目录号 | 产品详情 | 靶点 | |
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T36489 | |||
Malformin A is a cyclopentapeptide fungal metabolite that has been found in A. niger and has diverse biological activities. It is a plant growth regulator that induces malformations in plant structure. Malformin A inhibits replication of tobacco mosaic virus (TMV) in local lesion and leaf-disc assays (IC50s = 19.7 and 45.4 μg/ml, respectively). It is cytotoxic to NCI-H460, MIA PaCa-2, MCF-7, SF-268, and WI-38 cancer cells (IC50s = 70, 50, 100, 70, and 100 nM, respectively), inhibits proliferation of PC3 and LNCaP cells (IC50s = 130 and 90 nM, respectively), and induces apoptosis and necrosis in PC3 and LNCaP cells. Malformin A also increases the accumulation of reactive oxygen species, decreases the mitochondrial membrane potential, and induces autophagy in PC3 and LNCaP cells. It is toxic to mice when administered intraperitoneally (LD50 = 3.1 mg/kg) but not orally up to doses of 50 mg/kg. | |||
T35904 | |||
O-11 is an analog of the fully saturated, 14-carbon fatty acid myristic acid, in which the methylene group at position 11 is replaced with oxygen. It is highly effective and selective at killingTrypanosoma brucei, the protozoan parasite responsible for African sleeping sickness, exhibiting an LD50of less than 1 μM in a cell culture assay.1,2The toxic effects of O-11 appear to be caused by its ability to inhibit the incorporation of a single myristate into the GPI anchor of the variant surface glycoprotein (VSG), a protein critical for evading the host immune response.1O-11 exhibits essentially no anti-fungal activity when assayed usingC. neoformans, but does have a minor inhibitory effect on HIV-1 replication in T-lymphocytes.3 1.Doering, T.L., Raper, J., Buxbaum, L.U., et al.An analog of myristic acid with selective toxicity for African trypanosomesScience2521851-1854(1991) 2.Doering, T.L., Lu, T., Werbovetz, K.A., et al.Toxicity of myristic acid analogs toward African trypanosomesProceedings of the National Academy of Sciences of the United States of America919735-9739(1994) 3.Langner, C.A., Lodge, J.K., Travis, S.J., et al.4-Oxatetradecanoic acid is fungicidal for Cryptococcus neoformans and inhibits replication of human immunodeficiency virus IThe Journal of Biological Chemisty267(24)17159-17169(1992) | |||
T36947 | |||
Pyrithiamine is the pyridine analog of thiamine that prevents growth of organisms that require intact thiamine. [1] It inhibits the growth of bacterial and fungal species at a pyrithiamine:thiamine ratio of 10:1 in growth media and induces symptoms of thiamine deficiency in mice at a dietary ratio of 3:1. These effects are reversible with addition of sufficient thiamine in all species. Pyrithiamine inhibits the formation of cocarboxylase from thiamine in chicken blood in a dose-dependent manner. [2] It has been used to induce thiamine deficiency in various disease models, including rat models of alcoholism and diencephalic amnesia, to study the effects of thiamine deficiency on disease pathology.[3] [4] Reference:[1]. Woolley, D.W., and White, A.G.C. Selective reversible inhibition of microbial growth with pyrithiamine. J. Exp. Med. 78(6), 489-497 (1943).[2]. Woolley, D.W. An enzymatic study of the mode of action of pyrithiamine (neopyrithiamine). J. Biol. Chem. 191(1), 43-54 (1951).[3]. Vetreno, R.P., Anzalone, S.J., and Savage, L.M. Impaired, spared, and enhanced ACh efflux across the hippocampus and striatum in diencephalic amnesia is dependent on task demands. Neurobiol. Learn Mem. 90(1), 237-244 (2008).[4]. Zahr, N.M., Sullivan, E.V., Rohlfing, T., et al. Concomitants of alcoholism: Differential effects of thiamine deficiency, liver damage, and food deprivation on the rat brain in vivo. Psychopharmacology (Berl) 233(14), 2675-2686 (2016). | |||
T36054 | |||
D13 is an acylhydrazone antifungal.1 It is active against C. neoformans in vitro (MIC80 = 0.06 μg/ml). D13 (20 mg/kg per day, p.o.) increases survival in mouse models of C. neoformans, C. albicans, or A. fumigatus infection. |1. Lazzarini, C., Haranahalli, K., Rieger, R., et al. Acylhydrazones as antifungal agents targeting the synthesis of fungal sphingolipids. Antimicrob. Agents Chemother. 62(5), e00156-00118 (2018). | |||
T41322 | |||
Dimethomorph 是一种吗啉类杀菌剂,属于甾醇生物合成抑制剂类杀菌剂,可抑制真菌细胞壁的形成。Dimethomorph 抑制了oomycete fungi,P. citrophthora,P. parasitica,P. capsici,和P. infestans 的菌丝生长 (EC50=0.14 μg/mL,0.38 μg/mL,<0.1 μg/mL 和 0.16-0.3 μg/mL),但是对绿藻物种C. vulgaris 和S. obliquus 的活性较低 (EC50=47.46 μg/mL 和 44.87 μg/mL)。在 MDA-kb2 人乳腺癌细胞的报告基因分析中,Dimethomorph 抑制雄激素受体 (AR) 的活性,而在酵母抗雄激素筛选中不起作用 (IC20=0.263 μM 和 38.5 μM)。 | |||
T36226 | |||
Beauveriolide I is a cyclodepsipeptide that has been found inBeauveriaand an inhibitor of lipid droplet formation.1It inhibits lipid droplet formation when used at concentrations of 3 and 10 μM, as well as inhibits cholesterol synthesis (IC50= 0.78 μM), in primary mouse peritoneal macrophages.1,2Beauveriolide I also inhibits acyl-coenzyme A:cholesterol acyltransferase (ACAT) activity in mouse macrophage membranes (IC50= 6 μM).2 1.Namatame, I., Tomoda, H., Si, S., et al.Beauveriolides, specific inhibitors of lipid droplet formation in mouse macrophages, produced by Beauveria sp. FO-6979J. Antibiot. (Tokyo)52(1)1-6(1999) 2.Namatame, I., Tomoda, H., Ishibashi, S., et al.Antiatherogenic activity of fungal beauveriolides, inhibitors of lipid droplet accumulation in macrophagesProc. Nat. Acad. Sci. USA101(3)737-742(2004) | |||
T36227 | |||
