responsible for integrin binding, and a C-terminal region. Periostin was originally isolated as an osteoblast-specific factor that functions as a cell adhesion molecule for pre-osteoblasts and in osteoblast recruitment, attachment and spreading. Periostin is also involved in many fundamental biological processes such as cell proliferation, cell invasion and angiogenesis. Periostin expression is increased by both transforming growth factor beta1 (TGF-beta1) and bone morphogenetic protein 2 (BMP-2). Changes in periostin expression are commonly detected in various cancers and pre-cancerous conditions, and periostin may be involved in regulating cancer cell activities that contribute to tumorigenesis, cancer progression and metastasis. Periostin up-regulation in cancers usually correlates with aggressiveness and/or poor survival. Periostin has shown to be involved in many aspects of allergic inflammation, such as eosinophil recruitment, airway remodeling, development of a Th2 phenotype and increased expression of inflammatory mediators. It is evaluated as a biomarker for bronchial asthma and airway inflammation.
Caspase-1 (mouse) Matched Pair Detection Set Reference: AG-46B-0003 Caspase-1 is the best-described inflammatory caspase. It processes the cytokines interleukin-1beta (IL-1beta) and interleukin-18 (IL-18) and induces pyroptotic cell death. Caspase-1 is activated by multiprotein complexes called inflammasomes in response to numerous stimuli that are detected through distinct inflammasomes. NLRC4 responds to cytosolic flagellin, murine NLRP1b responds to anthrax lethal toxin, AIM2 responds to cytosolic DNA and NLRP3/NALP3 responds to a variety of agonists including crystals. The caspase-1 (mouse) Matched Pair Detection Set contains all reagents for the development of a sandwich ELISA to measure caspase-1 (mouse) in cell culture supernatants. This Matched Pair Detection Set is a quantitative detection method, alternative to Western blotting to measure caspase-1 secretion.
IL-1alpha (mouse) Matched Pair Detection Set Reference: AG-46B-0004 The most prominent members of the interleukin-1 (IL-1) superfamily are IL-1alpha and IL-1beta. They lack a signal peptide and are secreted by an unconventional, endoplasmic reticulum-Golgi-independent mechanism. IL-1alpha was reported to be more widely and constitutively expressed and has intracellular functions, but also acts locally in a membrane-bound form by activating IL-1R1. Additionally, passive release of IL-1alpha upon cell death can trigger a sterile inflammatory response to dying cells. The cleavage of IL-1alpha is not mediated by caspase-1 and is not required for binding to IL-1R1. Recently it has been observed that all activators of the inflammasome NLRP3/NALP3 induce the simultaneous secretion of IL-1alpha and IL-1beta. Although most activators fully rely on the inflammasome for IL-1alpha secretion, some induce the processing and secretion of IL-1alpha in an inflammasome-independent manner.
Periostin (human) Matched Pair Detection Set Reference: AG-46B-0005 Periostin is a 90-kDa matricellular protein that consists of a typical signal sequence, followed by a cysteine-rich region, an EMI domain (protein-protein interactions), four tandem fasciclin-like domains that are responsible for integrin binding, and a C-terminal region. Periostin was originally isolated as an osteoblast-specific factor that functions as a cell adhesion molecule for pre-osteoblasts and in osteoblast recruitment, attachment and spreading. Periostin is also involved in many fundamental biological processes such as cell proliferation, cell invasion and angiogenesis. Periostin expression is increased by both transforming growth factor beta1 (TGF-beta1) and bone morphogenetic protein 2 (BMP-2). Changes in periostin expression are commonly detected in various cancers and pre-cancerous conditions, and periostin may be involved in regulating cancer cell activities that contribute to tumorigenesis, cancer progression and metastasis. Periostin up-regulation in cancers usually correlates with aggressiveness and/or poor survival. Periostin has shown to be involved in many aspects of allergic inflammation, such as eosinophil recruitment, airway remodeling, development of a Th2 phenotype and increased expression of inflammatory mediators. It is evaluated as a biomarker for bronchial asthma and airway inflammation.
IL-36Ra (human) Matched Pair Detection Set Reference: AG-46B-0006 IL-36Ra/IL-1F5 is a highly and specific antagonist of the IL-1 receptor-related protein 2-mediated response to IL-36alpha (IL-1F6), IL-36beta (IL-1F8) and IL-36gamma (IL-1F9). These cytokines bind to IL-36R (IL-1Rrp2) and IL-1RAcP, activating similar intracellular signals as IL-1. IL-36Ra inhibits the production of proinflammatory cytokines, including IL-12, IL-1beta, IL-6, TNF-alpha and IL-23 induced by IL-36 in BMDC and CD4 T cells. Skin and dendritic cells are targets of the IL-36 interleukins leading to a Th1 response. Recently mutations that affect the levels and the activity of IL-36Ra have been found in patients with pustular psoriasis, leading to enhanced production of inflammatory cytokines (IL-8 in particular) by keratinocytes.