Beauveriolide III is a cyclodepsipeptide that has been found inBeauveriaand an inhibitor of lipid droplet formation.1It inhibits lipid droplet formation when used at concentrations of 3 and 10 μM, as well as inhibits cholesterol synthesis (IC50= 0.41 μM), in primary mouse peritoneal macrophages.1,2Beauveriolide III also inhibits acyl-coenzyme A:cholesterol acyltransferase (ACAT) activity in mouse macrophage membranes (IC50= 5.5 μM).2Beauveriolide III (25 and 50 mg/kg) reduces the size of aortic atherosclerotic lesions inLdlr-/-andApoE-/-mouse models of atherosclerosis. 1.Namatame, I., Tomoda, H., Si, S., et al.Beauveriolides, specific inhibitors of lipid droplet formation in mouse macrophages, produced by Beauveria sp. FO-6979J. Antibiot. (Tokyo)52(1)1-6(1999) 2.Namatame, I., Tomoda, H., Ishibashi, S., et al.Antiatherogenic activity of fungal beauveriolides, inhibitors of lipid droplet accumulation in macrophagesProc. Nat. Acad. Sci. USA101(3)737-742(2004) | |||
T35779 | |||
Oosporein is a mycotoxin that has been found inBeauveriaand has diverse biological activities.1,2It is cytotoxic to Sf9 and Sf21 insect cells with 50% cytotoxic concentration (CC50) values of 4.23 and 10.43 μM, respectively.3Oosporin induces lethality in day-old cockerels (LD50= 6.12 mg/kg).4It inhibits Na+/K+-, Ca2+-, and Mg2+-ATPase activities by 27, 52, and 100%, respectively, in equine erythrocyte ghosts when used at a concentration of 200 μg/ml.2Oosporein inhibits herpes simplex 1 (HSV-1), but not HeLa cell orE. coli, DNA polymerase (IC50s = 75, 610, and >700 μM, respectively).5It is active against the bacteriumS. pneumoniae(MIC = 32 μg/ml) and the plant pathogenic fungusP. infestans(MIC = 16 μM).1,6 1.Wainwright, M., Betts, R.P., and Teale, D.M.Antibiotic activity of oosporein from Verticillium psalliotaeTrans. Br. Mycol. Soc.86(1)168-170(1986) 2.Jeffs, L.B., and Khachatourians, G.G.Toxic properties of Beauveria pigments on erythrocyte membranesToxicon. 35(8)1351-1356(1997) 3.Arboleda Valencia, J.W., Gaitán Bustamante, A.L., Jiménez, A.V., et al.Cytotoxic activity of fungal metabolites from the pathogenic fungus Beauveria bassiana: An intraspecific evaluation of beauvericin productionCurr. Microbiol.63(3)306-312(2011) 4.Cole, R.J., Kirksey, J.W., Cutler, H.G., et al.Toxic effects of oosporein from Chaetomium trilateraleJ. Agric. Food Chem.22(3)517-520(1974) 5.Terry, B.J., Liu, W.C., Cianci, C.W., et al.Inhibition of herpes simplex virus type 1 DNA polymerase by the natural product oosporeinJ. Antibiot. (Tokyo)45(2)286-288(1992) 6.Nagaoka, T., Nakata, K., Kouno, K., et al.Antifungal activity of oosporein from an antagonistic fungus against Phytophthora infestansZ. Naturforsch. C. J. Biosci.59(3-4)302-304(2004) | |||
T35772 | |||
Emestrin is a mycotoxin originally isolated from E. striata that has antimicrobial, immunomodulatory, and cytotoxic activities.1,2,3,4,5 It is active against the fungi C. albicans and C. neoformans, as well as the bacteria E. coli, S. aureus, and methicillin-resistant S. aureus (MRSA; IC50s = 3.94, 0.6, 2.21, 4.55, and 2.21 μg/ml, respectively).2 Emestrin is a chemokine (C-C motif) receptor 2 (CCR2) antagonist (IC50 = 5.4 μM in a radioligand binding assay using isolated human monocytes).3 Emestrin (0.1 μg/ml) induces apoptosis in HL-60 cells.4 It induces heart, thymus, and liver tissue necrosis in mice when administered at doses ranging from 18 to 30 mg/kg.5 |1. Seya, H., Nakajima, S., Kawai, K.-i., et al. Structure and absolute configuration of emestrin, a new macrocyclic epidithiodioxopiperazine from Emericella striata. J. Chem. Soc. Chem. Commun. 10, 657-658 (1985).|2. Herath, H.M.T.B., Jacob, M., Wilson, A.D., et al. New secondary metabolites from bioactive extracts of the fungus Armillaria tabescens. Nat. Prod. Res. 27(17), 1562-1568 (2013).|3. Herath, K.B., Jayasuriya, H., Ondeyka, J.G., et al. Isolation and structures of novel fungal metabolites as chemokine receptor (CCR2) antagonists. J. Antibiot. (Tokyo) 58(11), 686-694 (2005).|4. Ueno, Y., Umemori, K., Niimi, E.-c., et al. Induction of apoptosis by T-2 toxin and other natural toxins in HL-60 human promyelotic leukemia cells. Nat. Toxins 3(3), 129-137 (1995).|5. Terao, K., Ito, E., Kawai, K.-i., et al. Experimental acute poisoning in mice induced by emestrin, a new mycotoxin isolated from Emericella species. Mycopathologia 112(2), 71-79 (1990). |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPY-01371 | IL-17RA Protein, Human, Recombinant (His) | Human | HEK293 | ||
Interleukin-17 receptor (IL-17R), also known as Interleukin-17 receptor A (IL-17RA) and CD217 antigen (CD217), is a cytokine receptor that binds interleukin 17. IL-17R/IL-17RA (CD217) is a proinflammatory cytokine secreted by activated T-lymphocytes. It is a potent inducer of the maturation of CD34-positive hematopoietic precursors into neutrophils. IL-17R/IL-17RA (CD217) is a ubiquitous type I membrane glycoprotein that binds with low affinity to interleukin 17A. Interleukin 17A and its receptor IL-17RA play a pathogenic role in many inflammatory and autoimmune diseases such as rheumatoid arthritis. Like other cytokine receptors, this receptor likely has a multimeric structure. Defects in IL-17R/IL-17RA (CD217) are the cause of familial candidiasis type 5 (CANDF5). CANDF5 is a rare disorder with altered immune responses and impaired clearance of fungal infections, selective against Candida. It is characterized by persistent and/or recurrent infections of the skin, nails, and mucous membranes caused by organisms of the genus Candida, mainly Candida albicans.
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TMPY-00772 | DC-SIGN Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
Dendritic cell (DC)-specific intercellular adhesion molecule 3 (ICAM-3) grabbing nonintegrin (DC-SIGN), also known as CD209, is a type II transmembrane protein on DCs with a C-type lectin extracellular domain, is capable of binding ICAM-3 on resting T cells in the secondary lymphoid organs, providing the initial contact between these cells during the establishment of cell-mediated immunity. It is not only a pattern recognition receptor but implicated in immunoregulation of DCs. It has an important role in mediating DC adhesion, migration, inflammation, activating primary T cell, triggering immune response and participating in immune escape of pathogens and tumors. DC-SIGN also mediates the capture and internalization of viral, bacterial, and fungal pathogens by dendritic cells, such as HIV-1, Ebola virus, cytomegalovirus, Dengue virus, and hepatitis C virus. DC-SIGN is unique in that it regulates adhesion processes, such as DC trafficking and T-cell synapse formation, as well as antigen capture. Moreover, even though several C-type lectins have been shown to bind HIV-1, DC-SIGN does not only capture HIV-1 but also protects it in early endosomes allowing HIV-1 transport by DC to lymphoid tissues, where it enhances trans infection of T cells.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-04483 | IRAK4 Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
Interleukin-1 receptor-associated kinase 4, also known as Renal carcinoma antigen NY-REN-64, IRAK-4, and IRAK4, is a member of the protein kinase superfamily, TKL Ser/Thr protein kinase family, and Pelle subfamily. IRAK4 contains one death domain and one protein kinase domain. IRAK4 is required for the efficient recruitment of IRAK1 to the IL-1 receptor complex following IL-1 engagement, triggering intracellular signaling cascades leading to transcriptional up-regulation and mRNA stabilization. It also phosphorylates IRAK1. A member of the IL-1 receptor (IL-1R)-associated kinase (IRAK) family, IRAK4, has been shown to play an essential role in Toll-like receptor (TLR)-mediated signaling. IL-1-mediated IRAK4 kinase activity in T cells is essential for the induction of IL-23R expression, Th17 differentiation, and autoimmune disease. Pharmacological blocking of IRAK4 kinase activity will retain some levels of host defense while reducing the levels and duration of inflammatory responses, which should provide beneficial therapies for sepsis and chronic inflammatory diseases. Defects in IRAK4 are the cause of recurrent isolated invasive pneumococcal disease type 1 (IPD1) which is defined as two episodes of IPD occurring at least 1 month apart, whether caused by the same or different serotypes or strains. Recurrent IPD occurs in at least 2% of patients in most series, making IPD the most important known risk factor for subsequent IPD. Defects in IRAK4 are also the cause of IRAK4 deficiency which causes extracellular pyogenic bacterial and fungal infections in otherwise healthy children.
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TMPH-03738 | Endochitinase B Protein, Zea mays, Recombinant (His & Myc) | Zea mays | E. coli | ||
Defense against chitin-containing fungal pathogens.
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TMPH-00819 | Pro-hevein Protein, Hevea brasiliensis, Recombinant (His) | Hevea brasiliensis | E. coli | ||
N-acetyl-D-glucosamine / N-acetyl-D-neuraminic acid binding lectin. Can inhibit fungal growth.
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TMPH-03231 | AFP2 Protein, Raphanus sativus, Recombinant (His & SUMO) | Raphanus sativus | E. coli | ||
Possesses antifungal activity sensitive to inorganic cations. Induces potential changes in fungal membranes and increased K(+) efflux and Ca(2+) uptake.
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TMPH-00036 | Polyphenol oxidase 2 Protein, Agaricus bisporus, Recombinant (His & Myc) | Agaricus bisporus | E. coli | ||
Copper-containing oxidase that catalyzes both the o-hydroxylation of monophenols and the subsequent oxidation of the resulting o-diphenols into reactive o-quinones, which evolve spontaneously to produce intermediates, which associate in dark brown pigments. Involved in the initial step of melanin synthesis. Melanins constitute a mechanism of defense and resistance to stress such as UV radiations, free radicals, gamma rays, dehydratation and extreme temperatures, and contribute to the fungal cell-wall resistance against hydrolytic enzymes in avoiding cellular lysis. Fungal pigments are also involved in the formation and stability of spores.
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TMPH-00035 | Polyphenol oxidase 2 Protein, Agaricus bisporus, Recombinant (His) | Agaricus bisporus | Baculovirus | ||
Copper-containing oxidase that catalyzes both the o-hydroxylation of monophenols and the subsequent oxidation of the resulting o-diphenols into reactive o-quinones, which evolve spontaneously to produce intermediates, which associate in dark brown pigments. Involved in the initial step of melanin synthesis. Melanins constitute a mechanism of defense and resistance to stress such as UV radiations, free radicals, gamma rays, dehydratation and extreme temperatures, and contribute to the fungal cell-wall resistance against hydrolytic enzymes in avoiding cellular lysis. Fungal pigments are also involved in the formation and stability of spores.
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TMPH-00761 | Cutinase Protein, Fusarium solani subsp. Cucurbitae, Recombinant | Neocosmosporum cucurbitae | E. coli | ||
Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle. Allows pathogenic fungi to penetrate through the cuticular barrier into the host plant during the initial stage of the fungal infection.
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TMPH-00760 | Cutinase Protein, Fusarium solani subsp. Cucurbitae, Recombinant (His) | Neocosmosporum cucurbitae | Yeast | ||
Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle. Allows pathogenic fungi to penetrate through the cuticular barrier into the host plant during the initial stage of the fungal infection.
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TMPY-00016 | Dectin-1 Protein, Human, Recombinant (mFc) | Human | HEK293 | ||
Dectin-1 was recently identified as the most important receptor for beta-glucan. It is a type II transmembrane protein which binds beta-1,3 and beta-1,6 glucans, and is expressed on most cells of the innate immune system and has been implicated in phagocytosis as well as killing of fungi by macrophages, neutrophils and dendritic cells. Recognition of beta-glucan by dectin-1 triggers effective immune response, including phagocytosis and proinflammatory factor production, to eliminate infecting fungi, which especially benefits immunocompromised patients against opportunistic fungal infection. In addition, dectin-1 is involved in the adaptive immune response as well as autoimmune diseases and immune tolerance. Dectin-1 can recognize and respond to live fungal pathogens and is being increasingly appreciated as having a key role in the innate responses to these pathogens. In addition to its exogenous ligands, Dectin-1 can recognize an unidentified endogenous ligand on T cells and may act as a co-stimulatory molecule. Recent studies have highlighted the importance of Dectin-1 in anti-fungal immunity, in both mice and humans, and have suggested a possible involvement of this receptor in the control of mycobacterial infections.
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TMPY-03726 | Dectin-1 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
Dectin-1 was recently identified as the most important receptor for beta-glucan. It is a type II transmembrane protein which binds beta-1,3 and beta-1,6 glucans, and is expressed on most cells of the innate immune system and has been implicated in phagocytosis as well as killing of fungi by macrophages, neutrophils and dendritic cells. Recognition of beta-glucan by dectin-1 triggers effective immune response, including phagocytosis and proinflammatory factor production, to eliminate infecting fungi, which especially benefits immunocompromised patients against opportunistic fungal infection. In addition, dectin-1 is involved in the adaptive immune response as well as autoimmune diseases and immune tolerance. Dectin-1 can recognize and respond to live fungal pathogens and is being increasingly appreciated as having a key role in the innate responses to these pathogens. In addition to its exogenous ligands, Dectin-1 can recognize an unidentified endogenous ligand on T cells and may act as a co-stimulatory molecule. Recent studies have highlighted the importance of Dectin-1 in anti-fungal immunity, in both mice and humans, and have suggested a possible involvement of this receptor in the control of mycobacterial infections.
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TMPY-04013 | Dectin-1 Protein, Human, Recombinant | Human | HEK293 | ||
Dectin-1 was recently identified as the most important receptor for beta-glucan. It is a type II transmembrane protein which binds beta-1,3 and beta-1,6 glucans, and is expressed on most cells of the innate immune system and has been implicated in phagocytosis as well as killing of fungi by macrophages, neutrophils and dendritic cells. Recognition of beta-glucan by dectin-1 triggers effective immune response, including phagocytosis and proinflammatory factor production, to eliminate infecting fungi, which especially benefits immunocompromised patients against opportunistic fungal infection. In addition, dectin-1 is involved in the adaptive immune response as well as autoimmune diseases and immune tolerance. Dectin-1 can recognize and respond to live fungal pathogens and is being increasingly appreciated as having a key role in the innate responses to these pathogens. In addition to its exogenous ligands, Dectin-1 can recognize an unidentified endogenous ligand on T cells and may act as a co-stimulatory molecule. Recent studies have highlighted the importance of Dectin-1 in anti-fungal immunity, in both mice and humans, and have suggested a possible involvement of this receptor in the control of mycobacterial infections.
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TMPY-01387 | Dectin-1 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Dectin-1 was recently identified as the most important receptor for beta-glucan. It is a type II transmembrane protein which binds beta-1,3 and beta-1,6 glucans, and is expressed on most cells of the innate immune system and has been implicated in phagocytosis as well as killing of fungi by macrophages, neutrophils and dendritic cells. Recognition of beta-glucan by dectin-1 triggers effective immune response, including phagocytosis and proinflammatory factor production, to eliminate infecting fungi, which especially benefits immunocompromised patients against opportunistic fungal infection. In addition, dectin-1 is involved in the adaptive immune response as well as autoimmune diseases and immune tolerance. Dectin-1 can recognize and respond to live fungal pathogens and is being increasingly appreciated as having a key role in the innate responses to these pathogens. In addition to its exogenous ligands, Dectin-1 can recognize an unidentified endogenous ligand on T cells and may act as a co-stimulatory molecule. Recent studies have highlighted the importance of Dectin-1 in anti-fungal immunity, in both mice and humans, and have suggested a possible involvement of this receptor in the control of mycobacterial infections.
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TMPY-05009 | Asp f 1 Protein, Neosartorya fumigata, Recombinant (His) | Neosartorya fumigata | HEK293 | ||
Asp f 1 (Aspergillus fumigatus allergen 1) is a major allergen produced by the mycelia of Aspergillus fumigatus. It is not present in spores and can be used as a specific marker for the detection of germination of this fungus. Allergic bronchopulmonary aspergillosis (ABPA) is an immunologically complex allergic disorder caused by the fungal pathogen Aspergillus fumigatus.
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TMPH-00331 | ALS3 Protein, Candida albicans, Recombinant (B2M & His & Myc) | Candida albicans | E. coli | ||
Cell surface adhesion protein which mediates both yeast-to-host tissue adherence and yeast aggregation. Plays an important role in the biofilm formation and pathogenesis of C.albicans infections. Necessary for C.albicans to bind to N-cadherin on endothelial cells and E-cadherin on oral epithelial cells and subsequent endocytosis by these cells. During disseminated infection, mediates initial trafficking to the brain and renal cortex and contributes to fungal persistence in the kidneys.
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TMPY-03173 | Dectin-2 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
C-type lectin domain family 4 member N (CLEC4N), also known as Dectin-2, is a C-type lectin expressed by dendritic cells (DCs) and macrophages. Members of the C-type lectin domain (CTLD) superfamily are metazoan proteins functionally important in glycoprotein metabolism, mechanisms of multicellular integration and immunity. They share a common fold and are involved in a variety of functions, such as generalized defense mechanisms against foreign agents, discrimination between healthy and pathogen-infected cells, and endocytosis and blood coagulation. Genome-level studies on human, elegans and melanogaster demonstrated almost complete divergence among invertebrate and mammalian families of CTLD-containing proteins (CTLDcps). The vertebrate CTLDcp family was essentially formed early in vertebrate evolution and is completely different from the invertebrate families. The composition of the CTLDcp superfamily in fish and mammals suggests that large scale duplication events played an important role in the evolution of vertebrates. Dectin-2 is important in host defense against C. albicans by inducing Th17 cell differentiation. Dectin-2 constitutes a major fungal pattern recognition receptor (PRR) that can couple to the Syk-CARD9 innate signaling pathway to activate DCs and regulate adaptive immune responses to fungal infection.
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TMPY-01202 | Dectin-2 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
C-type lectin domain family 4 member N (CLEC4N), also known as Dectin-2, is a C-type lectin expressed by dendritic cells (DCs) and macrophages. Members of the C-type lectin domain (CTLD) superfamily are metazoan proteins functionally important in glycoprotein metabolism, mechanisms of multicellular integration and immunity. They share a common fold and are involved in a variety of functions, such as generalized defense mechanisms against foreign agents, discrimination between healthy and pathogen-infected cells, and endocytosis and blood coagulation. Genome-level studies on human, elegans and melanogaster demonstrated almost complete divergence among invertebrate and mammalian families of CTLD-containing proteins (CTLDcps). The vertebrate CTLDcp family was essentially formed early in vertebrate evolution and is completely different from the invertebrate families. The composition of the CTLDcp superfamily in fish and mammals suggests that large scale duplication events played an important role in the evolution of vertebrates. Dectin-2 is important in host defense against C. albicans by inducing Th17 cell differentiation. Dectin-2 constitutes a major fungal pattern recognition receptor (PRR) that can couple to the Syk-CARD9 innate signaling pathway to activate DCs and regulate adaptive immune responses to fungal infection.
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TMPH-00337 | HWP1 Protein, Candida albicans, Recombinant (His) | Candida albicans | E. coli | ||
Major hyphal cell wall protein which plays a role of adhesin and is required for mating, normal hyphal development, cell-to-cell adhesive functions necessary for biofilm integrity, attachment to host, and virulence. Promotes interactions with host and bacterial molecules, thus leading to effective colonization within polymicrobial communities. Plays a crucial role in gastrointestinal colonization, in mucosal symptomatic and asymptomatic infections, in vaginitis, as well as in lethal oroesophageal candidiasis, caused by the combined action of fungal virulence factors and host inflammatory responses when protective immunity is absent.
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TMPJ-01440 | Cutinase Protein, Thermobifida fusca, Recombinant (His) | Thermobifida fusca | E. coli | ||
Cutinase belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is cutin hydrolase. Cutinase is a serine esterase containing the classical Ser, His, Asp triad of serine hydrolases. The protein belongs to the alpha-beta class, with a central beta-sheet of 5 parallel strands covered by 5 helices on either side of the sheet. Cutin monomers released from the cuticle by small amounts of cutinase on fungal spore surfaces can greatly increase the amount of cutinase secreted by the spore. The active site cleft is partly covered by 2 thin bridges formed by amino acid side chains, by contrast with the hydrophobic lid possessed by other lipases. The protein also contains 2 disulfide bridges, which are essential for activity, their cleavage resulting in complete loss of enzymatic activity.
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TMPY-05305 | alanyl-tRNA synthetase Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
Alanyl-tRNA synthetase (AARS) belongs to the family of ligases, specifically those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. This enzyme participates in alanine and aspartate metabolism and aminoacyl-tRNA biosynthesis. Alanyl-tRNA synthetase (AlaRS) catalyzes synthesis of Ala-tRNA (Ala) and hydrolysis of mis-acylated Ser- and Gly-tRNA (Ala) at 2 different catalytic sites. Their role is not confined to catalyze the attachment of amino acids to transfer RNAs and thereby establish the rules of genetic code by virtue of matching the nucleotide triplet of anticodon with cognate amino acid. Under apoptotic conditions in cell culture, the full-length enzyme is secreted, and the two cytokine activities can be generated by leukocyte elastase, an extracellular protease. Secretion of this tRNA synthetase may contribute to apoptosis both by arresting translation and producing needed cytokines. This protein could be an attractive target of drugs against bacterial, fungal and parasitic infections.
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TMPY-05119 | IL-17RA Protein, Human, Recombinant (His & hFc), Biotinylated | Human | HEK293 | ||
Interleukin-17 receptor (IL-17R), also known as Interleukin-17 receptor A (IL-17RA) and CD217 antigen (CD217), is a cytokine receptor that binds interleukin 17. IL-17R/IL-17RA (CD217) is a proinflammatory cytokine secreted by activated T-lymphocytes. It is a potent inducer of the maturation of CD34-positive hematopoietic precursors into neutrophils. IL-17R/IL-17RA (CD217) is a ubiquitous type I membrane glycoprotein that binds with low affinity to interleukin 17A. Interleukin 17A and its receptor IL-17RA play a pathogenic role in many inflammatory and autoimmune diseases such as rheumatoid arthritis. Like other cytokine receptors, this receptor likely has a multimeric structure. Defects in IL-17R/IL-17RA (CD217) are the cause of familial candidiasis type 5 (CANDF5). CANDF5 is a rare disorder with altered immune responses and impaired clearance of fungal infections, selective against Candida. It is characterized by persistent and/or recurrent infections of the skin, nails, and mucous membranes caused by organisms of the genus Candida, mainly Candida albicans.
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TMPY-02996 | IL-17RA Protein, Rat, Recombinant (His) | Rat | HEK293 | ||
Interleukin-17 receptor (IL-17R), also known as Interleukin-17 receptor A (IL-17RA) and CD217 antigen (CD217), is a cytokine receptor that binds interleukin 17. IL-17R/IL-17RA (CD217) is a proinflammatory cytokine secreted by activated T-lymphocytes. It is a potent inducer of the maturation of CD34-positive hematopoietic precursors into neutrophils. IL-17R/IL-17RA (CD217) is a ubiquitous type I membrane glycoprotein that binds with low affinity to interleukin 17A. Interleukin 17A and its receptor IL-17RA play a pathogenic role in many inflammatory and autoimmune diseases such as rheumatoid arthritis. Like other cytokine receptors, this receptor likely has a multimeric structure. Defects in IL-17R/IL-17RA (CD217) are the cause of familial candidiasis type 5 (CANDF5). CANDF5 is a rare disorder with altered immune responses and impaired clearance of fungal infections, selective against Candida. It is characterized by persistent and/or recurrent infections of the skin, nails, and mucous membranes caused by organisms of the genus Candida, mainly Candida albicans.
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TMPY-03557 | IL-17RA Protein, Mouse, Recombinant (hFc) | Mouse | HEK293 | ||
Interleukin-17 receptor (IL-17R), also known as Interleukin-17 receptor A (IL-17RA) and CD217 antigen (CD217), is a cytokine receptor that binds interleukin 17. IL-17R/IL-17RA (CD217) is a proinflammatory cytokine secreted by activated T-lymphocytes. It is a potent inducer of the maturation of CD34-positive hematopoietic precursors into neutrophils. IL-17R/IL-17RA (CD217) is a ubiquitous type I membrane glycoprotein that binds with low affinity to interleukin 17A. Interleukin 17A and its receptor IL-17RA play a pathogenic role in many inflammatory and autoimmune diseases such as rheumatoid arthritis. Like other cytokine receptors, this receptor likely has a multimeric structure. Defects in IL-17R/IL-17RA (CD217) are the cause of familial candidiasis type 5 (CANDF5). CANDF5 is a rare disorder with altered immune responses and impaired clearance of fungal infections, selective against Candida. It is characterized by persistent and/or recurrent infections of the skin, nails, and mucous membranes caused by organisms of the genus Candida, mainly Candida albicans.
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TMPY-02441 | alanyl-tRNA synthetase Protein, Mouse, Recombinant (His) | Mouse | Baculovirus-Insect Cells | ||
Alanyl-tRNA synthetase (AARS) belongs to the family of ligases, specifically those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. This enzyme participates in alanine and aspartate metabolism and aminoacyl-tRNA biosynthesis. Alanyl-tRNA synthetase (AlaRS) catalyzes synthesis of Ala-tRNA (Ala) and hydrolysis of mis-acylated Ser- and Gly-tRNA (Ala) at 2 different catalytic sites. Their role is not confined to catalyze the attachment of amino acids to transfer RNAs and thereby establish the rules of genetic code by virtue of matching the nucleotide triplet of anticodon with cognate amino acid. Under apoptotic conditions in cell culture, the full-length enzyme is secreted, and the two cytokine activities can be generated by leukocyte elastase, an extracellular protease. Secretion of this tRNA synthetase may contribute to apoptosis both by arresting translation and producing needed cytokines. This protein could be an attractive target of drugs against bacterial, fungal and parasitic infections.
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TMPY-01849 | IL-17RA Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Interleukin-17 receptor (IL-17R), also known as Interleukin-17 receptor A (IL-17RA) and CD217 antigen (CD217), is a cytokine receptor that binds interleukin 17. IL-17R/IL-17RA (CD217) is a proinflammatory cytokine secreted by activated T-lymphocytes. It is a potent inducer of the maturation of CD34-positive hematopoietic precursors into neutrophils. IL-17R/IL-17RA (CD217) is a ubiquitous type I membrane glycoprotein that binds with low affinity to interleukin 17A. Interleukin 17A and its receptor IL-17RA play a pathogenic role in many inflammatory and autoimmune diseases such as rheumatoid arthritis. Like other cytokine receptors, this receptor likely has a multimeric structure. Defects in IL-17R/IL-17RA (CD217) are the cause of familial candidiasis type 5 (CANDF5). CANDF5 is a rare disorder with altered immune responses and impaired clearance of fungal infections, selective against Candida. It is characterized by persistent and/or recurrent infections of the skin, nails, and mucous membranes caused by organisms of the genus Candida, mainly Candida albicans.
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TMPY-03214 | IL-17RA Protein, Rhesus, Recombinant (hFc) | Rhesus | HEK293 | ||
Interleukin-17 receptor (IL-17R), also known as Interleukin-17 receptor A (IL-17RA) and CD217 antigen (CD217), is a cytokine receptor that binds interleukin 17. IL-17R/IL-17RA (CD217) is a proinflammatory cytokine secreted by activated T-lymphocytes. It is a potent inducer of the maturation of CD34-positive hematopoietic precursors into neutrophils. IL-17R/IL-17RA (CD217) is a ubiquitous type I membrane glycoprotein that binds with low affinity to interleukin 17A. Interleukin 17A and its receptor IL-17RA play a pathogenic role in many inflammatory and autoimmune diseases such as rheumatoid arthritis. Like other cytokine receptors, this receptor likely has a multimeric structure. Defects in IL-17R/IL-17RA (CD217) are the cause of familial candidiasis type 5 (CANDF5). CANDF5 is a rare disorder with altered immune responses and impaired clearance of fungal infections, selective against Candida. It is characterized by persistent and/or recurrent infections of the skin, nails, and mucous membranes caused by organisms of the genus Candida, mainly Candida albicans.
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TMPY-03910 | IL-17RA Protein, Rat, Recombinant (hFc) | Rat | HEK293 | ||
Interleukin-17 receptor (IL-17R), also known as Interleukin-17 receptor A (IL-17RA) and CD217 antigen (CD217), is a cytokine receptor that binds interleukin 17. IL-17R/IL-17RA (CD217) is a proinflammatory cytokine secreted by activated T-lymphocytes. It is a potent inducer of the maturation of CD34-positive hematopoietic precursors into neutrophils. IL-17R/IL-17RA (CD217) is a ubiquitous type I membrane glycoprotein that binds with low affinity to interleukin 17A. Interleukin 17A and its receptor IL-17RA play a pathogenic role in many inflammatory and autoimmune diseases such as rheumatoid arthritis. Like other cytokine receptors, this receptor likely has a multimeric structure. Defects in IL-17R/IL-17RA (CD217) are the cause of familial candidiasis type 5 (CANDF5). CANDF5 is a rare disorder with altered immune responses and impaired clearance of fungal infections, selective against Candida. It is characterized by persistent and/or recurrent infections of the skin, nails, and mucous membranes caused by organisms of the genus Candida, mainly Candida albicans.
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TMPY-04842 | IL-17RA Protein, Rhesus, Recombinant (His) | Rhesus | HEK293 | ||
Interleukin-17 receptor (IL-17R), also known as Interleukin-17 receptor A (IL-17RA) and CD217 antigen (CD217), is a cytokine receptor that binds interleukin 17. IL-17R/IL-17RA (CD217) is a proinflammatory cytokine secreted by activated T-lymphocytes. It is a potent inducer of the maturation of CD34-positive hematopoietic precursors into neutrophils. IL-17R/IL-17RA (CD217) is a ubiquitous type I membrane glycoprotein that binds with low affinity to interleukin 17A. Interleukin 17A and its receptor IL-17RA play a pathogenic role in many inflammatory and autoimmune diseases such as rheumatoid arthritis. Like other cytokine receptors, this receptor likely has a multimeric structure. Defects in IL-17R/IL-17RA (CD217) are the cause of familial candidiasis type 5 (CANDF5). CANDF5 is a rare disorder with altered immune responses and impaired clearance of fungal infections, selective against Candida. It is characterized by persistent and/or recurrent infections of the skin, nails, and mucous membranes caused by organisms of the genus Candida, mainly Candida albicans.
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TMPY-06391 | IL-17RA Protein, Human, Recombinant (aa 1-320, His & Avi),Biotinylated | Human | HEK293 | ||
Interleukin-17 receptor (IL-17R), also known as Interleukin-17 receptor A (IL-17RA) and CD217 antigen (CD217), is a cytokine receptor that binds interleukin 17. IL-17R/IL-17RA (CD217) is a proinflammatory cytokine secreted by activated T-lymphocytes. It is a potent inducer of the maturation of CD34-positive hematopoietic precursors into neutrophils. IL-17R/IL-17RA (CD217) is a ubiquitous type I membrane glycoprotein that binds with low affinity to interleukin 17A. Interleukin 17A and its receptor IL-17RA play a pathogenic role in many inflammatory and autoimmune diseases such as rheumatoid arthritis. Like other cytokine receptors, this receptor likely has a multimeric structure. Defects in IL-17R/IL-17RA (CD217) are the cause of familial candidiasis type 5 (CANDF5). CANDF5 is a rare disorder with altered immune responses and impaired clearance of fungal infections, selective against Candida. It is characterized by persistent and/or recurrent infections of the skin, nails, and mucous membranes caused by organisms of the genus Candida, mainly Candida albicans.
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TMPY-05120 | IL-17RA Protein, Human, Recombinant (His), Biotinylated | Human | HEK293 | ||
Interleukin-17 receptor (IL-17R), also known as Interleukin-17 receptor A (IL-17RA) and CD217 antigen (CD217), is a cytokine receptor that binds interleukin 17. IL-17R/IL-17RA (CD217) is a proinflammatory cytokine secreted by activated T-lymphocytes. It is a potent inducer of the maturation of CD34-positive hematopoietic precursors into neutrophils. IL-17R/IL-17RA (CD217) is a ubiquitous type I membrane glycoprotein that binds with low affinity to interleukin 17A. Interleukin 17A and its receptor IL-17RA play a pathogenic role in many inflammatory and autoimmune diseases such as rheumatoid arthritis. Like other cytokine receptors, this receptor likely has a multimeric structure. Defects in IL-17R/IL-17RA (CD217) are the cause of familial candidiasis type 5 (CANDF5). CANDF5 is a rare disorder with altered immune responses and impaired clearance of fungal infections, selective against Candida. It is characterized by persistent and/or recurrent infections of the skin, nails, and mucous membranes caused by organisms of the genus Candida, mainly Candida albicans.
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TMPY-06390 | IL-17RA Protein, Human, Recombinant (hFc & Avi), Biotinylated | Human | HEK293 | ||
Interleukin-17 receptor (IL-17R), also known as Interleukin-17 receptor A (IL-17RA) and CD217 antigen (CD217), is a cytokine receptor that binds interleukin 17. IL-17R/IL-17RA (CD217) is a proinflammatory cytokine secreted by activated T-lymphocytes. It is a potent inducer of the maturation of CD34-positive hematopoietic precursors into neutrophils. IL-17R/IL-17RA (CD217) is a ubiquitous type I membrane glycoprotein that binds with low affinity to interleukin 17A. Interleukin 17A and its receptor IL-17RA play a pathogenic role in many inflammatory and autoimmune diseases such as rheumatoid arthritis. Like other cytokine receptors, this receptor likely has a multimeric structure. Defects in IL-17R/IL-17RA (CD217) are the cause of familial candidiasis type 5 (CANDF5). CANDF5 is a rare disorder with altered immune responses and impaired clearance of fungal infections, selective against Candida. It is characterized by persistent and/or recurrent infections of the skin, nails, and mucous membranes caused by organisms of the genus Candida, mainly Candida albicans.
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TMPY-05430 | IL-17RA Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
Interleukin-17 receptor (IL-17R), also known as Interleukin-17 receptor A (IL-17RA) and CD217 antigen (CD217), is a cytokine receptor that binds interleukin 17. IL-17R/IL-17RA (CD217) is a proinflammatory cytokine secreted by activated T-lymphocytes. It is a potent inducer of the maturation of CD34-positive hematopoietic precursors into neutrophils. IL-17R/IL-17RA (CD217) is a ubiquitous type I membrane glycoprotein that binds with low affinity to interleukin 17A. Interleukin 17A and its receptor IL-17RA play a pathogenic role in many inflammatory and autoimmune diseases such as rheumatoid arthritis. Like other cytokine receptors, this receptor likely has a multimeric structure. Defects in IL-17R/IL-17RA (CD217) are the cause of familial candidiasis type 5 (CANDF5). CANDF5 is a rare disorder with altered immune responses and impaired clearance of fungal infections, selective against Candida. It is characterized by persistent and/or recurrent infections of the skin, nails, and mucous membranes caused by organisms of the genus Candida, mainly Candida albicans.
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TMPY-04714 | DC-SIGN Protein, Rhesus, Recombinant (hFc) | Rhesus | HEK293 | ||
Dendritic cell (DC)-specific intercellular adhesion molecule 3 (ICAM-3) grabbing nonintegrin (DC-SIGN), also known as CD209, is a type II transmembrane protein on DCs with a C-type lectin extracellular domain, is capable of binding ICAM-3 on resting T cells in the secondary lymphoid organs, providing the initial contact between these cells during the establishment of cell-mediated immunity. It is not only a pattern recognition receptor but implicated in immunoregulation of DCs. It has an important role in mediating DC adhesion, migration, inflammation, activating primary T cell, triggering immune response and participating in immune escape of pathogens and tumors. DC-SIGN also mediates the capture and internalization of viral, bacterial, and fungal pathogens by dendritic cells, such as HIV-1, Ebola virus, cytomegalovirus, Dengue virus, and hepatitis C virus. DC-SIGN is unique in that it regulates adhesion processes, such as DC trafficking and T-cell synapse formation, as well as antigen capture. Moreover, even though several C-type lectins have been shown to bind HIV-1, DC-SIGN does not only capture HIV-1 but also protects it in early endosomes allowing HIV-1 transport by DC to lymphoid tissues, where it enhances trans infection of T cells.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-04715 | DC-SIGN Protein, Rhesus, Recombinant (His) | Rhesus | HEK293 | ||
Dendritic cell (DC)-specific intercellular adhesion molecule 3 (ICAM-3) grabbing nonintegrin (DC-SIGN), also known as CD209, is a type II transmembrane protein on DCs with a C-type lectin extracellular domain, is capable of binding ICAM-3 on resting T cells in the secondary lymphoid organs, providing the initial contact between these cells during the establishment of cell-mediated immunity. It is not only a pattern recognition receptor but implicated in immunoregulation of DCs. It has an important role in mediating DC adhesion, migration, inflammation, activating primary T cell, triggering immune response and participating in immune escape of pathogens and tumors. DC-SIGN also mediates the capture and internalization of viral, bacterial, and fungal pathogens by dendritic cells, such as HIV-1, Ebola virus, cytomegalovirus, Dengue virus, and hepatitis C virus. DC-SIGN is unique in that it regulates adhesion processes, such as DC trafficking and T-cell synapse formation, as well as antigen capture. Moreover, even though several C-type lectins have been shown to bind HIV-1, DC-SIGN does not only capture HIV-1 but also protects it in early endosomes allowing HIV-1 transport by DC to lymphoid tissues, where it enhances trans infection of T cells.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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